GPCRdb

Ligand source activities (1 row/activity)

Potency
Affinity

Get vendors

Ligands					Receptor			Assay information							Chemical information
Sel. page	Common name	GPCRdb ID	#Vendors	Reference ligand	Fold selectivity (Potency)	# tested GPCRs (Potency)	Species	p-value (-log)	Type	Activity Relation	Activity Value	Assay Type	Assay Description	Source	Mol weight	Rot Bonds	H don	H acc	LogP	Smiles	DOI
	10353365	90022	1	None	13	3	Human	10.1	pEC50	=	10.1	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	90022	1	None	13	3	Human	10.1	pEC50	=	10.1	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	117972056	148911	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	5	0	4	5.2	Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3883435	148911	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	5	0	4	5.2	Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1	10.1016/j.bmc.2016.11.018
	117971665	149004	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	415	5	0	4	5.8	FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884532	149004	0	None	-	1	Human	9.4	pEC50	=	9.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	415	5	0	4	5.8	FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	117971685	148991	0	None	-	1	Human	9.3	pEC50	=	9.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	387	5	0	4	5.0	FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884187	148991	0	None	-	1	Human	9.3	pEC50	=	9.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	387	5	0	4	5.0	FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	1395	9306	15	None	-7	4	Rat	9.2	pEC50	=	9.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	9306	15	None	-7	4	Rat	9.2	pEC50	=	9.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	9306	15	None	-7	4	Rat	9.2	pEC50	=	9.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	1395	9306	15	None	3	4	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	9837317	9306	15	None	3	4	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL121053	9306	15	None	3	4	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	71131322	130184	0	None	43	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616857	130184	0	None	43	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	90098428	130183	0	None	60	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616856	130183	0	None	60	2	Human	9.2	pEC50	=	9.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	68109941	162901	0	None	-	1	Human	9.0	pEC50	=	9.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	162901	0	None	-	1	Human	9.0	pEC50	=	9.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	1395	9306	15	None	-7	4	Rat	8.9	pEC50	=	8.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	9306	15	None	-7	4	Rat	8.9	pEC50	=	8.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	9306	15	None	-7	4	Rat	8.9	pEC50	=	8.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	123289788	149015	0	None	-	1	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884636	149015	0	None	-	1	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	117972250	149090	3	None	32	2	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885379	149090	3	None	32	2	Human	8.9	pEC50	=	8.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	134130172	148937	0	None	-	1	Human	8.8	pEC50	=	8.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3883634	148937	0	None	-	1	Human	8.8	pEC50	=	8.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1	10.1016/j.bmc.2016.11.018
	117968349	148978	0	None	-	1	Human	8.7	pEC50	=	8.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	429	6	0	4	6.0	FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884094	148978	0	None	-	1	Human	8.7	pEC50	=	8.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	429	6	0	4	6.0	FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	1393	8321	64	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	1396	8321	64	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	213056	8321	64	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	CHEMBL8759	8321	64	None	2	6	Human	8.0	pEC50	=	8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	117968551	149001	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	393	6	0	4	5.0	CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884343	149001	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	393	6	0	4	5.0	CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	146036859	181326	5	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	293	2	0	3	3.8	Brc1cccc2c1nnn2CC1CCCCC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4556144	181326	5	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	293	2	0	3	3.8	Brc1cccc2c1nnn2CC1CCCCC1	10.1021/acs.jmedchem.8b00161
	68108471	89423	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	436	4	0	4	5.4	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/jm3010724
	CHEMBL2179326	89423	0	None	-	1	Human	8.0	pEC50	=	8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	436	4	0	4	5.4	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/jm3010724
	156020355	184807	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	184807	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	67060140	174176	0	None	26	2	Rat	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4295230	174176	0	None	26	2	Rat	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	71135411	130175	0	None	5	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616848	130175	0	None	5	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	57459497	90676	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	442	4	0	5	5.0	COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206439	90676	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	442	4	0	5	5.0	COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1	10.1021/jm300912k
	44361501	126082	0	None	-	1	Rat	7.0	pEC50	=	7	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O	10.1021/jm030967o
	CHEMBL343994	126082	0	None	-	1	Rat	7.0	pEC50	=	7	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O	10.1021/jm030967o
	70683631	81363	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	384	6	0	4	5.4	CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029795	81363	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	384	6	0	4	5.4	CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	70689929	81383	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	387	6	0	5	5.2	Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	CHEMBL2029813	81383	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	387	6	0	5	5.2	Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	70689930	81387	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029817	81387	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	66785101	164824	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4085882	164824	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	71136186	158848	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	CHEMBL3967432	158848	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	151031	165072	8	None	-	1	Rat	4.0	pEC50	=	4	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	NC(C(=O)O)C1CC(O)=NO1	10.1021/jm701394a
	59951973	165072	8	None	-	1	Rat	4.0	pEC50	=	4	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	NC(C(=O)O)C1CC(O)=NO1	10.1021/jm701394a
	CHEMBL408899	165072	8	None	-	1	Rat	4.0	pEC50	=	4	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	NC(C(=O)O)C1CC(O)=NO1	10.1021/jm701394a
	168298834	199472	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5219313	199472	0	None	-	1	Human	7.0	pEC50	=	7	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	11951272	74004	0	None	-	1	Human	6.0	pEC50	=	6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	12	1	6	6.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL187939	74004	0	None	-	1	Human	6.0	pEC50	=	6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	12	1	6	6.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	59234239	121337	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337502	121337	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	57459640	89412	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	366	4	0	4	4.7	Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179314	89412	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	366	4	0	4	4.7	Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	11545979	172575	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL424795	172575	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	44595851	10574	4	None	-3	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	6259	10574	4	None	-3	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	CHEMBL4092105	10574	4	None	-3	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	11950926	74033	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.4	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL188080	74033	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.4	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	155514221	176618	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	191	2	0	3	2.0	Fc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4439927	176618	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	191	2	0	3	2.0	Fc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	118714735	121335	0	None	-	1	Human	5.0	pEC50	=	5.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	309	6	0	4	3.4	CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337500	121335	0	None	-	1	Human	5.0	pEC50	=	5.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	309	6	0	4	3.4	CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	70681520	81381	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029811	81381	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1	10.1021/jm2016864
	59599475	155937	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	7	2	8	3.7	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3943547	155937	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	7	2	8	3.7	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O	10.1016/j.bmcl.2016.11.049
	46225569	208141	0	None	12	2	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL604467	208141	0	None	12	2	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1021/jm101414h
	59599577	151663	0	None	-1	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3909995	151663	0	None	-1	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	11646457	73088	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL184917	73088	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	46226934	206824	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	373	5	0	7	2.7	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL595587	206824	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	373	5	0	7	2.7	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12	10.1016/j.bmcl.2009.11.008
	69093509	90685	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	448	5	0	5	5.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	CHEMBL2206448	90685	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	448	5	0	5	5.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	117972256	148976	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl	10.1016/j.bmc.2016.11.018
	CHEMBL3884075	148976	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl	10.1016/j.bmc.2016.11.018
	117972015	149000	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	407	6	0	4	5.2	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884332	149000	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	407	6	0	4	5.2	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1	10.1016/j.bmc.2016.11.018
	68107863	199151	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5207431	199151	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	1393	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	1396	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	213056	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL8759	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	1393	8321	64	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	1396	8321	64	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	213056	8321	64	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL8759	8321	64	None	-2	6	Rat	8.0	pEC50	=	8.0	Functional	Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	1393	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	1396	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	213056	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL8759	8321	64	None	2	6	Human	8.0	pEC50	=	8.0	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	71136653	130181	0	None	51	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616854	130181	0	None	51	2	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	156013901	184017	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	184017	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	71137034	130177	0	None	7	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616850	130177	0	None	7	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	71454787	87584	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	428	4	0	4	6.0	N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152118	87584	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	428	4	0	4	6.0	N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	70685763	81362	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	370	7	0	4	4.9	CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029794	81362	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	370	7	0	4	4.9	CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	51357934	68749	0	None	-	1	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	CHEMBL1774227	68749	0	None	-	1	Rat	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	9815617	121277	7	None	-1	2	Rat	6.0	pEC50	=	6.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	121277	7	None	-1	2	Rat	6.0	pEC50	=	6.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	57459485	89410	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	6	3.6	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12	10.1021/jm3010724
	CHEMBL2179312	89410	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	6	3.6	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12	10.1021/jm3010724
	11951989	74802	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	11	1	6	5.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL191391	74802	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	11	1	6	5.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C	10.1016/j.bmcl.2005.06.017
	70685761	81356	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029787	81356	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	49822037	89414	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	412	3	0	4	5.0	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179316	89414	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	412	3	0	4	5.0	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	57459500	89417	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	374	3	0	4	4.7	CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179320	89417	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	374	3	0	4	4.7	CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	71117470	152460	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	498	5	1	6	4.7	Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1	nan
	CHEMBL3916091	152460	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	498	5	1	6	4.7	Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1	nan
	25173448	191041	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL483754	191041	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	71681826	96836	0	None	-1	3	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381651	96836	0	None	-1	3	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	44155423	15471	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095750	15471	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	24809653	81358	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	314	5	0	4	3.6	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F	10.1021/jm2016864
	CHEMBL2029790	81358	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	314	5	0	4	3.6	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F	10.1021/jm2016864
	11950744	133586	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	6	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL365440	133586	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	6	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71117232	160670	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	398	7	1	7	2.3	Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	nan
	CHEMBL3983091	160670	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	398	7	1	7	2.3	Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	nan
	155523303	177614	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4453680	177614	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	46887460	15618	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097044	15618	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	90643858	118643	0	None	25	2	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287695	118643	0	None	25	2	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	156013901	184017	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	184017	0	None	114	2	Human	7.9	pEC50	=	7.9	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	68109335	163890	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074664	163890	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	71136640	130180	0	None	60	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616853	130180	0	None	60	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	46215878	87583	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	388	2	0	4	5.1	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21	10.1021/jm201561r
	CHEMBL2152117	87583	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	388	2	0	4	5.1	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21	10.1021/jm201561r
	156012835	184213	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	184213	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156016100	184466	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	184466	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	46887271	15462	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	275	8	0	2	4.8	CCCCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095701	15462	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	275	8	0	2	4.8	CCCCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	156016100	184466	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	184466	0	None	-1	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	162669954	189448	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	353	6	0	4	4.0	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4789052	189448	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	353	6	0	4	4.0	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	44155986	15320	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094462	15320	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	71117222	152863	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3919237	152863	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	57459655	89408	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	359	2	0	5	4.3	CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179310	89408	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	359	2	0	5	4.3	CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	68107697	89422	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	4	4.7	FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179325	89422	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	4	0	4	4.7	FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	156012835	184213	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	184213	0	None	-2	2	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	58103861	89429	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	4.7	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm3010724
	CHEMBL2179332	89429	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	4.7	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm3010724
	90668093	116315	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221832	116315	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O	10.1039/C0MD00200C
	53322147	64498	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669380	64498	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53325451	64517	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	404	6	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669398	64517	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	404	6	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46190878	8653	7	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	6253	8653	7	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	CHEMBL595759	8653	7	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	155548817	180619	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	90668101	116326	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	384	7	1	4	5.8	CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221842	116326	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	384	7	1	4	5.8	CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O	10.1039/C0MD00200C
	1310	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	1369	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	33032	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	44272391	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	88747398	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	CHEMBL575060	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	DB00142	9095	110	None	-389	17	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2010.12.048
	70694131	81376	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.7	Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	CHEMBL2029806	81376	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.7	Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	71137012	130178	0	None	11	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616851	130178	0	None	11	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	117971683	149084	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885312	149084	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	134131394	149092	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885396	149092	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155536450	178958	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	406	3	0	4	5.4	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4473537	178958	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	406	3	0	4	5.4	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	25008958	68738	1	None	-	1	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	404	4	0	5	4.4	COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1	10.1021/jm101414h
	CHEMBL1774112	68738	1	None	-	1	Rat	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	404	4	0	5	4.4	COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1	10.1021/jm101414h
	50992248	173321	0	None	1	2	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	CHEMBL4279401	173321	0	None	1	2	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	71137010	130176	0	None	5	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616849	130176	0	None	5	2	Human	7.9	pEC50	=	7.9	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	162651557	186964	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	319	6	0	3	4.3	c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4749289	186964	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	319	6	0	3	4.3	c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	24815439	208714	1	None	-18	2	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.ejmech.2019.111881
	CHEMBL607689	208714	1	None	-18	2	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.ejmech.2019.111881
	46887273	15464	5	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	219	4	0	2	3.2	CCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095703	15464	5	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	219	4	0	2	3.2	CCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	6604704	108177	35	None	2	3	Human	4.9	pEC50	=	4.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970207b
	CHEMBL29726	108177	35	None	2	3	Human	4.9	pEC50	=	4.9	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970207b
	1310	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	9095	110	None	-457	17	Rat	4.9	pEC50	=	4.9	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44397878	131179	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	389	6	1	5	5.6	CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL363945	131179	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	389	6	1	5	5.6	CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71116730	155841	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	CHEMBL3942904	155841	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	44155989	15319	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094461	15319	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	305	7	0	4	3.8	CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	25073615	173243	0	None	-4	2	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	CHEMBL4278070	173243	0	None	-4	2	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	11951270	74100	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.3	CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL188455	74100	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	9	1	6	5.3	CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	156817945	197263	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5179002	197263	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	162676513	190292	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	4	0	3	3.5	c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4799794	190292	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	4	0	3	3.5	c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	70689928	81382	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	5.0	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029812	81382	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	5.0	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	46887493	15356	1	None	-	1	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094762	15356	1	None	-	1	Human	4.9	pEC50	=	4.9	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	162674797	190247	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4799164	190247	0	None	-	1	Human	5.9	pEC50	=	5.9	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	155562956	181956	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	365	2	0	3	4.0	Brc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4570470	181956	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	365	2	0	3	4.0	Brc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	67060162	173742	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4287326	173742	0	None	-	1	Human	7.9	pEC50	=	7.9	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	71116701	151637	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	CHEMBL3909811	151637	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	146036860	180057	6	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	2	0	3	2.9	CC(C)Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4525401	180057	6	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	2	0	3	2.9	CC(C)Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	155552571	180935	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	319	2	0	3	3.6	FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4546739	180935	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	319	2	0	3	3.6	FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	118714748	121348	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337514	121348	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	155519836	177149	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4447702	177149	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1	10.1021/acs.jmedchem.8b00161
	46227787	206472	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	390	4	1	4	5.2	N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL593168	206472	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	390	4	1	4	5.2	N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	25173776	191081	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	267	3	0	2	3.7	C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484128	191081	0	None	-	1	Human	6.9	pEC50	=	6.9	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	267	3	0	2	3.7	C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	59599515	154926	0	None	-10	2	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3935529	154926	0	None	-10	2	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	24815882	68731	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774104	68731	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21	10.1021/jm101414h
	71137008	130182	0	None	7	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616855	130182	0	None	7	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	25195461	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	8946	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	CHEMBL3337527	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	DB12059	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	68109272	165397	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4092275	165397	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	70689926	81374	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	1	5	4.6	CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029804	81374	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	1	5	4.6	CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	70977933	178083	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	241	2	0	3	2.9	FC(F)(F)c1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4460927	178083	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	241	2	0	3	2.9	FC(F)(F)c1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	57459517	89420	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	372	3	0	4	4.3	FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179323	89420	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	372	3	0	4	4.3	FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	25173286	179473	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL450207	179473	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	5	0	3	4.0	CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	155534303	178723	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4470447	178723	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	155567633	182779	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4589377	182779	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	66785780	165523	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093657	165523	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	58103890	87586	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	457	4	2	4	6.1	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1	10.1021/jm201561r
	CHEMBL2152120	87586	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	457	4	2	4	6.1	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1	10.1021/jm201561r
	11531870	71087	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	420	10	1	4	5.6	CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL181089	71087	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	420	10	1	4	5.6	CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	59234231	8924	4	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	6330	8924	4	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	6331	8924	4	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	CHEMBL3337510	8924	4	None	-1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	118714757	121357	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337523	121357	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	66785393	163673	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072134	163673	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	9815616	121578	6	None	-2	4	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	CHEMBL334014	121578	6	None	-2	4	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	11530877	71652	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182166	71652	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	9815616	121578	6	None	-2	4	Rat	6.8	pEC50	=	6.8	Functional	Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	CHEMBL334014	121578	6	None	-2	4	Rat	6.8	pEC50	=	6.8	Functional	Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.ejmech.2020.112521
	156014194	183989	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	183989	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	184693	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	184693	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	7504549	178290	1	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	3	0	3	4.1	c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4464043	178290	1	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	3	0	3	4.1	c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1	10.1021/acs.jmedchem.8b00161
	71462632	89427	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	344	4	0	4	4.5	CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179330	89427	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	344	4	0	4	4.5	CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	168299101	199529	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5220917	199529	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O	10.1021/acs.jmedchem.2c00969
	44591744	195444	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL503697	195444	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	156020355	184807	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	184807	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	53321493	64516	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669397	64516	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46227786	206624	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	407	5	0	4	5.6	N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL594334	206624	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	407	5	0	4	5.6	N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	155533313	178631	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4468977	178631	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	155548817	180619	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	90668097	116321	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	7	1	3	4.5	CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221838	116321	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	7	1	3	4.5	CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	68109333	164408	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4081244	164408	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	53323491	64501	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	287	3	1	3	3.5	CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669383	64501	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	287	3	1	3	3.5	CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	24815355	68730	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774103	68730	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	51030965	173929	0	None	1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	CHEMBL4290744	173929	0	None	1	2	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	60096246	162726	0	None	-6	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	CHEMBL4061162	162726	0	None	-6	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	117972153	149080	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3885265	149080	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	405	6	0	4	5.0	Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1	10.1016/j.bmc.2016.11.018
	49822115	8927	21	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.2c00969
	8947	8927	21	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.2c00969
	CHEMBL3947764	8927	21	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.2c00969
	71136746	155379	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3939174	155379	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	71136655	130179	0	None	12	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616852	130179	0	None	12	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	9815617	121277	7	None	-1	2	Rat	7.8	pEC50	=	7.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	121277	7	None	-1	2	Rat	7.8	pEC50	=	7.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	46215704	87585	0	None	33	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	447	3	1	4	6.2	O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1	10.1021/jm201561r
	CHEMBL2152119	87585	0	None	33	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	447	3	1	4	6.2	O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1	10.1021/jm201561r
	156020355	184807	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	184807	0	None	104	2	Human	6.8	pEC50	=	6.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	156014194	183989	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	183989	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	184693	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	184693	0	None	-2	2	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	10976811	116490	0	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	214	2	3	5	-1.0	N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1	10.1021/jm0308085
	CHEMBL322887	116490	0	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	214	2	3	5	-1.0	N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1	10.1021/jm0308085
	1310	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	1369	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	33032	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	44272391	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	88747398	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	CHEMBL575060	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	DB00142	9095	110	None	-457	17	Rat	4.8	pEC50	=	4.8	Functional	Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00158-5
	11310142	9200	19	None	13	3	Human	6.8	pEC50	=	6.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	9200	19	None	13	3	Human	6.8	pEC50	=	6.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	9200	19	None	13	3	Human	6.8	pEC50	=	6.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	51357397	68732	0	None	-	1	Rat	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	330	3	0	4	3.8	Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774105	68732	0	None	-	1	Rat	5.8	pEC50	=	5.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	330	3	0	4	3.8	Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21	10.1021/jm101414h
	70696263	81385	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029815	81385	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	49822116	153770	13	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3926416	153770	13	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	168299087	199521	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	320	4	1	4	3.8	CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5220552	199521	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	320	4	1	4	3.8	CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	46216056	87577	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	358	2	1	5	3.8	N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152110	87577	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	358	2	1	5	3.8	N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	25008437	68735	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21	10.1021/jm101414h
	CHEMBL1774109	68735	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21	10.1021/jm101414h
	117972044	149061	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1	10.1016/j.bmc.2016.11.018
	CHEMBL3885097	149061	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1	10.1016/j.bmc.2016.11.018
	155566740	182664	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	2	0	3	3.9	Clc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4586335	182664	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	2	0	3	3.9	Clc1ccc(Cn2nnc3c(Br)cccc32)cc1	10.1021/acs.jmedchem.8b00161
	49765871	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	6317	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	CHEMBL2179319	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	60096236	165201	0	None	-3	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4090293	165201	0	None	-3	2	Human	7.8	pEC50	=	7.8	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	66784246	163143	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4066051	163143	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785300	163251	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	CHEMBL4067421	163251	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	59599580	159495	0	None	8	2	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3973048	159495	0	None	8	2	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	71116952	154092	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3929070	154092	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	59497100	121358	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	342	4	0	3	4.3	O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	CHEMBL3337524	121358	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	342	4	0	3	4.3	O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	162659390	187971	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.1	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	CHEMBL4761080	187971	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.1	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	1402	6910	44	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.09.028
	9825084	6910	44	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.09.028
	CHEMBL108939	6910	44	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.09.028
	10608207	125542	5	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	203	2	3	3	-0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	CHEMBL341888	125542	5	None	-	1	Rat	4.8	pEC50	=	4.8	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	203	2	3	3	-0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	11537726	73467	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185490	73467	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	25004010	81372	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	399	6	1	5	4.7	CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029802	81372	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	399	6	1	5	4.7	CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	168298053	199526	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	356	3	1	3	4.8	FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	CHEMBL5220838	199526	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	356	3	1	3	4.8	FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	44155644	15622	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccccc2C#N)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097054	15622	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccccc2C#N)C(=O)O1	10.1016/j.bmcl.2010.03.089
	1310	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	9095	110	None	-389	17	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	71117549	153622	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	437	4	0	6	1.8	CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3925103	153622	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	437	4	0	6	1.8	CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	155548817	180619	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	118714745	121345	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	5	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337511	121345	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	5	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O	10.1021/jm500496m
	57459504	89415	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	434	4	0	4	5.4	FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm3010724
	CHEMBL2179317	89415	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	434	4	0	4	5.4	FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm3010724
	134131242	149057	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	353	4	0	4	4.3	Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885072	149057	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	353	4	0	4	4.3	Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155519900	177179	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl	10.1021/acs.jmedchem.8b00161
	CHEMBL4448031	177179	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl	10.1021/acs.jmedchem.8b00161
	155565817	182400	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1cccc(Cn2nnc3c(Br)cccc32)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4580527	182400	0	None	-	1	Human	7.8	pEC50	=	7.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1cccc(Cn2nnc3c(Br)cccc32)c1	10.1021/acs.jmedchem.8b00161
	60096190	165292	0	None	-9	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091203	165292	0	None	-9	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	10353365	90022	1	None	13	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	90022	1	None	13	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	49822115	8927	21	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	8947	8927	21	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	CHEMBL3947764	8927	21	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	1393	8321	64	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	1396	8321	64	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	213056	8321	64	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	CHEMBL8759	8321	64	None	-2	6	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	66787355	163004	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	163004	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	66784572	163687	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072262	163687	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	134130477	149102	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	313	5	0	4	3.9	Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885492	149102	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	313	5	0	4	3.9	Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	162644700	186202	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	4	3.8	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4740255	186202	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	4	3.8	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	155527610	178027	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4460043	178027	0	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)nc1	10.1021/acs.jmedchem.8b00161
	44591797	191423	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484958	191423	0	None	-	1	Human	5.8	pEC50	=	5.8	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	104766	6822	42	None	-2	14	Human	4.8	pEC50	=	4.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970207b
	1365	6822	42	None	-2	14	Human	4.8	pEC50	=	4.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970207b
	CHEMBL34453	6822	42	None	-2	14	Human	4.8	pEC50	=	4.8	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970207b
	1310	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	1369	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	33032	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	44272391	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	88747398	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	CHEMBL575060	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	DB00142	9095	110	None	-457	17	Rat	4.7	pEC50	=	4.7	Functional	Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2015.04.043
	1310	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	9095	110	None	-389	17	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44591771	191019	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	351	4	0	3	4.6	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL483561	191019	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	351	4	0	3	4.6	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	162649571	186900	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	311	3	0	3	3.7	Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4748614	186900	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	311	3	0	3	3.7	Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	51356833	68747	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	400	3	0	4	4.9	Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774225	68747	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	400	3	0	4	4.9	Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21	10.1021/jm101414h
	46227797	208414	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL605921	208414	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	25004352	81364	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	400	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029796	81364	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	400	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	46227797	208414	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL605921	208414	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	393	4	0	4	5.8	N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	11655609	172680	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL424998	172680	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71476419	130187	0	None	51	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616860	130187	0	None	51	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	60096204	162903	0	None	-2	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4063336	162903	0	None	-2	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11220424	165740	0	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095995	165740	0	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71456562	87579	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	394	4	0	4	5.3	N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152113	87579	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	394	4	0	4	5.3	N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	155519573	180047	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4525207	180047	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	44155748	15276	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2cccc(O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094124	15276	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2cccc(O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	118263352	121360	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	4	0	3	4.5	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O	10.1021/jm500496m
	CHEMBL3337526	121360	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	344	4	0	3	4.5	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O	10.1021/jm500496m
	25009651	68736	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21	10.1021/jm101414h
	CHEMBL1774110	68736	0	None	-	1	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21	10.1021/jm101414h
	11559813	71782	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	374	10	1	4	5.3	Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182316	71782	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	374	10	1	4	5.3	Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	90668095	116318	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	6	1	3	4.4	CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221835	116318	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	320	6	1	3	4.4	CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O	10.1039/C0MD00200C
	90668102	116327	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	376	6	1	4	4.9	CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221843	116327	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	376	6	1	4	4.9	CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O	10.1039/C0MD00200C
	46917716	116328	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	1	3	4.7	CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221844	116328	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	1	3	4.7	CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O	10.1039/C0MD00200C
	53326710	64515	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	389	5	0	3	6.5	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669396	64515	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	389	5	0	3	6.5	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46190877	8652	7	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	6252	8652	7	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	CHEMBL605836	8652	7	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	24815976	206538	0	None	-5	2	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593745	206538	0	None	-5	2	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225336	206827	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595609	206827	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	90668098	116322	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	292	5	1	3	4.0	CCCn1ccc2c(NCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221839	116322	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	292	5	1	3	4.0	CCCn1ccc2c(NCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	10197984	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	1394	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL275079	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1016/j.bmcl.2012.01.039
	10197984	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	10197984	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	1394	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL275079	9199	44	None	1	5	Human	8.6	pEC50	=	8.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	66786902	166240	0	None	-	1	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4101354	166240	0	None	-	1	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	71457756	90677	0	None	66	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206440	90677	0	None	66	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	134130276	149082	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885277	149082	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155536501	178973	1	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	265	2	0	3	3.0	Brc1cccc2c1nnn2CC1CCC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4473685	178973	1	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	265	2	0	3	3.0	Brc1cccc2c1nnn2CC1CCC1	10.1021/acs.jmedchem.8b00161
	68108457	155335	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3938796	155335	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5074658	221102	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1	10.1021/acs.jmedchem.1c00563
	71137011	130185	0	None	58	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616858	130185	0	None	58	2	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	53240406	130174	17	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	50992248	173321	0	None	-1	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	CHEMBL4279401	173321	0	None	-1	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	376	5	0	5	3.9	CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2	10.1016/j.bmcl.2018.08.022
	1392	6861	48	None	5	4	Rat	6.7	pEC50	=	6.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	5310984	6861	48	None	5	4	Rat	6.7	pEC50	=	6.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	CHEMBL40086	6861	48	None	5	4	Rat	6.7	pEC50	=	6.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	104766	6822	42	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm0308085
	1365	6822	42	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm0308085
	CHEMBL34453	6822	42	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm0308085
	11596869	150415	0	None	-8	2	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	417	7	2	8	3.9	CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3899832	150415	0	None	-8	2	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	417	7	2	8	3.9	CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	25173287	177153	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	6	0	3	4.4	CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL444778	177153	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	6	0	3	4.4	CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	24809687	81373	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	351	5	0	5	3.3	CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029803	81373	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	351	5	0	5	3.3	CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	156817927	198385	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	433	5	0	5	4.2	Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5195400	198385	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	433	5	0	5	4.2	Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	44363330	43247	0	None	-	1	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL144747	43247	0	None	-	1	Rat	7.7	pEC50	=	7.7	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	53240406	130174	17	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	11275666	96832	1	None	1	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381647	96832	1	None	1	3	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	156018305	184613	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	184613	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	155539343	179608	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4514174	179608	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	366	2	0	4	3.4	Brc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	104766	6822	42	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	1365	6822	42	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	CHEMBL34453	6822	42	None	2	14	Rat	5.7	pEC50	=	5.7	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(99)00266-8
	24815434	206475	0	None	5	2	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL593196	206475	0	None	5	2	Rat	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1021/jm101414h
	156018305	184613	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	184613	0	None	89	2	Human	6.7	pEC50	=	6.7	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	42610167	87576	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	420	3	0	5	4.5	N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152109	87576	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	420	3	0	5	4.5	N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	71117258	153327	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	467	6	1	8	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21	nan
	CHEMBL3922773	153327	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	467	6	1	8	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21	nan
	46887416	15315	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094416	15315	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	51357936	68751	0	None	3	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	CHEMBL1774231	68751	0	None	3	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	24815439	208714	1	None	18	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL607689	208714	1	None	18	2	Rat	7.7	pEC50	=	7.7	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1021/jm101414h
	53240406	130174	17	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	107	4	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	25173773	191703	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL485336	191703	0	None	-	1	Human	7.7	pEC50	=	7.7	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	71117730	150709	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	CHEMBL3902193	150709	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	66784890	162829	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4062535	162829	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	68109425	165069	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4088960	165069	0	None	-	1	Human	6.7	pEC50	=	6.7	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	155560108	181688	2	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	225	1	0	3	2.2	CCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4564533	181688	2	None	-	1	Human	5.7	pEC50	=	5.7	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	225	1	0	3	2.2	CCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	11950745	130422	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	497	9	1	6	5.9	CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	CHEMBL361934	130422	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	497	9	1	6	5.9	CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	59599555	160327	0	None	1	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3980125	160327	0	None	1	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	11951806	73579	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	487	12	1	6	6.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1	10.1016/j.bmcl.2005.06.017
	CHEMBL186018	73579	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	487	12	1	6	6.6	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1	10.1016/j.bmcl.2005.06.017
	162654261	187433	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	6	0	4	3.9	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4755053	187433	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	6	0	4	3.9	COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	9979770	73112	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185054	73112	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	46227789	206496	1	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	361	3	0	7	2.5	CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	CHEMBL593399	206496	1	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	361	3	0	7	2.5	CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	155531064	178417	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4465783	178417	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	339	2	0	3	4.0	Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	9834591	144378	69	None	2	3	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL375611	144378	69	None	2	3	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	46215709	87578	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	354	2	0	4	4.5	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21	10.1021/jm201561r
	CHEMBL2152112	87578	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	354	2	0	4	4.5	Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21	10.1021/jm201561r
	156013901	184017	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	184017	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	70685768	81388	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	5	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	CHEMBL2029818	81388	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	5	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	134130478	149103	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	364	5	0	5	4.5	Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885493	149103	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	364	5	0	5	4.5	Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	44300122	19901	0	None	-	1	Rat	5.6	pEC50	=	5.6	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	279	4	4	5	-0.3	Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1	10.1016/s0960-894x(01)00329-8
	CHEMBL1190517	19901	0	None	-	1	Rat	5.6	pEC50	=	5.6	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	279	4	4	5	-0.3	Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1	10.1016/s0960-894x(01)00329-8
	CHEMBL541050	19901	0	None	-	1	Rat	5.6	pEC50	=	5.6	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	279	4	4	5	-0.3	Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1	10.1016/s0960-894x(01)00329-8
	156013901	184017	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635729	184017	0	None	114	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	42610166	208448	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	5.0	N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL606153	208448	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	384	3	0	4	5.0	N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	1310	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	68107863	199151	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5207431	199151	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1	10.1021/acs.jmedchem.2c00593
	25173617	195435	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	4	0	3	3.7	CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL503572	195435	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	4	0	3	3.7	CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	57459501	89418	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	402	5	0	4	5.5	CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179321	89418	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	402	5	0	4	5.5	CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	46887372	15576	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096713	15576	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	162669368	189547	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	330	5	0	4	3.7	N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4790241	189547	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	330	5	0	4	3.7	N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44300605	20127	0	None	-3	3	Rat	4.6	pEC50	=	4.6	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1192345	20127	0	None	-3	3	Rat	4.6	pEC50	=	4.6	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL543568	20127	0	None	-3	3	Rat	4.6	pEC50	=	4.6	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1	10.1016/s0960-894x(01)00329-8
	71136654	130186	0	None	3	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616859	130186	0	None	3	2	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	162659966	188030	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	3	0	3	3.4	Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4761771	188030	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	291	3	0	3	3.4	Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	156014680	184029	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	184029	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	51357400	68745	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	408	4	0	5	4.4	Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774222	68745	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	408	4	0	5	4.4	Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	51357399	68744	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	392	3	0	4	4.5	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774221	68744	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	392	3	0	4	4.5	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21	10.1021/jm101414h
	68108857	164117	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4077609	164117	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	71458417	87588	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	437	4	0	3	6.8	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12	10.1021/jm201561r
	CHEMBL2152122	87588	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	437	4	0	3	6.8	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12	10.1021/jm201561r
	44155645	15468	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095745	15468	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	51030965	173929	0	None	-1	2	Rat	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	CHEMBL4290744	173929	0	None	-1	2	Rat	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	312	3	0	5	2.3	CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21	10.1016/j.bmcl.2018.08.022
	CHEMBL5083384	221636	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1	10.1021/acs.jmedchem.1c00563
	CHEMBL5090853	222061	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1F	10.1021/acs.jmedchem.1c00563
	156014680	184029	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	184029	0	None	-2	2	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	59497075	121359	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	376	4	0	3	4.7	O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	CHEMBL3337525	121359	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	376	4	0	3	4.7	O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1	10.1021/jm500496m
	46917791	64519	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	472	6	0	4	6.7	CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669400	64519	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	472	6	0	4	6.7	CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668094	116316	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221833	116316	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	69344751	116317	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221834	116317	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	336	7	1	4	4.1	CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	58966955	116320	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	337	7	0	4	4.0	CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221837	116320	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	337	7	0	4	4.0	CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	90668103	116329	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	340	6	0	3	4.6	CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221845	116329	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	340	6	0	3	4.6	CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	49801371	165520	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093620	165520	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	53326074	64502	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	5	0	4	4.0	CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669384	64502	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	5	0	4	4.0	CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46225334	206825	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595607	206825	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225583	206953	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596527	206953	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24815883	208241	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604993	208241	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	53325603	64496	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669377	64496	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	21393580	15465	0	None	-	1	Human	4.6	pEC50	=	4.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	253	3	0	2	3.3	O=C1OC(Cc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095704	15465	0	None	-	1	Human	4.6	pEC50	=	4.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	253	3	0	2	3.3	O=C1OC(Cc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	60096211	96834	0	None	-1	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381649	96834	0	None	-1	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	1310	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	1369	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	33032	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	44272391	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	88747398	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	CHEMBL575060	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	DB00142	9095	110	None	-389	17	Human	5.6	pEC50	=	5.6	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01124
	69093106	90681	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F	10.1021/jm300912k
	CHEMBL2206444	90681	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F	10.1021/jm300912k
	44591748	191820	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL485528	191820	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	60096183	166063	0	None	-3	2	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL4099470	166063	0	None	-3	2	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	24809650	81360	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	326	6	0	5	3.5	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC	10.1021/jm2016864
	CHEMBL2029792	81360	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	326	6	0	5	3.5	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC	10.1021/jm2016864
	162665716	189148	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	5	0	4	4.0	c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4784990	189148	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	323	5	0	4	4.0	c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	1310	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	1369	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	33032	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	44272391	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	88747398	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	CHEMBL575060	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	DB00142	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmcl.2005.09.014
	1310	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	1369	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	33032	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	44272391	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	88747398	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	CHEMBL575060	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	DB00142	9095	110	None	-389	17	Human	4.6	pEC50	=	4.6	Functional	Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2007.02.040
	25173365	191584	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	5	0	3	3.6	CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL485175	191584	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	5	0	3	3.6	CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	70685767	81384	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.6	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	CHEMBL2029814	81384	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	371	5	0	5	4.6	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1	10.1021/jm2016864
	CHEMBL5073573	221079	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc([N+](=O)[O-])c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	9815616	121578	6	None	-2	4	Rat	5.6	pEC50	=	5.6	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	121578	6	None	-2	4	Rat	5.6	pEC50	=	5.6	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	71136188	152533	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	CHEMBL3916627	152533	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	155515810	176793	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4442487	176793	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	3954	7451	60	None	6	2	Human	7.6	pEC50	=	7.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1016/j.bmcl.2009.11.008
	9868580	7451	60	None	6	2	Human	7.6	pEC50	=	7.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1016/j.bmcl.2009.11.008
	CHEMBL593013	7451	60	None	6	2	Human	7.6	pEC50	=	7.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1016/j.bmcl.2009.11.008
	49765871	8926	45	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	6317	8926	45	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	CHEMBL2179319	8926	45	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	162677102	190305	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	401	5	0	4	4.8	Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4799882	190305	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	401	5	0	4	4.8	Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	155511507	176373	1	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	239	2	0	3	2.6	CCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4436220	176373	1	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	239	2	0	3	2.6	CCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	44156621	15508	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	7	0	4	3.4	CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096080	15508	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	7	0	4	3.4	CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	134131309	148952	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	359	2	0	3	6.1	Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1	10.1016/j.bmc.2016.11.018
	CHEMBL3883923	148952	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	359	2	0	3	6.1	Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1	10.1016/j.bmc.2016.11.018
	67060140	174176	0	None	-26	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4295230	174176	0	None	-26	2	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	362	4	0	5	3.7	Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	162661604	188282	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	307	4	0	4	3.1	COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4764905	188282	0	None	-	1	Human	5.6	pEC50	=	5.6	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	307	4	0	4	3.1	COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44591746	191694	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1	10.1016/j.bmcl.2009.03.032
	CHEMBL485330	191694	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1	10.1016/j.bmcl.2009.03.032
	70685766	81380	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029810	81380	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	60096231	164434	15	None	-48	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	CHEMBL4081453	164434	15	None	-48	4	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	44591715	198254	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL519341	198254	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	117967312	149088	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885353	149088	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	117967312	149088	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885353	149088	3	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.3	FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155551721	182208	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4576215	182208	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	337	3	0	3	4.9	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	51357935	68750	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	372	3	0	4	4.4	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F	10.1021/jm101414h
	CHEMBL1774229	68750	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	372	3	0	4	4.4	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F	10.1021/jm101414h
	168299593	199511	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	385	7	0	5	4.7	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5220316	199511	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	385	7	0	5	4.7	CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	71116726	152054	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	CHEMBL3912982	152054	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	137652500	163968	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075697	163968	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	71128768	151358	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3907644	151358	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	44591714	191080	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484127	191080	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL5069547	220998	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(F)cc1	10.1021/acs.jmedchem.1c00563
	118714743	121344	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	4	0	4	3.8	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337509	121344	0	None	-	1	Human	6.6	pEC50	=	6.6	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	4	0	4	3.8	CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	25010196	68737	0	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21	10.1021/jm101414h
	CHEMBL1774111	68737	0	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21	10.1021/jm101414h
	134131502	148930	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	363	5	0	4	5.1	Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3883585	148930	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	363	5	0	4	5.1	Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	155525998	177814	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	371	3	0	3	5.3	Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4456816	177814	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	371	3	0	3	5.3	Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	9815616	121578	6	None	-2	4	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	121578	6	None	-2	4	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	66785010	162642	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4060306	162642	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	66787433	163242	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067298	163242	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	49801369	165528	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093792	165528	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	25073303	173812	0	None	11	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4288731	173812	0	None	11	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	156018381	184701	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	184701	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	70689923	81361	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	336	7	0	4	4.2	CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029793	81361	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	336	7	0	4	4.2	CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O	10.1021/jm2016864
	155524603	177705	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	322	2	0	4	3.3	Clc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4455228	177705	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	322	2	0	4	3.3	Clc1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL5091768	222104	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4ccc(Cl)cc4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	11690196	149544	0	None	4	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	416	7	2	7	4.5	CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3892611	149544	0	None	4	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	416	7	2	7	4.5	CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O	10.1016/j.bmcl.2016.11.049
	156018381	184701	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	184701	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	118714734	121334	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	296	6	0	4	3.3	CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337499	121334	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	296	6	0	4	3.3	CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	57459483	89428	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.9	CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179331	89428	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.9	CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	51357937	68753	0	None	2	2	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774233	68753	0	None	2	2	Human	8.5	pEC50	=	8.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	60096201	165347	0	None	-5	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091735	165347	0	None	-5	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	10198133	213287	12	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL8839	213287	12	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	10198133	213287	12	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	213287	12	None	1	4	Human	8.4	pEC50	=	8.4	Functional	Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	42629118	191038	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	319	3	0	2	4.5	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL483750	191038	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	319	3	0	2	4.5	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	70696264	81389	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	407	6	0	5	5.6	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029819	81389	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	407	6	0	5	5.6	CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O	10.1021/jm2016864
	162662455	188801	3	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4780781	188801	3	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	146036862	182417	6	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	279	2	0	3	3.4	Brc1cccc2c1nnn2CC1CCCC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4580916	182417	6	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	279	2	0	3	3.4	Brc1cccc2c1nnn2CC1CCCC1	10.1021/acs.jmedchem.8b00161
	162662455	188801	3	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1021/acs.jmedchem.1c00563
	CHEMBL4780781	188801	3	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	419	7	0	5	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1	10.1021/acs.jmedchem.1c00563
	CHEMBL5085978	221785	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1	10.1021/acs.jmedchem.1c00563
	66785087	164919	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4087196	164919	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	11362035	6831	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	6328	6831	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	6329	6831	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	CHEMBL105296	6831	1	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2009.11.008
	156010124	183810	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	183810	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	1377	8122	26	None	1	8	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm030967o
	5310979	8122	26	None	1	8	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm030967o
	CHEMBL284193	8122	26	None	1	8	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm030967o
	1368	9070	37	None	-1	11	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm030967o
	5310956	9070	37	None	-1	11	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm030967o
	CHEMBL280563	9070	37	None	-1	11	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm030967o
	44361316	41746	2	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL143267	41746	2	None	-	1	Rat	6.5	pEC50	=	6.5	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	217	5	4	4	-1.2	N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O	10.1021/jm030967o
	1392	6861	48	None	5	4	Rat	6.5	pEC50	=	6.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	5310984	6861	48	None	5	4	Rat	6.5	pEC50	=	6.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	CHEMBL40086	6861	48	None	5	4	Rat	6.5	pEC50	=	6.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	521212	74108	59	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	209	2	0	3	2.5	c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL1884989	74108	59	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	209	2	0	3	2.5	c1ccc(Cn2nnc3ccccc32)cc1	10.1021/acs.jmedchem.8b00161
	156010124	183810	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	183810	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	44591812	199332	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL521175	199332	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	59599459	156208	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3945882	156208	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	118714740	121341	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	5	0	6	2.5	CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337506	121341	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	5	0	6	2.5	CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O	10.1021/jm500496m
	57459482	90675	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	433	4	0	6	4.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1	10.1021/jm300912k
	CHEMBL2206438	90675	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	433	4	0	6	4.2	COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1	10.1021/jm300912k
	118714756	121356	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337522	121356	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	44178197	68755	0	None	1	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774235	68755	0	None	1	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL5078863	221370	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	25073615	173243	0	None	4	2	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	CHEMBL4278070	173243	0	None	4	2	Rat	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	300	3	0	5	2.4	CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1	10.1016/j.bmcl.2018.08.022
	25002940	7890	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	10.1021/jm2016864
	6320	7890	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	10.1021/jm2016864
	CHEMBL2029821	7890	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	10.1021/jm2016864
	53326709	64513	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	405	6	0	5	5.1	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669394	64513	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	405	6	0	5	5.1	CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53324151	64514	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	4	0	3	4.7	CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669395	64514	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	4	0	3	4.7	CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668099	116324	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221840	116324	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	156017237	184540	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	184540	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	53317704	64503	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	5	1	4	4.1	CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669385	64503	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	327	5	1	4	4.1	CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46225582	208394	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL605831	208394	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	118714738	121339	0	None	-	1	Human	4.5	pEC50	=	4.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	273	4	0	4	2.8	CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337504	121339	0	None	-	1	Human	4.5	pEC50	=	4.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	273	4	0	4	2.8	CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O	10.1021/jm500496m
	70683629	81357	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1	10.1021/jm2016864
	CHEMBL2029788	81357	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	296	5	0	4	3.4	COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1	10.1021/jm2016864
	11951099	74253	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	479	8	1	5	7.1	CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189264	74253	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	479	8	1	5	7.1	CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	59599568	152828	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3918914	152828	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	44591772	198246	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	4	0	3	4.7	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL519332	198246	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	4	0	3	4.7	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	117972047	148949	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	327	6	0	4	4.0	Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3883827	148949	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	327	6	0	4	4.0	Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	46215876	87582	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	374	2	1	3	5.1	N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152116	87582	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	374	2	1	3	5.1	N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	162670769	189747	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	4	4.2	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4793069	189747	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	4	4.2	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	156016100	184466	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	184466	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156017237	184540	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	184540	0	None	1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	71136746	155379	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3939174	155379	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	156015654	184300	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	184300	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156016100	184466	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4641860	184466	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1162	42	0	18	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	11631795	71573	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL181953	71573	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	155531978	178511	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	363	3	0	5	4.2	N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4467158	178511	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	363	3	0	5	4.2	N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	51357934	68749	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	CHEMBL1774227	68749	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1	10.1021/jm101414h
	66784529	163872	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074421	163872	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	71451227	87581	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	438	3	1	5	5.4	N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152115	87581	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	438	3	1	5	5.4	N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	25073303	173812	0	None	-11	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	CHEMBL4288731	173812	0	None	-11	2	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	348	4	0	5	3.4	Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C	10.1016/j.bmcl.2018.08.022
	156015654	184300	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	184300	0	None	-1	2	Human	6.5	pEC50	=	6.5	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	44155754	15284	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2cccc(N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094146	15284	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2cccc(N)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44300258	20423	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1194540	20423	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL552836	20423	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1	10.1016/s0960-894x(01)00329-8
	51357396	68729	0	None	-	1	Rat	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774102	68729	0	None	-	1	Rat	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21	10.1021/jm101414h
	118714737	121338	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337503	121338	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	349	5	0	4	4.2	CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O	10.1021/jm500496m
	71117091	156128	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	412	4	1	6	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21	nan
	CHEMBL3945222	156128	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	412	4	1	6	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21	nan
	127030385	145941	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	217	5	4	4	-1.0	N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL3787264	145941	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	217	5	4	4	-1.0	N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	137635882	162673	0	None	1	2	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4060567	162673	0	None	1	2	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	9815617	121277	7	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	121277	7	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	1393	8321	64	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1396	8321	64	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	213056	8321	64	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	CHEMBL8759	8321	64	None	2	6	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	11187949	72377	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183319	72377	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	373	10	1	5	5.3	Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	162649047	186570	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	3	4.2	Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4744761	186570	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	341	5	0	3	4.2	Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	44591796	191422	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484957	191422	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	304	3	0	3	3.4	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	24905705	190801	1	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL482081	190801	1	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	46887319	15765	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098388	15765	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	25003298	81379	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029809	81379	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O	10.1021/jm2016864
	10047169	9998	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.09.028
	1403	9998	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.09.028
	CHEMBL182371	9998	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.09.028
	10047169	9998	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2005.06.017
	1403	9998	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2005.06.017
	CHEMBL182371	9998	1	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2005.06.017
	44591713	191079	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484126	191079	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	118714753	121353	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1	10.1021/jm500496m
	CHEMBL3337519	121353	0	None	-	1	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1	10.1021/jm500496m
	44178197	68755	0	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774235	68755	0	None	-1	2	Rat	7.5	pEC50	=	7.5	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	51354020	68756	0	None	23	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/acs.jmedchem.1c00563
	CHEMBL1774236	68756	0	None	23	2	Human	7.5	pEC50	=	7.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/acs.jmedchem.1c00563
	1393	8321	64	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	1396	8321	64	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	213056	8321	64	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	CHEMBL8759	8321	64	None	-2	6	Rat	7.5	pEC50	=	7.5	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	71457756	90677	0	None	66	2	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	90677	0	None	66	2	Human	7.5	pEC50	=	7.5	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	46887371	15575	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096712	15575	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	325	4	0	3	4.4	CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	162661233	188291	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4765006	188291	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1	10.1016/j.ejmech.2019.111881
	CHEMBL5076606	221231	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	136950	15466	26	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	269	4	0	3	3.1	O=C1OC(COc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095705	15466	26	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	269	4	0	3	3.1	O=C1OC(COc2ccccc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	59066632	213349	89	None	1	2	Human	4.5	pEC50	=	4.5	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9602569
	92136	213349	89	None	1	2	Human	4.5	pEC50	=	4.5	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9602569
	CHEMBL88804	213349	89	None	1	2	Human	4.5	pEC50	=	4.5	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9602569
	44300135	20056	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	279	4	4	5	-0.3	Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL1191723	20056	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	279	4	4	5	-0.3	Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL542862	20056	0	None	-	1	Rat	4.5	pEC50	=	4.5	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	279	4	4	5	-0.3	Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(01)00329-8
	11951271	74285	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	10	1	6	5.7	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189516	74285	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	10	1	6	5.7	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	118714746	121346	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	389	5	0	4	4.4	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O	10.1021/jm500496m
	CHEMBL3337512	121346	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	389	5	0	4	4.4	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O	10.1021/jm500496m
	71117198	157077	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	358	3	1	4	1.7	CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3952803	157077	0	None	-	1	Human	6.5	pEC50	=	6.5	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	358	3	1	4	1.7	CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	11950746	73867	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	419	9	1	6	5.1	CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	CHEMBL187342	73867	0	None	-	1	Human	5.5	pEC50	=	5.5	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	419	9	1	6	5.1	CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	627502	15354	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094733	15354	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	46887370	15574	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096711	15574	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	46887322	15768	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098391	15768	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	59391336	121333	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	294	6	0	3	3.6	CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337498	121333	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	294	6	0	3	3.6	CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	10176836	42648	0	None	-	1	Rat	4.4	pEC50	=	4.4	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	221	2	3	3	-0.2	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F	10.1021/jm000346k
	CHEMBL144201	42648	0	None	-	1	Rat	4.4	pEC50	=	4.4	Functional	Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	221	2	3	3	-0.2	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F	10.1021/jm000346k
	70685762	81359	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	330	5	0	4	4.1	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	CHEMBL2029791	81359	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	330	5	0	4	4.1	COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl	10.1021/jm2016864
	69093439	90680	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206443	90680	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	71457756	90677	0	None	66	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	90677	0	None	66	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	155560423	181854	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	387	3	0	3	5.8	FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4568356	181854	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	387	3	0	3	5.8	FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	44300820	20150	0	None	-1	2	Rat	4.4	pEC50	=	4.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	265	4	3	5	-0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1192558	20150	0	None	-1	2	Rat	4.4	pEC50	=	4.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	265	4	3	5	-0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL543811	20150	0	None	-1	2	Rat	4.4	pEC50	=	4.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	265	4	3	5	-0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1	10.1016/s0960-894x(01)00329-8
	68108457	155335	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3938796	155335	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	25002941	81392	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	6	0	5	5.1	CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029823	81392	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	391	6	0	5	5.1	CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O	10.1021/jm2016864
	66786069	163240	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	163240	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	44591794	191420	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	370	4	0	4	4.1	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484956	191420	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	370	4	0	4	4.1	C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	44155534	15456	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095638	15456	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44591647	191586	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	4.1	O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL485176	191586	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	4.1	O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	11531272	71976	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	392	10	1	4	5.4	Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182511	71976	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	392	10	1	4	5.4	Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	11710164	73110	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185046	73110	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	357	10	1	5	4.6	Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	57459481	89413	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	340	3	0	4	4.3	CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179315	89413	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	340	3	0	4	4.3	CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	23770349	15682	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccccc2Cl)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097656	15682	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2ccccc2Cl)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	57459635	89419	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	418	4	0	4	5.2	FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179322	89419	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	418	4	0	4	5.2	FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	59599552	155082	0	None	12	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3936830	155082	0	None	12	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	71135411	130175	0	None	5	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616848	130175	0	None	5	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	25002939	81391	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029822	81391	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	377	6	0	5	4.8	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL5083201	221630	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Cl)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	71136199	149465	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	3	0	7	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3892060	149465	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	3	0	7	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	11310142	9200	19	None	13	3	Human	6.4	pEC50	=	6.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	9200	19	None	13	3	Human	6.4	pEC50	=	6.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	9200	19	None	13	3	Human	6.4	pEC50	=	6.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	25002587	81377	4	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029807	81377	4	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.7	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O	10.1021/jm2016864
	53320818	64510	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	346	4	0	4	4.3	CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669391	64510	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	346	4	0	4	4.3	CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53325452	64518	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	438	6	0	4	6.4	CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669399	64518	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	438	6	0	4	6.4	CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668096	116319	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	350	7	0	4	4.1	CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221836	116319	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	350	7	0	4	4.1	CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	53324803	64500	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	299	3	0	4	3.5	CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669382	64500	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	299	3	0	4	3.5	CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	24815439	208714	1	None	-18	2	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607689	208714	1	None	-18	2	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225581	208766	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL608103	208766	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44361401	38115	0	None	1	5	Rat	8.4	pEC50	=	8.4	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL140197	38115	0	None	1	5	Rat	8.4	pEC50	=	8.4	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	117972155	149033	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884833	149033	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	71457757	90686	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	466	5	0	5	5.4	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	CHEMBL2206449	90686	0	None	-	1	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	466	5	0	5	5.4	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/jm300912k
	71137012	130178	0	None	11	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616851	130178	0	None	11	2	Human	8.4	pEC50	=	8.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	162654912	187431	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	387	6	0	4	4.1	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4755035	187431	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	387	6	0	4	4.1	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1	10.1016/j.ejmech.2019.111881
	162674461	190110	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	403	6	0	4	4.4	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4797417	190110	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	403	6	0	4	4.4	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL5083122	221621	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1Cc1ccc(Cl)cc1	10.1021/acs.jmedchem.1c00563
	66785551	163932	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075258	163932	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66784675	163953	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075537	163953	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	162642952	188516	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	3	5.2	Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4777206	188516	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	373	5	0	3	5.2	Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1	10.1016/j.ejmech.2019.111881
	155554782	181377	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	203	3	0	4	1.9	COc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4557213	181377	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	203	3	0	4	1.9	COc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	57459524	89421	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	358	3	0	4	4.2	FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179324	89421	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	358	3	0	4	4.2	FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	10474978	20231	0	None	1	2	Rat	5.4	pEC50	=	5.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1193146	20231	0	None	1	2	Rat	5.4	pEC50	=	5.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1	10.1016/s0960-894x(01)00329-8
	CHEMBL544508	20231	0	None	1	2	Rat	5.4	pEC50	=	5.4	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1	10.1016/s0960-894x(01)00329-8
	59599576	149317	0	None	-5	2	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3890848	149317	0	None	-5	2	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	421	9	2	6	5.0	CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	44591745	199123	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL520677	199123	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1	10.1016/j.bmcl.2009.03.032
	68109677	163972	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075762	163972	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66786493	164039	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076639	164039	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	46887415	15314	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094415	15314	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	299	5	0	4	3.1	COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	70685764	81365	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	0	4	5.2	CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029797	81365	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	358	6	0	4	5.2	CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	137659992	166015	0	None	-8	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4098939	166015	0	None	-8	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	162645511	186377	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	305	5	0	3	3.9	c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4742196	186377	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	305	5	0	3	3.9	c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44392708	72854	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	423	11	1	7	4.7	Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183807	72854	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	423	11	1	7	4.7	Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	25008615	68734	0	None	1	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774108	68734	0	None	1	2	Human	7.4	pEC50	=	7.4	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	71116772	154447	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	CHEMBL3931730	154447	0	None	-	1	Human	7.4	pEC50	=	7.4	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	44591793	191131	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	269	3	0	4	2.5	C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484403	191131	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	269	3	0	4	2.5	C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	71137008	130182	0	None	7	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616855	130182	0	None	7	2	Human	7.4	pEC50	=	7.4	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	156019582	184790	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	184790	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	3954	7451	60	None	-6	2	Rat	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm5000563
	9868580	7451	60	None	-6	2	Rat	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm5000563
	CHEMBL593013	7451	60	None	-6	2	Rat	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm5000563
	44155643	15621	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097053	15621	0	None	-	1	Human	5.4	pEC50	=	5.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	156019582	184790	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	184790	0	None	2	2	Human	6.4	pEC50	=	6.4	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	46227795	206742	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	357	2	0	3	5.3	CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1	10.1016/j.bmcl.2009.11.008
	CHEMBL595043	206742	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	357	2	0	3	5.3	CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1	10.1016/j.bmcl.2009.11.008
	46227792	206871	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	415	3	0	7	3.0	Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1	10.1016/j.bmcl.2009.11.008
	CHEMBL595967	206871	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	415	3	0	7	3.0	Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1	10.1016/j.bmcl.2009.11.008
	70689927	81375	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	CHEMBL2029805	81375	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	373	6	0	5	4.9	Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	10822010	43160	1	None	-	1	Rat	5.4	pEC50	=	5.4	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	CHEMBL144678	43160	1	None	-	1	Rat	5.4	pEC50	=	5.4	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F	10.1021/jm000346k
	1377	8122	26	None	1	8	Rat	7.4	pEC50	=	7.4	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm901523t
	5310979	8122	26	None	1	8	Rat	7.4	pEC50	=	7.4	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL284193	8122	26	None	1	8	Rat	7.4	pEC50	=	7.4	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm901523t
	11344646	133554	1	None	2	3	Human	7.4	pEC50	=	7.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	CHEMBL365368	133554	1	None	2	3	Human	7.4	pEC50	=	7.4	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	46887493	15356	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094762	15356	1	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	11951449	73496	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL185659	73496	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	51356571	68746	0	None	-	1	Rat	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.8	C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C	10.1021/jm101414h
	CHEMBL1774224	68746	0	None	-	1	Rat	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	388	3	0	4	4.8	C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C	10.1021/jm101414h
	11494153	72855	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	356	10	1	4	5.2	Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183808	72855	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	356	10	1	4	5.2	Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	118714752	121352	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	401	4	0	4	4.5	N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337518	121352	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	401	4	0	4	4.5	N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	71136640	130180	0	None	60	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616853	130180	0	None	60	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	53240406	130174	17	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	70689925	81371	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	295	5	1	4	3.5	CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	CHEMBL2029801	81371	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	295	5	1	4	3.5	CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1	10.1021/jm2016864
	118714741	121342	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	364	6	0	5	3.1	CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337507	121342	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	364	6	0	5	3.1	CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	57459480	89409	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	347	4	0	6	3.1	COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179311	89409	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	347	4	0	6	3.1	COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	60096231	164434	15	None	-48	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	CHEMBL4081453	164434	15	None	-48	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	59599565	152093	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3913281	152093	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	44300587	19805	0	None	12	2	Rat	5.3	pEC50	=	5.3	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189911	19805	0	None	12	2	Rat	5.3	pEC50	=	5.3	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL539761	19805	0	None	12	2	Rat	5.3	pEC50	=	5.3	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1	10.1016/s0960-894x(01)00329-8
	162647052	186408	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4742843	186408	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1	10.1016/j.ejmech.2019.111881
	156014680	184029	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	184029	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	70692086	81367	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029799	81367	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	44591774	198872	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL520300	198872	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	54583299	68727	0	None	-	1	Rat	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	390	4	0	6	3.7	Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1	10.1021/jm101414h
	CHEMBL1774100	68727	0	None	-	1	Rat	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	390	4	0	6	3.7	Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1	10.1021/jm101414h
	118714751	121351	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337517	121351	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	25008615	68734	0	None	-1	2	Rat	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774108	68734	0	None	-1	2	Rat	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	374	3	0	4	4.4	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21	10.1021/jm101414h
	53240406	130174	17	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	107	4	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	71119170	155551	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3940610	155551	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	1392	6861	48	None	5	4	Rat	6.3	pEC50	=	6.3	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(01)00329-8
	5310984	6861	48	None	5	4	Rat	6.3	pEC50	=	6.3	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL40086	6861	48	None	5	4	Rat	6.3	pEC50	=	6.3	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1016/s0960-894x(01)00329-8
	156014680	184029	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635960	184029	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1250	48	0	20	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	10330132	108159	1	None	10	2	Rat	5.3	pEC50	=	5.3	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(99)00266-8
	CHEMBL297150	108159	1	None	10	2	Rat	5.3	pEC50	=	5.3	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1016/s0960-894x(99)00266-8
	1374	8862	35	None	-19	4	Human	4.3	pEC50	=	4.3	Functional	Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor	ChEMBL	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	10.1021/jm060950g
	5311455	8862	35	None	-19	4	Human	4.3	pEC50	=	4.3	Functional	Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor	ChEMBL	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	10.1021/jm060950g
	CHEMBL39372	8862	35	None	-19	4	Human	4.3	pEC50	=	4.3	Functional	Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor	ChEMBL	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	10.1021/jm060950g
	168299034	199460	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5219080	199460	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O	10.1021/acs.jmedchem.2c00969
	118714750	121350	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337516	121350	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	367	4	0	4	4.2	N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	168295099	199829	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	378	6	0	5	4.0	CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5219090	199829	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	378	6	0	5	4.0	CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5223017	199829	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	378	6	0	5	4.0	CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O	10.1021/acs.jmedchem.2c00969
	46830123	7859	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	6321	7859	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	CHEMBL1094763	7859	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	46197780	12354	0	None	-25	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	273	7	4	4	-0.2	N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1076865	12354	0	None	-25	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	273	7	4	4	-0.2	N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O	10.1021/jm901523t
	44591684	191115	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL484340	191115	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	44361401	38115	0	None	1	5	Rat	8.3	pEC50	=	8.3	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL140197	38115	0	None	1	5	Rat	8.3	pEC50	=	8.3	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	1393	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	1396	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	213056	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	CHEMBL8759	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm970719q
	1393	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	1396	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	213056	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	CHEMBL8759	8321	64	None	2	6	Human	8.3	pEC50	=	8.3	Functional	Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1016/s0960-894x(98)00146-2
	71476419	130187	0	None	51	2	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616860	130187	0	None	51	2	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	71457756	90677	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	90677	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	71457756	90677	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL2206440	90677	0	None	66	2	Human	8.3	pEC50	=	8.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	117968589	149046	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	423	6	0	4	5.7	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884936	149046	0	None	-	1	Human	8.3	pEC50	=	8.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	423	6	0	4	5.7	CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1	10.1016/j.bmc.2016.11.018
	53240406	130174	17	None	107	4	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	107	4	Human	8.3	pEC50	=	8.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	68109580	165304	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4091370	165304	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	162650622	186829	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	431	6	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br	10.1016/j.ejmech.2019.111881
	CHEMBL4747716	186829	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	431	6	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br	10.1016/j.ejmech.2019.111881
	162662472	188832	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	371	6	0	4	3.6	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL4781224	188832	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	371	6	0	4	3.6	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F	10.1016/j.ejmech.2019.111881
	155513095	176483	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	329	2	0	3	3.4	Brc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4437986	176483	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	329	2	0	3	3.4	Brc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	155540333	179275	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4483344	179275	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	338	3	0	4	4.3	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL5074997	221130	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1CC1CCC1	10.1021/acs.jmedchem.1c00563
	CHEMBL5091657	222098	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1F	10.1021/acs.jmedchem.1c00563
	10807972	42591	1	None	-3	4	Rat	7.3	pEC50	=	7.3	Functional	Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	CHEMBL144151	42591	1	None	-3	4	Rat	7.3	pEC50	=	7.3	Functional	Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	104766	6822	42	None	2	14	Rat	5.3	pEC50	=	5.3	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	1365	6822	42	None	2	14	Rat	5.3	pEC50	=	5.3	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	CHEMBL34453	6822	42	None	2	14	Rat	5.3	pEC50	=	5.3	Functional	Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1016/S0960-894X(97)00068-1
	46215708	87580	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	424	3	0	5	5.3	N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152114	87580	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	424	3	0	5	5.3	N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	71450118	89425	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	330	3	0	4	4.2	CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179328	89425	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	330	3	0	4	4.2	CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	53320175	64511	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669392	64511	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	390	5	0	4	5.9	CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	90668092	116314	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221831	116314	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	90668100	116325	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221841	116325	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	322	6	1	4	4.0	CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O	10.1039/C0MD00200C
	90668105	116331	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	356	6	0	4	4.6	CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221847	116331	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	356	6	0	4	4.6	CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O	10.1039/C0MD00200C
	53325603	64496	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669377	64496	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	306	3	0	4	2.9	CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53316861	64497	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	320	3	1	4	3.0	CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669378	64497	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	320	3	1	4	3.0	CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53323493	64506	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	341	4	0	4	4.2	CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669388	64506	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	341	4	0	4	4.2	CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	24849462	206537	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593744	206537	0	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	90668104	116330	0	None	-	1	Human	4.3	pEC50	=	4.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	0	3	4.6	CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221846	116330	0	None	-	1	Human	4.3	pEC50	=	4.3	Functional	Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis	ChEMBL	326	5	0	3	4.6	CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	60096194	163367	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068679	163367	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	156014194	183989	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	183989	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	184693	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	184693	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	71117065	156054	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	539	3	1	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21	nan
	CHEMBL3944557	156054	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	539	3	1	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21	nan
	156014194	183989	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4635373	183989	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	941	27	0	13	8.5	COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156018860	184693	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645193	184693	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	1074	36	0	16	8.6	COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	57459542	89424	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	401	4	0	5	4.5	FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179327	89424	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	401	4	0	5	4.5	FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	28407322	189616	9	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	277	3	0	3	3.1	c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4791292	189616	9	None	-	1	Human	5.3	pEC50	=	5.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	277	3	0	3	3.1	c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	3756397	15086	2	None	-7	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	239	7	4	4	-0.5	NC(CCP(=O)(O)CCC(=O)O)C(=O)O	10.1021/jm901523t
	4041087	15086	2	None	-7	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	239	7	4	4	-0.5	NC(CCP(=O)(O)CCC(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1092727	15086	2	None	-7	4	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	239	7	4	4	-0.5	NC(CCP(=O)(O)CCC(=O)O)C(=O)O	10.1021/jm901523t
	44591747	191695	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL485331	191695	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	297	4	0	3	3.7	COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	71137034	130177	0	None	7	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616850	130177	0	None	7	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	156012835	184213	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	184213	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156012835	184213	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4638687	184213	0	None	-2	2	Human	6.3	pEC50	=	6.3	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	985	30	0	14	8.5	COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	71137010	130176	0	None	5	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616849	130176	0	None	5	2	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	162646719	186388	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	3	4.7	Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	CHEMBL4742364	186388	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	3	4.7	Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	162662970	188711	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	343	5	0	4	3.6	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL4779768	188711	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	343	5	0	4	3.6	Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL5090065	222019	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)nc1	10.1021/acs.jmedchem.1c00563
	156015654	184300	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	184300	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	118714744	121330	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	4	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O	10.1021/jm500496m
	CHEMBL3337456	121330	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	347	4	0	4	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O	10.1021/jm500496m
	66788653	89411	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	394	3	0	4	4.9	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179313	89411	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	394	3	0	4	4.9	FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	156015654	184300	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4639821	184300	0	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	897	24	0	12	8.5	COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	70681519	81370	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029800	81370	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O	10.1021/jm2016864
	162669063	189515	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	4	4.7	Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4789937	189515	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	357	5	0	4	4.7	Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	44392629	71542	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	456	10	1	4	5.9	CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL181921	71542	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	456	10	1	4	5.9	CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	11271167	73574	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	11	1	6	6.1	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL185994	73574	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	11	1	6	6.1	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	11950927	130207	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	11	1	6	6.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL361724	130207	0	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	475	11	1	6	6.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	57459477	89430	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm3010724
	CHEMBL2179333	89430	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm3010724
	71117141	154227	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	CHEMBL3930164	154227	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	57459477	89430	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm300912k
	CHEMBL2179333	89430	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	385	3	0	5	4.1	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12	10.1021/jm300912k
	49801368	166437	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4103808	166437	0	None	-	1	Human	7.3	pEC50	=	7.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	59599616	153042	1	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3920609	153042	1	None	-1	2	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	25125217	7343	25	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	7678	7343	25	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL3937907	7343	25	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	DB16073	7343	25	None	-	1	Human	6.3	pEC50	=	6.3	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	44428730	151484	1	None	-	1	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL390863	151484	1	None	-	1	Rat	4.3	pEC50	=	4.3	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	137652320	164053	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076786	164053	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	24779944	14640	0	None	-36	3	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	225	6	4	4	-0.9	N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1089852	14640	0	None	-36	3	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	225	6	4	4	-0.9	N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O	10.1021/jm901523t
	44428730	151484	1	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL390863	151484	1	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	185	3	3	5	-0.2	CCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	11546303	72008	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	10	1	5	5.0	CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182668	72008	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	10	1	5	5.0	CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	44392671	72043	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	7	1	5	6.4	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182822	72043	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	7	1	5	6.4	Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2004.09.028
	46887369	15647	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097380	15647	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	311	5	0	3	4.2	CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1	10.1016/j.bmcl.2010.03.089
	CHEMBL5081320	221521	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4ccc(F)cc4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	44155863	15318	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094460	15318	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	262	6	1	3	3.6	CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	25173209	195802	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	5	0	3	3.6	O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL509096	195802	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	289	5	0	3	3.6	O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1	10.1016/j.bmcl.2009.03.032
	44155315	15427	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095385	15427	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	247	6	0	2	4.0	CCCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155642	15620	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097052	15620	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	281	6	0	2	4.6	CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	46887367	15645	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097378	15645	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	297	5	0	3	3.7	CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	71117030	152631	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	5	1	7	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21	nan
	CHEMBL3917329	152631	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	423	5	1	7	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21	nan
	44591795	199219	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	320	3	0	3	3.9	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL520837	199219	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	320	3	0	3	3.9	C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	11952168	74117	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	14	1	6	6.2	CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	CHEMBL188538	74117	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	461	14	1	6	6.2	CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21	10.1016/j.bmcl.2005.06.017
	57459494	90679	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206442	90679	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	155566352	182713	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	416	3	0	4	5.1	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4587631	182713	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	416	3	0	4	5.1	Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1	10.1021/acs.jmedchem.8b00161
	11626955	158590	0	None	18	2	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3965244	158590	0	None	18	2	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	471	7	2	8	4.6	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O	10.1016/j.bmcl.2016.11.049
	117971699	149063	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	397	6	0	4	4.9	FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885115	149063	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	397	6	0	4	4.9	FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	71131322	130184	0	None	43	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616857	130184	0	None	43	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	60096228	163566	0	None	-2	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4070866	163566	0	None	-2	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71137011	130185	0	None	58	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616858	130185	0	None	58	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	134130002	148945	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3883801	148945	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	389	6	0	4	5.6	Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	69093928	90684	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206447	90684	0	None	-	1	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	60096250	165700	0	None	-1	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095567	165700	0	None	-1	2	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	117972041	148987	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1	10.1016/j.bmc.2016.11.018
	CHEMBL3884170	148987	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	347	5	0	4	4.6	Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1	10.1016/j.bmc.2016.11.018
	155559961	181674	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	2	0	3	3.3	Clc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4564190	181674	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	285	2	0	3	3.3	Clc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	155567522	182750	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	3	0	3	3.0	CCCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4588508	182750	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	253	3	0	3	3.0	CCCCn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL5086642	221820	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CCC1	10.1021/acs.jmedchem.1c00563
	CHEMBL5088821	221958	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1F	10.1021/acs.jmedchem.1c00563
	CHEMBL5093895	222231	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC2CCC1C2	10.1021/acs.jmedchem.1c00563
	155522079	177480	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	304	3	0	4	3.7	Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	CHEMBL4451873	177480	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	304	3	0	4	3.7	Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1	10.1021/acs.jmedchem.8b00161
	57459487	90674	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	402	4	0	4	5.0	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1	10.1021/jm300912k
	CHEMBL2206437	90674	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	402	4	0	4	5.0	Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1	10.1021/jm300912k
	1310	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	1369	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	33032	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	44272391	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	88747398	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	CHEMBL575060	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	DB00142	9095	110	None	-457	17	Rat	6.2	pEC50	=	6.2	Functional	Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(99)00266-8
	10376615	87344	0	None	-	1	Rat	6.2	pEC50	=	6.2	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	232	4	4	5	-2.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL214917	87344	0	None	-	1	Rat	6.2	pEC50	=	6.2	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	232	4	4	5	-2.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL544505	87344	0	None	-	1	Rat	6.2	pEC50	=	6.2	Functional	Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist	ChEMBL	232	4	4	5	-2.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL5074682	221105	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4cccc(F)c4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	10473248	20958	0	None	4	3	Rat	5.2	pEC50	=	5.2	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1198741	20958	0	None	4	3	Rat	5.2	pEC50	=	5.2	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL540015	20958	0	None	4	3	Rat	5.2	pEC50	=	5.2	Functional	Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2	ChEMBL	280	4	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1	10.1016/s0960-894x(01)00329-8
	42610165	87574	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	435	4	0	5	5.2	N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152107	87574	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	435	4	0	5	5.2	N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL5079928	221433	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3ccccc3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	155559438	181638	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	198	2	0	4	1.7	N#Cc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4563304	181638	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	198	2	0	4	1.7	N#Cc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	66785027	165117	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089416	165117	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL5076356	221210	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		O=C1c2nc3cccc(-c4ccccc4)c3n2CCN1CC1CC1	10.1021/acs.jmedchem.1c00563
	53316862	64499	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669381	64499	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	298	3	0	3	4.1	CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53323492	64505	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	356	7	0	4	4.5	CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669387	64505	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	356	7	0	4	4.5	CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53325450	64512	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	418	7	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669393	64512	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	418	7	0	4	5.7	CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	46225584	206454	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593056	206454	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46226929	209392	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	366	5	0	7	2.3	CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O	10.1016/j.bmcl.2009.11.008
	CHEMBL612133	209392	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	366	5	0	7	2.3	CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O	10.1016/j.bmcl.2009.11.008
	68109379	164004	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4076286	164004	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	24815434	206475	0	None	-5	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593196	206475	0	None	-5	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225337	206756	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595151	206756	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225335	206826	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595608	206826	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24849789	206913	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596270	206913	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225569	208141	0	None	-12	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604467	208141	0	None	-12	2	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44591813	191438	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484972	191438	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	324	5	0	3	3.8	C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	11950742	73881	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL187398	73881	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	70685769	81390	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	405	5	0	5	5.3	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1	10.1021/jm2016864
	CHEMBL2029820	81390	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	405	5	0	5	5.3	Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1	10.1021/jm2016864
	155552204	180921	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	CHEMBL4546388	180921	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	305	2	0	3	3.4	Fc1ccccc1Cn1nnc2c(Br)cccc21	10.1021/acs.jmedchem.8b00161
	71136691	150399	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	CHEMBL3899706	150399	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	68109605	165169	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089955	165169	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	9815616	121578	6	None	-2	4	Rat	7.2	pEC50	=	7.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	121578	6	None	-2	4	Rat	7.2	pEC50	=	7.2	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	44155538	15280	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2cccc(F)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094134	15280	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2cccc(F)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155316	15470	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095749	15470	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	277	7	0	3	4.0	CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155420	15531	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2cccc(C)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096423	15531	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	261	6	0	2	4.3	CCCCCCC1CN(c2cccc(C)c2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	46227790	206870	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	375	4	0	7	2.9	CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	CHEMBL595966	206870	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	375	4	0	7	2.9	CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	70689924	81366	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029798	81366	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	359	6	0	5	4.6	CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O	10.1021/jm2016864
	162665242	188887	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	4	5.3	Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl	10.1016/j.ejmech.2019.111881
	CHEMBL4781971	188887	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	4	5.3	Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl	10.1016/j.ejmech.2019.111881
	11951987	75007	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC	10.1016/j.bmcl.2005.06.017
	CHEMBL191579	75007	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	433	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC	10.1016/j.bmcl.2005.06.017
	46887320	15766	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098389	15766	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	283	4	0	3	3.4	Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1	10.1016/j.bmcl.2010.03.089
	118714739	121340	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	350	5	0	5	3.1	CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337505	121340	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	350	5	0	5	3.1	CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	46197778	14990	0	None	-6	5	Rat	5.2	pEC50	=	5.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	237	6	4	4	-0.3	N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O	10.1021/jm901523t
	CHEMBL1092243	14990	0	None	-6	5	Rat	5.2	pEC50	=	5.2	Functional	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader	ChEMBL	237	6	4	4	-0.3	N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O	10.1021/jm901523t
	11626305	73428	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	437	10	1	5	5.7	CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185290	73428	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	437	10	1	5	5.7	CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O	10.1016/j.bmcl.2004.09.028
	44428731	149925	0	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL389585	149925	0	None	-	1	Rat	4.2	pEC50	=	4.2	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	11575058	72375	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL183304	72375	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	118714755	121355	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337521	121355	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	369	4	0	4	3.8	N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	155550797	181899	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4569581	181899	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1	10.1021/acs.jmedchem.8b00161
	59599538	151823	0	None	-1	2	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3911282	151823	0	None	-1	2	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	445	9	2	8	4.5	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2016.11.049
	71136653	130181	0	None	51	2	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616854	130181	0	None	51	2	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	57459475	89426	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	331	3	0	5	3.5	CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	CHEMBL2179329	89426	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	331	3	0	5	3.5	CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12	10.1021/jm3010724
	1393	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	1396	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	213056	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	CHEMBL8759	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	1393	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1396	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	213056	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	CHEMBL8759	8321	64	None	2	6	Human	8.2	pEC50	=	8.2	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	156817932	198853	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5202739	198853	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	60096224	163324	0	None	-43	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068189	163324	0	None	-43	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71461395	90682	1	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206445	90682	1	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	23725156	68733	0	None	-	1	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	357	3	0	3	4.7	Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL1774107	68733	0	None	-	1	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	357	3	0	3	4.7	Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1021/jm101414h
	49801370	163814	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4073628	163814	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	90098428	130183	0	None	60	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616856	130183	0	None	60	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	25173616	191273	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL484731	191273	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	156010124	183810	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	183810	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	156010124	183810	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4632373	183810	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	44591773	191039	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	3	0	2	4.0	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL483751	191039	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	303	3	0	2	4.0	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	162662443	188790	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	369	6	0	4	4.0	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4780663	188790	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	369	6	0	4	4.0	O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1	10.1016/j.ejmech.2019.111881
	162675793	190194	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	375	5	0	4	4.6	Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	CHEMBL4798495	190194	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	375	5	0	4	4.6	Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl	10.1016/j.ejmech.2019.111881
	155546950	180438	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	320	3	0	4	4.2	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4534604	180438	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	320	3	0	4	4.2	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1	10.1021/acs.jmedchem.8b00161
	155565811	182399	1	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	269	2	0	3	2.7	Fc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4580525	182399	1	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	269	2	0	3	2.7	Fc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	146036861	182828	6	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	251	2	0	3	2.6	Brc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4590535	182828	6	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	251	2	0	3	2.6	Brc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	155549028	180576	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	3	0	3	4.4	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4538026	180576	0	None	-	1	Human	7.2	pEC50	=	7.2	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	321	3	0	3	4.4	Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1	10.1021/acs.jmedchem.8b00161
	71460259	87575	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	434	4	1	5	5.2	N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	CHEMBL2152108	87575	0	None	-	1	Human	6.2	pEC50	=	6.2	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	434	4	1	5	5.2	N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12	10.1021/jm201561r
	44155535	15279	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccccc2F)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1094133	15279	0	None	-	1	Human	5.2	pEC50	=	5.2	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccccc2F)C(=O)O1	10.1016/j.bmcl.2010.03.089
	134130007	148969	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	391	6	0	6	4.4	Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3884042	148969	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay	ChEMBL	391	6	0	6	4.4	Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	44428731	149925	0	None	-	1	Rat	4.1	pEC50	=	4.1	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	CHEMBL389585	149925	0	None	-	1	Rat	4.1	pEC50	=	4.1	Functional	Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	199	4	3	5	0.2	CCCc1c(C(N)C(=O)O)cnn1O	10.1016/j.bmc.2007.02.047
	68107827	199263	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5208947	199263	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	155535327	178794	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	281	3	0	4	2.6	COc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4471540	178794	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	281	3	0	4	2.6	COc1cc(Br)c2nnn(CC3CC3)c2c1	10.1021/acs.jmedchem.8b00161
	71136654	130186	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616859	130186	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	57459636	89407	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	357	4	0	5	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179309	89407	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	357	4	0	5	3.9	N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	66786816	165135	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4089612	165135	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	162675603	190075	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	6	0	4	4.8	FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4796990	190075	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	6	0	4	4.8	FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	54580322	68748	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	402	3	0	4	5.0	Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21	10.1021/jm101414h
	CHEMBL1774226	68748	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	402	3	0	4	5.0	Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21	10.1021/jm101414h
	25173691	195787	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL508821	195787	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	317	5	0	3	4.4	CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	162643509	188448	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	CHEMBL4776355	188448	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	295	3	0	3	3.2	Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	11951986	131097	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	445	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1	10.1016/j.bmcl.2005.06.017
	CHEMBL363531	131097	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	445	12	1	6	5.4	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1	10.1016/j.bmcl.2005.06.017
	44591792	200149	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL525075	200149	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	268	3	0	3	3.1	C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	168298153	199518	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	421	6	0	4	5.8	FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	CHEMBL5220484	199518	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	421	6	0	4	5.8	FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.2c00969
	25173778	191692	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL485329	191692	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	301	3	0	2	4.3	C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	51357936	68751	0	None	-3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	CHEMBL1774231	68751	0	None	-3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C	10.1021/jm101414h
	44155747	15469	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095746	15469	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	272	6	0	3	3.9	CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	11951991	140700	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	12	1	6	5.7	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL371578	140700	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	447	12	1	6	5.7	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C	10.1016/j.bmcl.2005.06.017
	66786131	163945	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075417	163945	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	11510036	73002	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL184531	73002	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	11952169	74304	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	459	10	1	6	5.8	CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189623	74304	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	459	10	1	6	5.8	CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	24815976	206538	0	None	5	2	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	CHEMBL593745	206538	0	None	5	2	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1021/jm101414h
	46887418	15771	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1098406	15771	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	337	4	0	3	4.1	O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	22368592	15524	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1096318	15524	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	263	6	1	3	3.7	CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	51354014	68752	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C	10.1021/jm101414h
	CHEMBL1774232	68752	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	418	4	0	5	4.6	COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C	10.1021/jm101414h
	11952347	74208	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	7	5.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12	10.1016/j.bmcl.2005.06.017
	CHEMBL188977	74208	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	463	11	1	7	5.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12	10.1016/j.bmcl.2005.06.017
	155518831	177138	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	353	3	0	3	5.5	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4447550	177138	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	353	3	0	3	5.5	Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1	10.1021/acs.jmedchem.8b00161
	CHEMBL5093066	222184	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL		None	None	None		Cn1c(CN2CCN(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ncccc21	10.1021/acs.jmedchem.1c00563
	156019582	184790	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	184790	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	59234231	8924	4	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6330	8924	4	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6331	8924	4	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	CHEMBL3337510	8924	4	None	-1	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	156019582	184790	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646555	184790	0	None	2	2	Human	7.1	pEC50	=	7.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	382	4	1	5	4.4	Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	67060124	173556	0	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	388	4	0	5	3.8	O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2	10.1016/j.bmcl.2018.08.022
	CHEMBL4283963	173556	0	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis	ChEMBL	388	4	0	5	3.8	O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2	10.1016/j.bmcl.2018.08.022
	46887272	15463	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	233	5	0	2	3.6	CCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095702	15463	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	233	5	0	2	3.6	CCCCCC1CN(c2ccccc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	44155540	15499	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	CHEMBL1095970	15499	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	265	6	0	2	4.1	CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1	10.1016/j.bmcl.2010.03.089
	53322148	64504	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	342	6	0	4	4.1	CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669386	64504	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	342	6	0	4	4.1	CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53326075	64507	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	383	4	0	5	4.0	CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669389	64507	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	383	4	0	5	4.0	CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53322149	64509	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	4	0	4	4.1	CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669390	64509	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	328	4	0	4	4.1	CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O	10.1016/j.bmcl.2010.12.048
	53324152	64520	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	264	3	0	3	3.5	CCCn1ccc2cc(-c3cccnc3)ccc2c1=O	10.1016/j.bmcl.2010.12.048
	CHEMBL1669402	64520	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay	ChEMBL	264	3	0	3	3.5	CCCn1ccc2cc(-c3cccnc3)ccc2c1=O	10.1016/j.bmcl.2010.12.048
	10176324	121605	1	None	4	4	Rat	8.1	pEC50	=	8.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	173	3	3	3	-0.6	C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O	10.1021/jm030967o
	CHEMBL334160	121605	1	None	4	4	Rat	8.1	pEC50	=	8.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	173	3	3	3	-0.6	C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O	10.1021/jm030967o
	57459488	90678	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206441	90678	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	68107827	199263	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5208947	199263	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	467	5	0	5	4.8	Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.2c00593
	60096178	163660	0	None	-10	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4071962	163660	0	None	-10	2	Human	8.1	pEC50	=	8.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	156018381	184701	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	184701	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	70209638	164388	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4080973	164388	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	156018381	184701	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	CHEMBL4645305	184701	0	None	-	1	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1	10.1021/acs.jmedchem.0c01058
	146036869	182516	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	287	2	0	3	3.2	Brc1cccc2c1nnn2Cc1ccccc1	10.1021/acs.jmedchem.8b00161
	CHEMBL4583006	182516	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	287	2	0	3	3.2	Brc1cccc2c1nnn2Cc1ccccc1	10.1021/acs.jmedchem.8b00161
	162657401	187885	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	CHEMBL4760211	187885	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1016/j.ejmech.2019.111881
	162657401	187885	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1021/acs.jmedchem.1c00563
	CHEMBL4760211	187885	3	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis	ChEMBL	355	3	0	3	3.9	Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1	10.1021/acs.jmedchem.1c00563
	118714747	121347	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337513	121347	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	51354020	68756	0	None	-23	2	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774236	68756	0	None	-23	2	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	422	4	0	5	4.6	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F	10.1021/jm101414h
	11495483	73441	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL185392	73441	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	421	9	1	5	6.2	Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	49822116	153770	13	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL3926416	153770	13	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	46830123	7859	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	6321	7859	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	CHEMBL1094763	7859	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	10.1016/j.bmcl.2010.03.089
	44450470	102861	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	CHEMBL260122	102861	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	70685765	81378	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	CHEMBL2029808	81378	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	357	5	0	5	4.3	Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1	10.1021/jm2016864
	156817932	198853	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	CHEMBL5202739	198853	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay	ChEMBL	465	4	0	5	4.1	O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1	10.1021/acs.jmedchem.2c00593
	25173697	179465	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	CHEMBL450076	179465	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	285	3	0	2	3.8	C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1	10.1016/j.bmcl.2009.03.032
	46887417	15716	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	CHEMBL1097984	15716	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay	ChEMBL	303	4	0	3	3.7	O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1	10.1016/j.bmcl.2010.03.089
	44450470	102861	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	CHEMBL260122	102861	1	None	-1	2	Rat	4.1	pEC50	=	4.1	Functional	Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation	ChEMBL	160	2	3	4	-0.9	N[C@H](C(=O)O)[C@H]1CC(O)=NO1	10.1021/jm701394a
	58081135	87587	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	383	2	1	2	5.9	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12	10.1021/jm201561r
	CHEMBL2152121	87587	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis	ChEMBL	383	2	1	2	5.9	FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12	10.1021/jm201561r
	1310	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	1369	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	33032	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	44272391	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	88747398	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	CHEMBL575060	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	DB00142	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm9602569
	46226952	206630	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	387	3	0	7	2.4	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	CHEMBL594386	206630	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	387	3	0	7	2.4	N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12	10.1016/j.bmcl.2009.11.008
	66612837	81355	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029786	81355	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm2016864
	66612837	81355	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL2029786	81355	0	None	-	1	Human	5.1	pEC50	=	5.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	266	4	0	3	3.4	CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O	10.1021/jm500496m
	155553087	180883	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1	10.1021/acs.jmedchem.8b00161
	CHEMBL4545027	180883	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	356	3	0	4	4.5	Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1	10.1021/acs.jmedchem.8b00161
	51356569	68728	2	None	10	3	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1021/jm101414h
	CHEMBL1774101	68728	2	None	10	3	Rat	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1021/jm101414h
	168299005	199533	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O	10.1021/acs.jmedchem.2c00969
	CHEMBL5221091	199533	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding	ChEMBL	372	7	0	6	3.8	CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O	10.1021/acs.jmedchem.2c00969
	66785182	163957	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075593	163957	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	59599545	153937	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	CHEMBL3927834	153937	0	None	3	2	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay	ChEMBL	437	7	2	8	4.2	CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O	10.1016/j.bmcl.2016.11.049
	71136655	130179	0	None	12	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616852	130179	0	None	12	2	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	51356569	68728	2	None	-10	3	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1016/j.ejmech.2019.111881
	CHEMBL1774101	68728	2	None	-10	3	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	335	4	0	4	4.0	COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1	10.1016/j.ejmech.2019.111881
	118714736	121336	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	321	4	0	4	3.3	CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337501	121336	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	321	4	0	4	3.3	CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O	10.1021/jm500496m
	11951447	74258	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL189290	74258	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	495	9	1	6	7.2	CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	44591712	191091	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	318	5	0	4	3.8	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	CHEMBL484178	191091	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	318	5	0	4	3.8	CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1	10.1016/j.bmcl.2009.03.032
	118714749	121349	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	CHEMBL3337515	121349	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	351	4	0	4	3.7	N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O	10.1021/jm500496m
	44392645	72018	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	CHEMBL182715	72018	0	None	-	1	Human	6.1	pEC50	=	6.1	Functional	Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay	ChEMBL	407	8	1	5	6.1	Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.09.028
	54584258	68726	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	456	5	0	6	3.3	COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1	10.1021/jm101414h
	CHEMBL1774099	68726	0	None	-	1	Rat	6.1	pEC50	=	6.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	456	5	0	6	3.3	COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1	10.1021/jm101414h
	137634033	163420	0	None	-1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4069251	163420	0	None	-1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	51357937	68753	0	None	-2	2	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774233	68753	0	None	-2	2	Rat	8.1	pEC50	=	8.1	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	156018305	184613	0	None	89	2	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	184613	0	None	89	2	Human	8.1	pEC50	=	8.1	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	156018305	184613	0	None	89	2	Human	8.0	pEC50	=	8.0	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4643961	184613	0	None	89	2	Human	8.0	pEC50	=	8.0	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	440	8	0	6	4.7	COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/acs.jmedchem.0c01058
	69093344	90683	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206446	90683	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	66786493	166458	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4104081	166458	0	None	-	1	Human	8.0	pEC50	=	8.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	156020355	184807	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	CHEMBL4646835	184807	0	None	104	2	Human	8.0	pEC50	=	8	Functional	Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay	ChEMBL	396	5	0	5	4.7	COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1	10.1021/acs.jmedchem.0c01058
	6604805	209467	2	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	195	3	3	3	-0.6	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F	10.1021/jm030967o
	CHEMBL61605	209467	2	None	-	1	Rat	7.1	pEC50	=	7.1	Functional	Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells	ChEMBL	195	3	3	3	-0.6	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F	10.1021/jm030967o
	162659759	188090	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	CHEMBL4762556	188090	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	359	5	0	4	4.3	Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F	10.1016/j.ejmech.2019.111881
	162662067	188188	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	349	6	0	4	3.7	Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O	10.1016/j.ejmech.2019.111881
	CHEMBL4763686	188188	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	349	6	0	4	3.7	Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O	10.1016/j.ejmech.2019.111881
	162662384	188831	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	5	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1	10.1016/j.ejmech.2019.111881
	CHEMBL4781222	188831	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	389	5	0	4	4.3	O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1	10.1016/j.ejmech.2019.111881
	155518472	177084	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	207	2	0	3	2.5	Clc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	CHEMBL4446625	177084	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay	ChEMBL	207	2	0	3	2.5	Clc1cccc2c1nnn2CC1CC1	10.1021/acs.jmedchem.8b00161
	156017237	184540	0	None	1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	184540	0	None	1	2	Human	6.1	pEC50	=	6.1	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156017237	184540	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	CHEMBL4642761	184540	0	None	1	2	Human	6.0	pEC50	=	6.0	Functional	Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay	ChEMBL	853	21	0	11	8.5	COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1	10.1021/acs.jmedchem.0c01058
	156817945	197263	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	CHEMBL5179002	197263	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1	10.1021/acs.jmedchem.2c00593
	3954	7451	60	None	6	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	9868580	7451	60	None	6	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL593013	7451	60	None	6	2	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	66784262	165010	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4088239	165010	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	70694132	81386	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O	10.1021/jm2016864
	CHEMBL2029816	81386	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting	ChEMBL	393	6	0	5	5.3	CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O	10.1021/jm2016864
	11655609	172680	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL424998	172680	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C	ChEMBL	463	11	1	8	4.8	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	1395	9306	15	None	-7	4	Rat	7.0	pEC50	=	7.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	9306	15	None	-7	4	Rat	7.0	pEC50	=	7.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	9306	15	None	-7	4	Rat	7.0	pEC50	=	7.0	Functional	Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	57459512	89416	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	367	4	0	5	3.7	Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	CHEMBL2179318	89416	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay	ChEMBL	367	4	0	5	3.7	Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/jm3010724
	118714742	121343	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	5	0	4	3.9	CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	CHEMBL3337508	121343	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	335	5	0	4	3.9	CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O	10.1021/jm500496m
	71117214	157886	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	446	4	0	8	2.1	Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1	nan
	CHEMBL3959189	157886	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	446	4	0	8	2.1	Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1	nan
	44591770	199097	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	CHEMBL520639	199097	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	311	5	0	3	4.1	CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1	10.1016/j.bmcl.2009.03.032
	68109333	166171	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4100691	166171	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	162649465	186844	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	3	5.0	Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	CHEMBL4747874	186844	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay	ChEMBL	391	5	0	3	5.0	Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1	10.1016/j.ejmech.2019.111881
	46226930	208696	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.5	CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	CHEMBL607518	208696	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay	ChEMBL	345	4	0	5	3.5	CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12	10.1016/j.bmcl.2009.11.008
	118714754	121354	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1	10.1021/jm500496m
	CHEMBL3337520	121354	0	None	-	1	Human	7.0	pEC50	=	7.0	Functional	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins	ChEMBL	363	5	0	5	3.5	COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1	10.1021/jm500496m
	11950553	74069	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	CHEMBL188286	74069	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr	ChEMBL	462	11	1	7	5.5	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C	10.1016/j.bmcl.2005.06.017
	71117402	157210	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	532	5	1	6	5.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21	nan
	CHEMBL3953950	157210	0	None	-	1	Human	6.0	pEC50	=	6.0	Functional	Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).	ChEMBL	532	5	1	6	5.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21	nan
	51354017	68754	0	None	-	1	Rat	6.0	pEC50	=	6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	CHEMBL1774234	68754	0	None	-	1	Rat	6.0	pEC50	=	6	Functional	Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay	ChEMBL	406	3	0	4	4.8	C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F	10.1021/jm101414h
	131636309	166824	0	None	-	1	Human	9.0	pIC50	=	9.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	445	4	0	5	5.6	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4108184	166824	0	None	-	1	Human	9.0	pIC50	=	9.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	445	4	0	5	5.6	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636462	166948	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	4.8	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	CHEMBL4109246	166948	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	4.8	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	131636310	167325	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	4	0	5	5.3	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4112479	167325	0	None	-	1	Human	8.8	pIC50	=	8.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	4	0	5	5.3	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636389	166885	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4108743	166885	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636463	167089	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4110543	167089	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	78319942	166959	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4109319	166959	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636453	167349	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112624	167349	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	11484819	63080	0	None	-2	2	Human	8.0	pIC50	=	8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629863	63080	0	None	-2	2	Human	8.0	pIC50	=	8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	44450479	103038	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261050	103038	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	9909080	162061	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL402886	162061	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22317744	63061	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629844	63061	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	22317767	63064	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629847	63064	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11235624	63079	0	None	-1	3	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	63079	0	None	-1	3	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317431	63187	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631864	63187	0	None	-	1	Rat	8.0	pIC50	=	8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	78324632	167032	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4110016	167032	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	78320556	167436	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	CHEMBL4113304	167436	0	None	-	1	Human	8.0	pIC50	=	8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	131636370	166657	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106787	166657	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636447	167522	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113943	167522	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636434	158152	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC	nan
	CHEMBL3961419	158152	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC	nan
	131636342	149671	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1	nan
	CHEMBL3893630	149671	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1	nan
	76318479	112880	0	None	-	1	Human	7.0	pIC50	=	7	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	446	6	1	5	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1	10.1039/C3MD00110E
	CHEMBL3133886	112880	0	None	-	1	Human	7.0	pIC50	=	7	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	446	6	1	5	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1	10.1039/C3MD00110E
	131636402	167203	0	None	-	1	Human	7.0	pIC50	=	7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	CHEMBL4111387	167203	0	None	-	1	Human	7.0	pIC50	=	7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	10778385	85514	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	269	6	3	4	1.2	NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112581	85514	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	269	6	3	4	1.2	NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10826383	85517	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	277	7	3	3	1.5	NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112584	85517	0	None	-1	2	Human	6.0	pIC50	=	6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	277	7	3	3	1.5	NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	44348769	23553	0	None	-3	2	Human	6.0	pIC50	=	6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	279	6	4	4	0.8	N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL124483	23553	0	None	-3	2	Human	6.0	pIC50	=	6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	279	6	4	4	0.8	N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	49858118	7894	0	None	10	2	Human	6.0	pIC50	=	6	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	6224	7894	0	None	10	2	Human	6.0	pIC50	=	6	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	CHEMBL1630807	7894	0	None	10	2	Human	6.0	pIC50	=	6	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	11269030	63078	0	None	-1	3	Rat	7.0	pIC50	=	7	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	63078	0	None	-1	3	Rat	7.0	pIC50	=	7	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	155550334	181076	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550009	181076	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155550334	181076	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550009	181076	0	None	-	1	Rat	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	449	5	1	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	131636325	167467	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113523	167467	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	155559601	181634	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563183	181634	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155566989	182656	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4586203	182656	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155559601	181634	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563183	181634	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	405	4	1	4	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155566989	182656	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4586203	182656	0	None	-	1	Rat	6.0	pIC50	=	6.0	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1	10.1021/acs.jmedchem.8b01266
	131636415	166664	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	463	7	1	7	3.9	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4106864	166664	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	463	7	1	7	3.9	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	9845873	167578	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL411440	167578	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	9845873	167578	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL411440	167578	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22224657	102947	0	None	2	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260636	102947	0	None	2	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9952648	103083	0	None	1	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	103083	0	None	1	2	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	11474913	63181	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631858	63181	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9845873	167578	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	167578	0	None	-	1	Rat	8.0	pIC50	=	8.0	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	90354590	152459	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3916087	152459	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	90354676	167178	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4111258	167178	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	131636304	167390	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1	nan
	CHEMBL4112952	167390	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1	nan
	131636458	167290	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112214	167290	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	10515174	85506	0	None	1	2	Human	6.0	pIC50	=	6.0	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	255	5	3	3	1.5	NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112574	85506	0	None	1	2	Human	6.0	pIC50	=	6.0	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	255	5	3	3	1.5	NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	44272296	72966	1	None	-	1	Rat	5.0	pIC50	=	5.0	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	245	4	4	3	0.4	C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O	10.1016/S0960-894X(97)00177-7
	CHEMBL18439	72966	1	None	-	1	Rat	5.0	pIC50	=	5.0	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	245	4	4	3	0.4	C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O	10.1016/S0960-894X(97)00177-7
	90643971	118778	0	None	-1	2	Rat	6.0	pIC50	=	6.0	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288667	118778	0	None	-1	2	Rat	6.0	pIC50	=	6.0	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	134138062	154278	0	None	-1	2	Human	6.0	pIC50	=	6.0	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	374	5	4	5	0.9	N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3930511	154278	0	None	-1	2	Human	6.0	pIC50	=	6.0	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	374	5	4	5	0.9	N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	162658781	190470	0	None	1	2	Human	6.9	pIC50	=	6.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4759209	190470	0	None	1	2	Human	6.9	pIC50	=	6.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803105	190470	0	None	1	2	Human	6.9	pIC50	=	6.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	18548766	102638	0	None	-	1	Rat	6.9	pIC50	=	6.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259053	102638	0	None	-	1	Rat	6.9	pIC50	=	6.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	131636289	167508	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	CHEMBL4113819	167508	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	22224854	102159	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256812	102159	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	131636351	157276	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F	nan
	CHEMBL3954434	157276	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F	nan
	90354488	167715	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	CHEMBL4115442	167715	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	131636294	166802	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108019	166802	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	67705089	159034	0	None	1	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3969063	159034	0	None	1	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	90367533	166862	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4108547	166862	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	131636379	167523	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113948	167523	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	3	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	137635882	162673	0	None	1	2	Human	4.9	pIC50	=	4.9	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4060567	162673	0	None	1	2	Human	4.9	pIC50	=	4.9	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	162644419	190401	0	None	186	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4778355	190401	0	None	186	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802356	190401	0	None	186	2	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	22448689	104331	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL270616	104331	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	11281280	63182	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	63182	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	90354550	166721	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107291	166721	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636419	154886	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1	nan
	CHEMBL3935209	154886	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1	nan
	131636316	166671	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4106929	166671	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	78324633	167360	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4112706	167360	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636296	167633	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4114910	167633	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354846	166787	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4107888	166787	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	131636366	167019	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4109916	167019	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636405	166908	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108937	166908	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354352	151503	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3908808	151503	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	76318478	112877	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1	10.1039/C3MD00110E
	CHEMBL3133883	112877	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1	10.1039/C3MD00110E
	44328753	214533	0	None	-45	6	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	8	3	4	4.2	CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL95868	214533	0	None	-45	6	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	8	3	4	4.2	CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	76336598	112878	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1	10.1039/C3MD00110E
	CHEMBL3133884	112878	0	None	-	1	Human	6.9	pIC50	=	6.9	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	504	3	1	4	5.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1	10.1039/C3MD00110E
	44329033	214759	0	None	-34	5	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	7	3	4	4.1	CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL97200	214759	0	None	-34	5	Rat	5.9	pIC50	=	5.9	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	409	7	3	4	4.1	CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	90643959	118770	0	None	-1	2	Rat	5.9	pIC50	=	5.9	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	460	4	1	7	3.2	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	CHEMBL3288646	118770	0	None	-1	2	Rat	5.9	pIC50	=	5.9	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	460	4	1	7	3.2	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	11158623	10124	11	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	6226	10124	11	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	CHEMBL1629855	10124	11	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	10115228	102948	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260642	102948	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	53324715	63193	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631870	63193	0	None	-	1	Rat	7.9	pIC50	=	7.9	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636423	166813	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	471	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	CHEMBL4108112	166813	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	471	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	122580887	167285	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112158	167285	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636280	166645	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106725	166645	0	None	-	1	Human	7.9	pIC50	=	7.9	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636375	167695	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4115306	167695	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	10710505	85513	0	None	-1	2	Human	5.9	pIC50	=	5.9	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	316	6	3	4	1.6	Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21	10.1021/jm970497w
	CHEMBL2112580	85513	0	None	-1	2	Human	5.9	pIC50	=	5.9	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	316	6	3	4	1.6	Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21	10.1021/jm970497w
	155526616	177914	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	CHEMBL4458387	177914	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	155530126	178247	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4463498	178247	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155526616	177914	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	CHEMBL4458387	177914	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	5	1	5	3.0	CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1	10.1021/acs.jmedchem.8b01266
	155530126	178247	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4463498	178247	0	None	-	1	Rat	5.9	pIC50	=	5.9	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	401	5	1	6	3.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	162654849	190449	0	None	-1	2	Human	5.8	pIC50	=	5.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4755204	190449	0	None	-1	2	Human	5.8	pIC50	=	5.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802906	190449	0	None	-1	2	Human	5.8	pIC50	=	5.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	155550549	181887	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4569114	181887	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155550549	181887	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4569114	181887	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	134139744	152737	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3918170	152737	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	11442010	63083	0	None	-5	3	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629866	63083	0	None	-5	3	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	18548908	103039	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261051	103039	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	9891158	162365	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL404463	162365	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	22317918	63074	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629858	63074	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	131636418	167366	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	4	5.7	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4112763	167366	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	4	5.7	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636410	167607	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	CHEMBL4114609	167607	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	131636388	167138	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4110884	167138	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636353	167705	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4115388	167705	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636385	167571	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	6	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4114364	167571	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	6	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	49858117	7875	4	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	6223	7875	4	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	CHEMBL1630806	7875	4	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	155566841	182639	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4585786	182639	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	155566841	182639	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4585786	182639	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	382	5	1	6	3.5	Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1	10.1021/acs.jmedchem.8b01266
	71681826	96836	0	None	-1	3	Human	4.8	pIC50	=	4.8	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381651	96836	0	None	-1	3	Human	4.8	pIC50	=	4.8	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	90643958	118769	0	None	-6	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288644	118769	0	None	-6	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12	10.1016/j.bmcl.2014.04.051
	22224970	162271	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404080	162271	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	22317715	63071	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629854	63071	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	53326017	63195	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631872	63195	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636403	166674	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106954	166674	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636317	167354	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4112663	167354	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	69669747	190432	11	None	-2	4	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4751065	190432	11	None	-2	4	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802733	190432	11	None	-2	4	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	90354858	166643	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	CHEMBL4106716	166643	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	67705326	160027	0	None	2	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	457	7	4	6	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3977508	160027	0	None	2	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	457	7	4	6	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	131636349	152010	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3912677	152010	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636444	166656	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.6	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4106785	166656	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.6	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	131636315	167308	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4112341	167308	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	22317185	63065	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629848	63065	0	None	-	1	Rat	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	44345358	120127	0	None	1	2	Human	5.8	pIC50	=	5.8	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	215	5	3	3	0.5	CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL331753	120127	0	None	1	2	Human	5.8	pIC50	=	5.8	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	215	5	3	3	0.5	CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970497w
	10456810	114656	0	None	-13	5	Rat	5.8	pIC50	=	5.8	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	457	8	3	4	4.7	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL319279	114656	0	None	-13	5	Rat	5.8	pIC50	=	5.8	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	457	8	3	4	4.7	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O	10.1016/s0960-894x(98)00510-1
	134132133	151567	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3909237	151567	0	None	-1	2	Human	6.8	pIC50	=	6.8	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	44450391	175614	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL437835	175614	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9820321	161787	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL401446	161787	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	135544097	162444	0	None	269	2	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404886	162444	0	None	269	2	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	9820321	161787	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL401446	161787	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	67633340	190500	0	None	1	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4780402	190500	0	None	1	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803381	190500	0	None	1	2	Human	7.8	pIC50	=	7.8	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	131636443	166625	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	6	0	5	5.5	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	CHEMBL4106566	166625	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	6	0	5	5.5	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	131636400	166780	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	CHEMBL4107829	166780	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	131636337	159454	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3972702	159454	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636401	167174	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	CHEMBL4111225	167174	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	11503055	9179	3	None	-31	2	Human	4.8	pIC50	=	4.8	Functional	Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1021/jm400439t
	9694	9179	3	None	-31	2	Human	4.8	pIC50	=	4.8	Functional	Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1021/jm400439t
	CHEMBL2204436	9179	3	None	-31	2	Human	4.8	pIC50	=	4.8	Functional	Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1021/jm400439t
	155538435	179146	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4476138	179146	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155539352	179614	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4514334	179614	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155562175	182603	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4584801	182603	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155539352	179614	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4514334	179614	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	369	4	1	4	4.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155562175	182603	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4584801	182603	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	361	5	1	5	2.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155538435	179146	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4476138	179146	0	None	-	1	Rat	5.8	pIC50	=	5.8	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	447	5	1	5	5.2	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	11298568	76150	1	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	CHEMBL192977	76150	1	None	5	2	Human	5.8	pIC50	=	5.8	Functional	Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	90643974	118780	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288675	118780	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	90643963	118772	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	366	2	0	5	4.2	Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	CHEMBL3288653	118772	0	None	-3	2	Rat	5.8	pIC50	=	5.8	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	366	2	0	5	4.2	Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	22224670	103042	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261081	103042	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	53316736	63058	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629715	63058	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	22317847	63184	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631861	63184	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11212447	63191	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631868	63191	0	None	-	1	Rat	7.8	pIC50	=	7.8	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636450	167417	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113175	167417	0	None	-	1	Human	7.8	pIC50	=	7.8	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	1	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636373	166637	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106692	166637	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636397	166762	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4107640	166762	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F	nan
	131636360	157027	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3952383	157027	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636427	167460	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4113474	167460	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	67707808	155421	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	432	6	4	6	1.3	COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3939492	155421	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	432	6	4	6	1.3	COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	131636372	166989	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	CHEMBL4109618	166989	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	0	6	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	131636299	167049	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	CHEMBL4110209	167049	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	10492773	23557	0	None	-2	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	277	6	3	3	1.4	Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL124501	23557	0	None	-2	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	277	6	3	3	1.4	Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	44348993	121363	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	297	6	3	3	1.8	N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL333771	121363	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	297	6	3	3	1.8	N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	44348706	123660	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	281	6	3	3	1.3	N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL338282	123660	0	None	1	2	Human	6.8	pIC50	=	6.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	281	6	3	3	1.3	N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	10828532	85540	0	None	-22	2	Human	5.8	pIC50	=	5.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	307	7	4	4	0.8	NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL2112634	85540	0	None	-22	2	Human	5.8	pIC50	=	5.8	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	307	7	4	4	0.8	NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	10359073	161753	1	None	-1	2	Human	4.8	pIC50	=	4.8	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	CHEMBL40123	161753	1	None	-1	2	Human	4.8	pIC50	=	4.8	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	18613455	102825	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259924	102825	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	44329031	115051	0	None	-15	7	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	437	10	3	4	5.0	CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL319732	115051	0	None	-15	7	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	437	10	3	4	5.0	CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	18548739	167144	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL411095	167144	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	18548739	167144	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL411095	167144	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636333	160967	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3985799	160967	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636339	166915	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4108997	166915	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	131636378	167267	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4111987	167267	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	131636395	167281	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4112129	167281	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636373	166637	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106692	166637	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636407	166882	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	3	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4108700	166882	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	3	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636408	167539	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4114047	167539	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636329	151415	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C	nan
	CHEMBL3908089	151415	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C	nan
	131636284	167283	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112146	167283	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90354963	167425	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	4	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	CHEMBL4113235	167425	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	4	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	131636406	167155	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4111067	167155	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90355009	167028	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4109993	167028	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	86695984	156544	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	472	7	3	8	1.9	Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1016/j.bmcl.2016.10.067
	CHEMBL3948272	156544	0	None	1	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	472	7	3	8	1.9	Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1016/j.bmcl.2016.10.067
	53316798	63179	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631856	63179	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	44348846	123790	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	341	7	3	5	0.5	CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL2111822	123790	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	341	7	3	5	0.5	CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL338911	123790	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	341	7	3	5	0.5	CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	90643954	118767	0	None	-2	2	Rat	5.7	pIC50	=	5.7	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	430	3	1	6	3.2	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288636	118767	0	None	-2	2	Rat	5.7	pIC50	=	5.7	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	430	3	1	6	3.2	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	155523578	177687	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4454867	177687	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155523578	177687	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4454867	177687	0	None	-	1	Rat	5.7	pIC50	=	5.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	11304010	63081	0	None	2	3	Rat	8.7	pIC50	=	8.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629864	63081	0	None	2	3	Rat	8.7	pIC50	=	8.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	122580902	166784	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4107872	166784	0	None	-	1	Human	8.7	pIC50	=	8.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636451	166789	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107913	166789	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636422	166821	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	5	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4108163	166821	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	5	0	5	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	131636461	166903	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108918	166903	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78320558	167226	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4111659	167226	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90354985	167458	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	425	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113466	167458	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	425	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78319944	167510	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4113834	167510	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.0	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	78320252	167304	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	CHEMBL4112321	167304	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	411	4	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	90354835	167343	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112598	167343	0	None	-	1	Human	8.6	pIC50	=	8.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636455	167183	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4111276	167183	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636460	167258	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	CHEMBL4111924	167258	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C	nan
	1397	9307	15	None	1	8	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	9886034	9307	15	None	1	8	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL186453	9307	15	None	1	8	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	22317728	63063	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629846	63063	0	None	-	1	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566598	149468	15	None	1	3	Human	7.7	pIC50	=	7.7	Functional	Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	149468	15	None	1	3	Human	7.7	pIC50	=	7.7	Functional	Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	67637138	190397	0	None	2	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4776989	190397	0	None	2	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802329	190397	0	None	2	2	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	131636365	166774	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107737	166774	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636282	167358	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112692	167358	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	2	0	4	5.2	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636409	167240	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	6	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1	nan
	CHEMBL4111753	167240	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	467	6	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1	nan
	131636331	151678	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3910129	151678	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636297	166761	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4107635	166761	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	122580890	167255	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4111874	167255	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	3	0	4	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	10807972	42591	1	None	-12	4	Human	6.7	pIC50	=	6.7	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL144151	42591	1	None	-12	4	Human	6.7	pIC50	=	6.7	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	1378	9195	54	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	1399	9195	54	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	9819927	9195	54	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	CHEMBL432038	9195	54	None	-9	14	Rat	6.7	pIC50	=	6.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(98)00510-1
	10358265	108903	0	None	-2	2	Human	4.7	pIC50	=	4.7	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL302411	108903	0	None	-2	2	Human	4.7	pIC50	=	4.7	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1	10.1016/s0960-894x(98)00352-7
	162663798	190498	0	None	1	2	Human	5.7	pIC50	=	5.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4779554	190498	0	None	1	2	Human	5.7	pIC50	=	5.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4803378	190498	0	None	1	2	Human	5.7	pIC50	=	5.7	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	1378	9195	54	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	1399	9195	54	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	9819927	9195	54	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	CHEMBL432038	9195	54	None	-2	14	Human	7.7	pIC50	=	7.7	Functional	Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmcl.2012.01.039
	131636435	155169	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	5	0	5	4.5	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC	nan
	CHEMBL3937514	155169	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	5	0	5	4.5	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC	nan
	131636361	167453	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113439	167453	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636283	167563	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4114284	167563	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	131636454	166744	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4107497	166744	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636290	167278	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112105	167278	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	122580905	166845	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108383	166845	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636285	167726	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.2	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4115529	167726	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.2	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	134154496	159289	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3971347	159289	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	134141510	153846	0	None	-2	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	339	5	4	5	0.1	Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1016/j.bmcl.2016.10.067
	CHEMBL3927108	153846	0	None	-2	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	339	5	4	5	0.1	Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1016/j.bmcl.2016.10.067
	44329029	170300	0	None	2	6	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	479	13	3	4	6.2	CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL420262	170300	0	None	2	6	Rat	5.7	pIC50	=	5.7	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	479	13	3	4	6.2	CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	9952648	103083	0	None	1	2	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261288	103083	0	None	1	2	Rat	7.7	pIC50	=	7.7	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	118906265	152726	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	CHEMBL3918111	152726	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	131636314	166820	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4108162	166820	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636448	167319	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112439	167319	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636346	159279	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	CHEMBL3971278	159279	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	131636369	167596	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4114534	167596	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636276	152685	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	CHEMBL3917816	152685	0	None	-	1	Human	7.7	pIC50	=	7.7	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	383	3	0	5	4.5	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	90367528	150859	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	CHEMBL3903357	150859	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl	nan
	44348911	23338	0	None	1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	331	6	3	3	2.1	N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL123847	23338	0	None	1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	331	6	3	3	2.1	N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O	10.1021/jm970498o
	10688450	23376	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL124078	23376	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	155547618	180365	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4533083	180365	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155547618	180365	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4533083	180365	0	None	-	1	Rat	6.7	pIC50	=	6.7	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	441	5	1	6	3.4	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	134129940	149224	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	359	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3890112	149224	0	None	-1	2	Human	6.7	pIC50	=	6.7	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	359	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	162652146	186992	0	None	1	2	Human	5.6	pIC50	=	5.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4749728	186992	0	None	1	2	Human	5.6	pIC50	=	5.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	1378	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	1399	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	9819927	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	CHEMBL432038	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm970498o
	22224852	102639	0	None	-2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259054	102639	0	None	-2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	9845873	167578	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL411440	167578	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	9845873	167578	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	167578	0	None	-	1	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	131636382	167186	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	CHEMBL4111287	167186	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F	nan
	131636396	167020	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	3	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4109918	167020	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	3	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636301	167215	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4111566	167215	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	10852666	85516	0	None	1	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	313	6	3	3	2.3	NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112583	85516	0	None	1	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	313	6	3	3	2.3	NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10567792	85519	0	None	3	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	321	6	3	3	2.5	NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112586	85519	0	None	3	2	Human	6.6	pIC50	=	6.6	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	321	6	3	3	2.5	NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	90355016	167481	0	None	-	1	Human	6.6	pIC50	=	6.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	1	6	3.7	COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4113592	167481	0	None	-	1	Human	6.6	pIC50	=	6.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	1	6	3.7	COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	86298614	118781	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288676	118781	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	86298614	118781	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288676	118781	0	None	-3	2	Rat	6.6	pIC50	=	6.6	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	353	2	0	6	3.3	Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	11211597	63082	0	None	-1	3	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629865	63082	0	None	-1	3	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636336	155443	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	378	2	0	5	4.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3939714	155443	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	378	2	0	5	4.3	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	131636311	159427	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	4	0	5	4.3	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl	nan
	CHEMBL3972441	159427	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	4	0	5	4.3	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl	nan
	131636326	167338	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112588	167338	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636323	154840	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3934756	154840	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1	nan
	131636298	166907	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4108936	166907	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1	nan
	122580894	167472	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113546	167472	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	4	5.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	155538978	179561	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4513332	179561	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155538978	179561	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4513332	179561	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	383	5	1	6	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155514808	176677	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4440771	176677	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155514808	176677	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4440771	176677	0	None	-	1	Rat	5.6	pIC50	=	5.6	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	409	6	1	6	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	11269030	63078	0	None	-1	3	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	63078	0	None	-1	3	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	131636328	155524	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3940380	155524	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	387	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636354	167129	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	392	2	0	5	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110789	167129	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	392	2	0	5	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	67705376	152117	0	None	-1	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	416	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3913414	152117	0	None	-1	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	416	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	69669820	190419	0	None	-2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4746125	190419	0	None	-2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802570	190419	0	None	-2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	131636374	166879	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108665	166879	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	90354688	167318	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112422	167318	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	1378	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	1399	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	9819927	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	CHEMBL432038	9195	54	None	-2	14	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	131636393	166851	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	4.9	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4108446	166851	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	4	4.9	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636442	167730	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	6	0	5	5.2	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	CHEMBL4115553	167730	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	6	0	5	5.2	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1	nan
	18613373	102949	0	None	-	1	Rat	6.6	pIC50	=	6.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260643	102949	0	None	-	1	Rat	6.6	pIC50	=	6.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	22224657	102947	0	None	2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260636	102947	0	None	2	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9952648	103083	0	None	1	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	103083	0	None	1	2	Rat	7.6	pIC50	=	7.6	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	131636338	154760	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3934173	154760	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	2	0	4	5.1	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	131636432	157069	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3952745	157069	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1	nan
	69669646	190458	0	None	2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4757159	190458	0	None	2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4802990	190458	0	None	2	2	Human	7.6	pIC50	=	7.6	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	131636367	153415	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	459	5	0	6	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3923457	153415	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	459	5	0	6	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636357	167484	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113614	167484	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	2	0	4	5.3	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354626	166642	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.7	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4106714	166642	0	None	-	1	Human	7.6	pIC50	=	7.6	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	401	4	0	5	4.7	COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	131636286	166675	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	6	4.6	COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106958	166675	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	6	4.6	COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636319	160841	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3984622	160841	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	134144441	157173	0	None	-1	2	Human	6.6	pIC50	=	6.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3953570	157173	0	None	-1	2	Human	6.6	pIC50	=	6.6	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	341	5	4	5	0.3	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	44329042	175862	0	None	-38	5	Rat	5.5	pIC50	=	5.5	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	381	6	3	4	3.5	CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	CHEMBL439775	175862	0	None	-38	5	Rat	5.5	pIC50	=	5.5	Functional	Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated	ChEMBL	381	6	3	4	3.5	CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O	10.1016/s0960-894x(98)00510-1
	155555318	181097	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550517	181097	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155555318	181097	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4550517	181097	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	6	1	7	2.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	131636300	166912	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	4	0	5	4.1	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	CHEMBL4108984	166912	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	4	0	5	4.1	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	131636399	167495	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	CHEMBL4113737	167495	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	1	6	4.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1	nan
	131636312	167083	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.9	C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1	nan
	CHEMBL4110503	167083	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	4	0	5	4.9	C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1	nan
	22224852	102639	0	None	-2	2	Rat	6.5	pIC50	=	6.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259054	102639	0	None	-2	2	Rat	6.5	pIC50	=	6.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	11158623	10124	11	None	1	4	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	6226	10124	11	None	1	4	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	CHEMBL1629855	10124	11	None	1	4	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	11484819	63080	0	None	2	2	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629863	63080	0	None	2	2	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	11406781	63199	0	None	-	1	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631876	63199	0	None	-	1	Rat	8.5	pIC50	=	8.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636376	167435	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4113300	167435	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	78319946	167711	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4115420	167711	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	4	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636324	166891	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108816	166891	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78320250	167241	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4111755	167241	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	78320247	167237	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4111744	167237	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78324635	167245	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4111773	167245	0	None	-	1	Human	8.5	pIC50	=	8.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636416	167674	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4115199	167674	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	4.9	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636417	166796	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	446	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4107975	166796	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	446	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636305	166864	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1	nan
	CHEMBL4108564	166864	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1	nan
	78319945	167121	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4110721	167121	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	6	4.7	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F	nan
	78319941	167721	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4115490	167721	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	131636446	167321	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4112442	167321	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.9	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	22317318	63198	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631875	63198	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636456	166647	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	1	6	4.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4106741	166647	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	5	1	6	4.0	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636412	166964	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	6	1	6	3.9	Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	CHEMBL4109387	166964	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	6	1	6	3.9	Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	131636306	158041	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl	nan
	CHEMBL3960280	158041	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl	nan
	15392101	107215	0	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/j.bmcl.2007.10.026
	CHEMBL290509	107215	0	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/j.bmcl.2007.10.026
	4694355	105515	36	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1016/S0960-894X(97)00177-7
	CHEMBL277961	105515	36	None	-	1	Rat	4.5	pIC50	=	4.5	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1016/S0960-894X(97)00177-7
	134144056	157416	0	None	-1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	307	5	4	5	-0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3955458	157416	0	None	-1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	307	5	4	5	-0.3	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	131636303	167584	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4114464	167584	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636293	166918	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4109021	166918	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636343	151649	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.5	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3909878	151649	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	4	0	5	4.5	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	90354563	156461	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	3	0	5	4.6	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br	nan
	CHEMBL3947609	156461	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	427	3	0	5	4.6	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br	nan
	44348859	23336	0	None	-15	2	Human	5.5	pIC50	=	5.5	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	278	6	4	4	0.7	Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL123842	23336	0	None	-15	2	Human	5.5	pIC50	=	5.5	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	278	6	4	4	0.7	Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	21309795	157602	0	None	-3	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3956934	157602	0	None	-3	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	90643961	118771	0	None	-2	2	Rat	5.5	pIC50	=	5.5	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	3	0	6	3.9	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	CHEMBL3288649	118771	0	None	-2	2	Rat	5.5	pIC50	=	5.5	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	3	0	6	3.9	COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1	10.1016/j.bmcl.2014.04.051
	155538001	179124	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	179124	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	179124	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155538001	179124	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	179124	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	179124	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	131636355	167645	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4114983	167645	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.6	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636341	154729	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3933840	154729	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1	nan
	131636359	167551	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	CHEMBL4114183	167551	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	162665071	190507	0	None	1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4781638	190507	0	None	1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803454	190507	0	None	1	2	Human	6.5	pIC50	=	6.5	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	18548862	164718	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408455	164718	0	None	-	1	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	134137754	154726	0	None	1	2	Human	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	400	6	3	5	2.3	[N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	CHEMBL3933829	154726	0	None	1	2	Human	7.5	pIC50	=	7.5	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	400	6	3	5	2.3	[N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1	10.1016/j.bmcl.2016.10.067
	131636320	157479	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3956003	157479	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1	nan
	155550453	181048	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4549344	181048	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	155550453	181048	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4549344	181048	0	None	-	1	Rat	6.5	pIC50	=	6.5	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	461	6	1	7	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1	10.1021/acs.jmedchem.8b01266
	22448579	162557	0	None	4	2	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL405895	162557	0	None	4	2	Rat	7.5	pIC50	=	7.5	Functional	Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	131636302	166800	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	3	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4108010	166800	0	None	-	1	Human	7.5	pIC50	=	7.5	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	385	3	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	22224825	165773	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL409638	165773	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	11211597	63082	0	None	-1	3	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629865	63082	0	None	-1	3	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636347	149789	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	CHEMBL3894707	149789	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.5	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F	nan
	131636457	167328	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4112521	167328	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	3	0	4	5.3	Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636386	167741	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	6	0	6	4.4	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4115662	167741	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	6	0	6	4.4	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	131636358	155785	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3942377	155785	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	44302608	107623	0	None	-2	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	340	5	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL293434	107623	0	None	-2	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	340	5	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	155531624	178452	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4466304	178452	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155531624	178452	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4466304	178452	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	387	4	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	9952648	103083	0	None	1	2	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261288	103083	0	None	1	2	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	131636291	167065	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110331	167065	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	44302856	109508	0	None	1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	354	6	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL304919	109508	0	None	1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	354	6	3	4	1.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	11235624	63079	0	None	-6	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	63079	0	None	-6	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636394	167357	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	4.6	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4112680	167357	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	4.6	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636398	167023	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	CHEMBL4109944	167023	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	5	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl	nan
	134152341	160242	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3979475	160242	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	155542028	179870	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4520084	179870	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155542028	179870	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4520084	179870	0	None	-	1	Rat	5.4	pIC50	=	5.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	371	4	1	5	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	18548824	164515	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408229	164515	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	18548824	164515	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL408229	164515	0	None	-	1	Rat	7.4	pIC50	=	7.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	90643966	118775	0	None	-1	2	Rat	5.4	pIC50	=	5.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	448	3	1	6	3.3	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288660	118775	0	None	-1	2	Rat	5.4	pIC50	=	5.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	448	3	1	6	3.3	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	11351088	63072	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629856	63072	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	22317928	63073	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629857	63073	0	None	-	1	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	11281280	63182	0	None	1	3	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	63182	0	None	1	3	Rat	8.4	pIC50	=	8.4	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636425	167264	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4111952	167264	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636383	167521	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4113929	167521	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	69669747	190432	11	None	-2	4	Human	8.4	pIC50	=	8.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4751065	190432	11	None	-2	4	Human	8.4	pIC50	=	8.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802733	190432	11	None	-2	4	Human	8.4	pIC50	=	8.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	78320560	166699	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4107140	166699	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	78320248	167525	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4113962	167525	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636390	166861	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	442	3	0	6	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108541	166861	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	442	3	0	6	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	77461009	167076	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4110444	167076	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.2	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	90354889	167482	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.8	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	CHEMBL4113601	167482	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	4	0	5	4.8	CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	131636421	166749	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4107565	166749	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	4	0	5	5.4	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F	nan
	131636313	167380	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4112898	167380	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636356	167548	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4114150	167548	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	451	3	0	5	5.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636348	166641	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4106709	166641	0	None	-	1	Human	8.4	pIC50	=	8.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636391	166887	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108785	166887	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	428	3	0	6	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636431	167066	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4110332	167066	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	131636429	167379	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4112889	167379	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	78320559	167682	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4115237	167682	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	131636295	167707	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4115390	167707	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	78320249	167043	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4110153	167043	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	6	4.8	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	131636424	166680	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4106969	166680	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	460	4	0	6	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636279	150503	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3900589	150503	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	437	3	0	5	5.4	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636345	150892	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F	nan
	CHEMBL3903640	150892	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.7	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F	nan
	21309795	157602	0	None	-3	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.6b01119
	CHEMBL3956934	157602	0	None	-3	2	Human	6.4	pIC50	=	6.4	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	327	4	3	3	1.8	N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.6b01119
	11281280	63182	0	None	-5	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	63182	0	None	-5	3	Human	7.4	pIC50	=	7.4	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	131636287	167289	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112202	167289	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636411	167282	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.5	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	CHEMBL4112136	167282	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	4	0	5	5.5	COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	44302686	207695	0	None	-1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	332	4	3	4	1.4	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL60164	207695	0	None	-1	2	Human	4.4	pIC50	=	4.4	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	332	4	3	4	1.4	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	155540306	179678	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4516001	179678	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	90643968	118776	0	None	-6	2	Rat	6.4	pIC50	=	6.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288662	118776	0	None	-6	2	Rat	6.4	pIC50	=	6.4	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	370	2	0	5	4.1	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12	10.1016/j.bmcl.2014.04.051
	155540306	179678	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4516001	179678	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	424	6	1	7	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	131636392	167097	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	469	5	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	CHEMBL4110601	167097	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	469	5	1	6	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1	nan
	44348939	125272	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	293	7	3	4	1.1	COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	CHEMBL341457	125272	0	None	-2	2	Human	6.4	pIC50	=	6.4	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	293	7	3	4	1.1	COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1	10.1021/jm970498o
	1373	9253	51	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	139055582	9253	51	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	446355	9253	51	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	CHEMBL257626	9253	51	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	DB04256	9253	51	None	-1	4	Human	5.4	pIC50	=	5.4	Functional	Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor	ChEMBL	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10.1021/jm060950g
	11777615	105637	0	None	2	2	Rat	4.4	pIC50	=	4.4	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	265	2	3	4	1.2	CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1	10.1016/S0960-894X(97)00177-7
	CHEMBL278949	105637	0	None	2	2	Rat	4.4	pIC50	=	4.4	Functional	Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined	ChEMBL	265	2	3	4	1.2	CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1	10.1016/S0960-894X(97)00177-7
	10783272	92897	0	None	-15	2	Human	5.4	pIC50	=	5.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2311086	92897	0	None	-15	2	Human	5.4	pIC50	=	5.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	339	7	3	3	2.7	N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	131636380	167497	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4113748	167497	0	None	-	1	Human	7.4	pIC50	=	7.4	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.9	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	155538001	179124	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	179124	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	179124	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	155538001	179124	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4475753	179124	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	CHEMBL4580695	179124	0	None	-	1	Rat	6.4	pIC50	=	6.4	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	406	6	1	7	3.7	COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1	10.1021/acs.jmedchem.8b01266
	131636274	151416	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3908096	151416	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	3	0	5	4.7	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1	nan
	69669702	190454	0	None	3	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4756556	190454	0	None	3	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4802948	190454	0	None	3	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	131636368	166866	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108571	166866	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.7	Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	10732318	85518	0	None	6	2	Human	6.4	pIC50	=	6.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	291	8	3	3	1.9	NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112585	85518	0	None	6	2	Human	6.4	pIC50	=	6.4	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	291	8	3	3	1.9	NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10385210	19804	0	None	2	3	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189910	19804	0	None	2	3	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL539760	19804	0	None	2	3	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	309	5	3	6	0.0	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1	10.1016/s0960-894x(01)00329-8
	10250423	19785	0	None	-1	2	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%	ChEMBL	364	4	3	4	1.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189797	19785	0	None	-1	2	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%	ChEMBL	364	4	3	4	1.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL539516	19785	0	None	-1	2	Rat	4.4	pIC50	=	4.4	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%	ChEMBL	364	4	3	4	1.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	57338826	156406	0	None	1	5	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3947221	156406	0	None	1	5	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	131636459	167634	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	CHEMBL4114912	167634	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F	nan
	44302931	170049	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	270	4	3	4	0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL418650	170049	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	270	4	3	4	0.5	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1	10.1016/s0960-894x(98)00352-7
	90643973	118779	0	None	-1	2	Rat	5.3	pIC50	=	5.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	4	1	6	3.4	O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO	10.1016/j.bmcl.2014.04.051
	CHEMBL3288674	118779	0	None	-1	2	Rat	5.3	pIC50	=	5.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	382	4	1	6	3.4	O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO	10.1016/j.bmcl.2014.04.051
	22224570	102690	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259269	102690	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	131636344	155093	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	4	0	5	4.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1	nan
	CHEMBL3936936	155093	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	4	0	5	4.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1	nan
	131636362	166791	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4107924	166791	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	22317491	63070	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629853	63070	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636437	150784	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl	nan
	CHEMBL3902842	150784	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	4	0	5	4.9	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl	nan
	1297	177031	36	None	-1	2	Human	4.3	pIC50	=	4.3	Functional	Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm00019a002
	CHEMBL444589	177031	36	None	-1	2	Human	4.3	pIC50	=	4.3	Functional	Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm00019a002
	162658340	190465	0	None	1	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4760856	190465	0	None	1	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803084	190465	0	None	1	2	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	131636321	156144	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3945334	156144	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1	nan
	70051296	96833	0	None	-1	3	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	CHEMBL2381648	96833	0	None	-1	3	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	22317724	63062	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629845	63062	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	53317987	63075	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629859	63075	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	11362246	63183	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631860	63183	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	53325611	63190	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631867	63190	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636413	166869	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	6	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	CHEMBL4108588	166869	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	6	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	131636381	167348	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112623	167348	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	409	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636384	167580	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	CHEMBL4114409	167580	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	5.0	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1	nan
	78320251	167723	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	CHEMBL4115497	167723	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	397	3	0	5	4.9	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl	nan
	131636430	167499	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	7	0	6	4.9	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4113756	167499	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	7	0	6	4.9	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	90354553	166693	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	CHEMBL4107066	166693	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	0	6	5.3	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F	nan
	131636464	167084	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	CHEMBL4110505	167084	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	4	0	5	4.5	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C	nan
	131636420	167135	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4110839	167135	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.3	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	131636426	166716	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	CHEMBL4107266	166716	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	441	5	0	5	5.5	Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1	nan
	78320557	167094	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4110578	167094	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	443	5	0	5	5.6	Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	1393	8321	64	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	1396	8321	64	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	213056	8321	64	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	CHEMBL8759	8321	64	None	2	6	Human	8.3	pIC50	=	8.3	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm4000165
	78324634	167081	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110486	167081	0	None	-	1	Human	8.3	pIC50	=	8.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	131636363	166819	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4108148	166819	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	2	0	4	5.9	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354342	166999	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	CHEMBL4109709	166999	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	4	0	5	5.0	COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl	nan
	131636441	166916	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	5	0	5	5.2	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	CHEMBL4109004	166916	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	5	0	5	5.2	CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	53320632	63069	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629852	63069	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636445	166742	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4107450	166742	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	403	5	0	5	5.0	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	1222	108514	63	None	-	1	Human	4.3	pIC50	=	4.3	Functional	Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm960059+
	CHEMBL299683	108514	63	None	-	1	Human	4.3	pIC50	=	4.3	Functional	Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm960059+
	6324634	154722	11	None	6	2	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00352-7
	CHEMBL39338	154722	11	None	6	2	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00352-7
	44302609	209412	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL61281	209412	0	None	-	1	Human	4.3	pIC50	=	4.3	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	314	4	3	4	1.3	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1	10.1016/s0960-894x(98)00352-7
	6324634	154722	11	None	6	2	Human	4.3	pIC50	=	4.3	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	CHEMBL39338	154722	11	None	6	2	Human	4.3	pIC50	=	4.3	Functional	Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1016/s0960-894x(98)00091-2
	131636364	167640	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	CHEMBL4114951	167640	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	3	0	5	4.0	COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F	nan
	10091203	19723	0	None	-2	3	Rat	4.3	pIC50	=	4.3	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1189303	19723	0	None	-2	3	Rat	4.3	pIC50	=	4.3	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL538489	19723	0	None	-2	3	Rat	4.3	pIC50	=	4.3	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	308	5	4	5	-0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1	10.1016/s0960-894x(01)00329-8
	11269030	63078	0	None	-1	3	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	63078	0	None	-1	3	Human	7.3	pIC50	=	7.3	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	10201802	103422	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL263649	103422	0	None	-	1	Rat	7.3	pIC50	=	7.3	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	10428048	10134	31	None	-3	2	Human	6.3	pIC50	=	6.3	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1039/C3MD00110E
	3955	10134	31	None	-3	2	Human	6.3	pIC50	=	6.3	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1039/C3MD00110E
	CHEMBL305406	10134	31	None	-3	2	Human	6.3	pIC50	=	6.3	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1039/C3MD00110E
	71566598	149468	15	None	-1	3	Rat	7.3	pIC50	=	7.3	Functional	Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	149468	15	None	-1	3	Rat	7.3	pIC50	=	7.3	Functional	Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	131636332	158070	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3960577	158070	0	None	-	1	Human	7.3	pIC50	=	7.3	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	405	2	0	4	5.0	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	155545491	180160	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	CHEMBL4527834	180160	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	155545491	180160	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	CHEMBL4527834	180160	0	None	-	1	Rat	6.3	pIC50	=	6.3	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	399	4	1	5	3.8	C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	137634033	163420	0	None	-1	2	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4069251	163420	0	None	-1	2	Human	5.3	pIC50	=	5.3	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	90643964	118773	0	None	-1	2	Rat	6.3	pIC50	=	6.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288656	118773	0	None	-1	2	Rat	6.3	pIC50	=	6.3	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	386	2	0	5	4.6	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12	10.1016/j.bmcl.2014.04.051
	131636436	160341	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3980239	160341	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	155554668	181382	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4557272	181382	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155554668	181382	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4557272	181382	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	394	5	1	6	3.9	Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	131636322	152171	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	5	0	5	4.7	CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F	nan
	CHEMBL3913916	152171	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	395	5	0	5	4.7	CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F	nan
	22317741	63186	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631863	63186	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317620	63192	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631869	63192	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL5076351	221209	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay	ChEMBL		None	None	None		CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1	10.1021/acs.jmedchem.1c02004
	90355554	166709	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	CHEMBL4107197	166709	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	5	5.2	CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl	nan
	131636428	167684	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	6	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	CHEMBL4115246	167684	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	449	6	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1	nan
	131636307	166712	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	CHEMBL4107211	166712	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C	nan
	67637415	190466	0	None	2	2	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4759992	190466	0	None	2	2	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803099	190466	0	None	2	2	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	131636377	166672	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	CHEMBL4106932	166672	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	447	4	0	6	5.1	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F	nan
	117821319	125596	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	431	2	0	5	4.7	C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21	10.1021/ml5005365
	CHEMBL3421840	125596	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	431	2	0	5	4.7	C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21	10.1021/ml5005365
	131636438	158003	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3960039	158003	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	423	5	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	44309100	109408	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/j.bmcl.2007.10.026
	CHEMBL304285	109408	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/j.bmcl.2007.10.026
	131636340	151542	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	3	0	5	4.5	Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	CHEMBL3909077	151542	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	407	3	0	5	4.5	Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F	nan
	44302930	107490	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	278	5	3	4	0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL292553	107490	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	278	5	3	4	0.2	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1	10.1016/s0960-894x(98)00352-7
	52944782	23719	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level	ChEMBL	241	4	3	3	0.9	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1	10.1016/j.bmc.2010.06.051
	CHEMBL1253502	23719	0	None	-	1	Human	4.2	pIC50	=	4.2	Functional	Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level	ChEMBL	241	4	3	3	0.9	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1	10.1016/j.bmc.2010.06.051
	19702198	168101	16	None	1	2	Rat	4.2	pIC50	=	4.2	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	10.1016/s0960-894x(01)00329-8
	CHEMBL412445	168101	16	None	1	2	Rat	4.2	pIC50	=	4.2	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	10.1016/s0960-894x(01)00329-8
	131636335	160048	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3977681	160048	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	367	2	0	4	4.8	Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1	nan
	131636278	154245	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C	nan
	CHEMBL3930304	154245	0	None	-	1	Human	7.2	pIC50	=	7.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	363	3	0	5	4.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C	nan
	10607617	85511	0	None	-2	2	Human	5.2	pIC50	=	5.2	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	187	4	3	3	-0.1	CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112579	85511	0	None	-2	2	Human	5.2	pIC50	=	5.2	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	187	4	3	3	-0.1	CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	134155683	158140	0	None	1	2	Human	7.2	pIC50	=	7.2	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	377	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3961306	158140	0	None	1	2	Human	7.2	pIC50	=	7.2	Functional	Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	377	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	155553540	180958	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4547431	180958	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155553540	180958	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4547431	180958	0	None	-	1	Rat	5.2	pIC50	=	5.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	355	4	1	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1	10.1021/acs.jmedchem.8b01266
	155551226	180761	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4541942	180761	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155559283	181637	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563286	181637	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155551226	180761	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	CHEMBL4541942	180761	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1	10.1021/acs.jmedchem.8b01266
	155559283	181637	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4563286	181637	0	None	-	1	Rat	6.2	pIC50	=	6.2	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	380	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1	10.1021/acs.jmedchem.8b01266
	11304010	63081	0	None	-2	3	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629864	63081	0	None	-2	3	Human	8.2	pIC50	=	8.2	Functional	Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	22317892	63077	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629860	63077	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	22317279	63188	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631865	63188	0	None	-	1	Rat	8.2	pIC50	=	8.2	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636308	167581	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	CHEMBL4114419	167581	0	None	-	1	Human	8.2	pIC50	=	8.2	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	431	5	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C	nan
	90354432	167598	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	1	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4114578	167598	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	465	5	1	6	4.4	COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	78319943	166690	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4107040	166690	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	399	4	0	5	4.8	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636404	167118	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4110709	167118	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	415	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354881	166870	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4108597	166870	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636327	167421	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.5	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	CHEMBL4113208	167421	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	377	4	0	5	4.5	CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC	nan
	1378	9195	54	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	1399	9195	54	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	9819927	9195	54	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	CHEMBL432038	9195	54	None	-2	14	Human	8.1	pIC50	=	8.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	131636281	167463	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113495	167463	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	3	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90354538	167141	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	485	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	CHEMBL4110899	167141	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	485	5	0	5	5.8	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F	nan
	131636440	167693	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	CHEMBL4115297	167693	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	391	5	0	5	4.8	CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC	nan
	10979251	96835	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381650	96835	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	10979251	96835	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	CHEMBL2381650	96835	0	None	-5	3	Human	5.2	pIC50	=	5.2	Functional	Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	22317408	63067	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629850	63067	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	131636433	151355	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3907628	151355	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	419	4	0	5	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	10297067	103079	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261263	103079	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	131636277	158433	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3963950	158433	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	3	0	5	4.8	Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	18548910	102709	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259340	102709	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	155565564	182349	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4579281	182349	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	155565564	182349	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4579281	182349	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	407	5	1	5	4.8	Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1	10.1021/acs.jmedchem.8b01266
	18548737	63177	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631854	63177	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	44302819	170015	0	None	-	1	Human	4.1	pIC50	=	4.1	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	298	4	3	4	0.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	CHEMBL418462	170015	0	None	-	1	Human	4.1	pIC50	=	4.1	Functional	In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.	ChEMBL	298	4	3	4	0.8	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1	10.1016/s0960-894x(98)00352-7
	155564600	182331	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	CHEMBL4578758	182331	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	155564600	182331	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	CHEMBL4578758	182331	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	393	5	1	5	4.5	Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1	10.1021/acs.jmedchem.8b01266
	162666357	190510	0	None	3	2	Human	7.1	pIC50	=	7.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4784701	190510	0	None	3	2	Human	7.1	pIC50	=	7.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803523	190510	0	None	3	2	Human	7.1	pIC50	=	7.1	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	137656301	165461	0	None	-	1	Human	5.1	pIC50	=	5.1	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4093017	165461	0	None	-	1	Human	5.1	pIC50	=	5.1	Functional	Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	44300389	20431	0	None	-1	2	Rat	4.1	pIC50	=	4.1	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	342	4	3	4	0.9	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL1194613	20431	0	None	-1	2	Rat	4.1	pIC50	=	4.1	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	342	4	3	4	0.9	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1	10.1016/s0960-894x(01)00329-8
	CHEMBL552984	20431	0	None	-1	2	Rat	4.1	pIC50	=	4.1	Functional	Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2	ChEMBL	342	4	3	4	0.9	N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1	10.1016/s0960-894x(01)00329-8
	131636292	167305	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	353	2	0	4	4.5	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	CHEMBL4112325	167305	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	353	2	0	4	4.5	Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1	nan
	131636439	160607	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3982561	160607	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	433	5	0	5	5.1	Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	117821004	125595	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	3	0	4	4.9	CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21	10.1021/ml5005365
	CHEMBL3421839	125595	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	400	3	0	4	4.9	CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21	10.1021/ml5005365
	155511336	176318	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4435396	176318	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155511336	176318	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4435396	176318	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	431	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	11235624	63079	0	None	-1	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	63079	0	None	-1	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11442010	63083	0	None	-2	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629866	63083	0	None	-2	3	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	25210562	221745	25	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay	ChEMBL		None	None	None		N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1	10.1021/acs.jmedchem.1c02004
	CHEMBL5085417	221745	25	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay	ChEMBL		None	None	None		N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1	10.1021/acs.jmedchem.1c02004
	131636350	150600	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1	nan
	CHEMBL3901364	150600	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	4	5.1	Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1	nan
	117824335	125594	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	2	0	4	4.5	Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1	10.1021/ml5005365
	CHEMBL3421838	125594	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay	ChEMBL	386	2	0	4	4.5	Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1	10.1021/ml5005365
	49836087	7847	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	6222	7847	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	CHEMBL1630805	7847	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	3335	9789	4	None	1	2	Human	5.1	pIC50	=	5.1	Functional	Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm960059+
	5311344	9789	4	None	1	2	Human	5.1	pIC50	=	5.1	Functional	Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm960059+
	CHEMBL39573	9789	4	None	1	2	Human	5.1	pIC50	=	5.1	Functional	Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm960059+
	131636449	167197	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	461	5	0	6	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4111376	167197	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	461	5	0	6	5.3	Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	90643970	118777	0	None	1	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	464	3	1	6	3.8	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288664	118777	0	None	1	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	464	3	1	6	3.8	Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12	10.1016/j.bmcl.2014.04.051
	10587622	85515	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	CHEMBL2112582	85515	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970497w
	10587622	85515	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	CHEMBL2112582	85515	0	None	-1	2	Human	6.1	pIC50	=	6.1	Functional	Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2	ChEMBL	263	6	3	3	1.1	NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm970498o
	90643956	118768	0	None	-5	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	CHEMBL3288639	118768	0	None	-5	2	Rat	6.1	pIC50	=	6.1	Functional	Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration	ChEMBL	352	2	0	5	3.9	Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12	10.1016/j.bmcl.2014.04.051
	155564325	182197	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4575990	182197	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155564325	182197	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4575990	182197	0	None	-	1	Rat	7.1	pIC50	=	7.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	429	5	1	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1	10.1021/acs.jmedchem.8b01266
	155521127	177329	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4450016	177329	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155521127	177329	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4450016	177329	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	413	5	1	5	4.8	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	76332991	112876	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	428	2	1	4	3.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1	10.1039/C3MD00110E
	CHEMBL3133882	112876	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	428	2	1	4	3.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1	10.1039/C3MD00110E
	76322144	112881	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	534	4	1	5	5.6	COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	CHEMBL3133887	112881	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	534	4	1	5	5.6	COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	155515940	176787	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4442453	176787	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	155515940	176787	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4442453	176787	0	None	-	1	Rat	6.1	pIC50	=	6.1	Functional	Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay	ChEMBL	397	5	1	5	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1	10.1021/acs.jmedchem.8b01266
	9888376	101990	1	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256011	101990	1	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	18548795	63175	0	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631757	63175	0	None	-	1	Rat	8.1	pIC50	=	8.1	Functional	Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	131636414	167033	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	483	7	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	CHEMBL4110033	167033	0	None	-	1	Human	8.1	pIC50	=	8.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	483	7	0	6	5.4	COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F	nan
	131636334	156934	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3951588	156934	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	421	2	0	4	5.5	Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1	nan
	131636352	167214	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	CHEMBL4111531	167214	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	413	4	0	5	5.1	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F	nan
	131636387	167699	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	CHEMBL4115328	167699	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	453	4	0	5	5.2	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1	nan
	131636371	166919	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	CHEMBL4109036	166919	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	429	5	0	6	4.8	COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F	nan
	131636452	167449	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	CHEMBL4113408	167449	0	None	-	1	Human	8.0	pIC50	=	8.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	439	4	0	6	4.6	Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1	nan
	67633284	190426	0	None	5	2	Human	8.0	pIC50	=	8.0	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4748699	190426	0	None	5	2	Human	8.0	pIC50	=	8.0	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802655	190426	0	None	5	2	Human	8.0	pIC50	=	8.0	Functional	Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	131636275	149639	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	5	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1	nan
	CHEMBL3893337	149639	0	None	-	1	Human	7.1	pIC50	=	7.1	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	389	3	0	5	4.4	Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1	nan
	76322143	112879	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	400	3	1	5	4.4	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	CHEMBL3133885	112879	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis	ChEMBL	400	3	1	5	4.4	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1039/C3MD00110E
	131636330	155247	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.6	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3938055	155247	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	371	2	0	4	4.6	Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL5089623	221996	2	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	CHEMBL5089623	221996	2	None	-	1	Human	7.0	pIC50	=	7.0	Functional	Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	131636318	150372	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3899445	150372	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	417	5	0	5	4.6	Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1	nan
	131636288	167603	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	CHEMBL4114600	167603	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	381	3	0	5	4.3	COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F	nan
	90354465	155024	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	CHEMBL3936284	155024	0	None	-	1	Human	7.0	pIC50	=	7.0	Functional	[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.	ChEMBL	435	4	0	5	4.9	Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1	nan
	44322537	213432	0	None	-	0	Human	6.0	pKi	=	6	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	517	7	0	7	6.2	CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1021/jm000007r
	CHEMBL89293	213432	0	None	-	0	Human	6.0	pKi	=	6	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	517	7	0	7	6.2	CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1021/jm000007r
	1393	8321	64	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	1396	8321	64	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	213056	8321	64	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	CHEMBL8759	8321	64	None	2	6	Human	8.0	pKi	=	8.0	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000007r
	10428048	10134	31	None	-3	2	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1021/jm000007r
	3955	10134	31	None	-3	2	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1021/jm000007r
	CHEMBL305406	10134	31	None	-3	2	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1021/jm000007r
	44322840	119348	0	None	-	0	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	201	2	4	4	-1.5	N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O	10.1021/jm000007r
	CHEMBL330097	119348	0	None	-	0	Human	7.0	pKi	=	7.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	201	2	4	4	-1.5	N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O	10.1021/jm000007r
	1415	9392	41	None	-	2	Human	5.0	pKi	=	5.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	245	3	4	3	-0.3	OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C	10.1021/jm000007r
	3972752	9392	41	None	-	2	Human	5.0	pKi	=	5.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	245	3	4	3	-0.3	OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C	10.1021/jm000007r
	CHEMBL86508	9392	41	None	-	2	Human	5.0	pKi	=	5.0	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	245	3	4	3	-0.3	OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C	10.1021/jm000007r
	1310	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	1369	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	33032	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	44272391	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	88747398	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	CHEMBL575060	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	DB00142	9095	110	None	-389	17	Human	4.9	pKi	=	4.9	Functional	Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm000007r
	10359073	161753	1	None	-1	2	Human	4.8	pKi	=	4.8	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL40123	161753	1	None	-1	2	Human	4.8	pKi	=	4.8	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	10197984	9199	44	None	1	5	Human	8.6	pKi	=	8.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm000007r
	1394	9199	44	None	1	5	Human	8.6	pKi	=	8.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm000007r
	CHEMBL275079	9199	44	None	1	5	Human	8.6	pKi	=	8.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm000007r
	3246152	168071	31	None	-	0	Human	5.7	pKi	=	5.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	4	3	3	-0.5	C[C@@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL41221	168071	31	None	-	0	Human	5.7	pKi	=	5.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	4	3	3	-0.5	C[C@@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	1297	177031	36	None	-1	2	Human	4.7	pKi	=	4.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm000007r
	CHEMBL444589	177031	36	None	-1	2	Human	4.7	pKi	=	4.7	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	10.1021/jm000007r
	1378	9195	54	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	1399	9195	54	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	9819927	9195	54	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	CHEMBL432038	9195	54	None	-2	14	Human	7.7	pKi	=	7.7	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm000007r
	439282	148362	8	None	-	0	Human	6.6	pKi	=	6.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	159	4	3	3	-0.6	C=C(C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL38499	148362	8	None	-	0	Human	6.6	pKi	=	6.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	159	4	3	3	-0.6	C=C(C[C@H](N)C(=O)O)C(=O)O	10.1021/jm000007r
	11820180	24834	1	None	-	0	Human	4.6	pKi	=	4.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	4	3	6	-2.1	N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O	10.1021/jm000007r
	CHEMBL126608	24834	1	None	-	0	Human	4.6	pKi	=	4.6	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	4	3	6	-2.1	N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O	10.1021/jm000007r
	10058694	213382	1	None	-	0	Human	8.4	pKi	=	8.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O	10.1021/jm000007r
	CHEMBL88999	213382	1	None	-	0	Human	8.4	pKi	=	8.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O	10.1021/jm000007r
	4694355	105515	36	None	-	1	Human	4.5	pKi	=	4.5	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1021/jm000007r
	CHEMBL277961	105515	36	None	-	1	Human	4.5	pKi	=	4.5	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	257	2	4	3	-0.3	NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21	10.1021/jm000007r
	16739377	98951	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	CHEMBL242344	98951	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	16739377	98951	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	CHEMBL242344	98951	0	None	-	0	Rat	4.5	pKi	=	4.5	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	253	4	3	5	1.3	NC(C(=O)O)c1cnn(O)c1CC1CCCCC1	10.1016/j.bmc.2007.02.047
	44322921	213616	1	None	-	0	Human	6.5	pKi	=	6.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O	10.1021/jm000007r
	CHEMBL90501	213616	1	None	-	0	Human	6.5	pKi	=	6.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O	10.1021/jm000007r
	59066632	213349	89	None	1	2	Human	4.5	pKi	=	4.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm000007r
	92136	213349	89	None	1	2	Human	4.5	pKi	=	4.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL88804	213349	89	None	1	2	Human	4.5	pKi	=	4.5	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm000007r
	44322745	112943	0	None	-	0	Human	4.4	pKi	=	4.4	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	203	3	3	6	-2.1	C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O	10.1021/jm000007r
	CHEMBL313713	112943	0	None	-	0	Human	4.4	pKi	=	4.4	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	203	3	3	6	-2.1	C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O	10.1021/jm000007r
	1392	6861	48	None	-	4	Human	6.4	pKi	=	6.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	5310984	6861	48	None	-	4	Human	6.4	pKi	=	6.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	CHEMBL40086	6861	48	None	-	4	Human	6.4	pKi	=	6.4	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	10330132	108159	1	None	-	2	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1021/jm000007r
	CHEMBL297150	108159	1	None	-	2	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	189	2	4	5	-2.2	NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O	10.1021/jm000007r
	1368	9070	37	None	1	11	Human	6.3	pKi	=	6.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm000007r
	5310956	9070	37	None	1	11	Human	6.3	pKi	=	6.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL280563	9070	37	None	1	11	Human	6.3	pKi	=	6.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm000007r
	104766	6822	42	None	-2	14	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	1365	6822	42	None	-2	14	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	CHEMBL34453	6822	42	None	-2	14	Human	5.3	pKi	=	5.3	Functional	Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm000007r
	6324634	154722	11	None	6	2	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	CHEMBL39338	154722	11	None	6	2	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm000007r
	1222	108514	63	None	-	1	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm000007r
	CHEMBL299683	108514	63	None	-	1	Human	4.3	pKi	=	4.3	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	10.1021/jm000007r
	10198359	80733	9	None	-10	4	Human	4.3	pKi	=	4.3	Functional	Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1021/jm000007r
	CHEMBL2021372	80733	9	None	-10	4	Human	4.3	pKi	=	4.3	Functional	Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1021/jm000007r
	44428738	175529	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	CHEMBL437169	175529	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	44428738	175529	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	CHEMBL437169	175529	0	None	-	0	Rat	4.2	pKi	=	4.2	Functional	Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level	ChEMBL	275	6	3	5	1.4	NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1	10.1016/j.bmc.2007.02.047
	44322529	213645	1	None	-	0	Human	7.1	pKi	=	7.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1021/jm000007r
	CHEMBL90675	213645	1	None	-	0	Human	7.1	pKi	=	7.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1021/jm000007r
	1439	9247	15	None	-	1	Human	4.1	pKi	=	4.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm000007r
	5311457	9247	15	None	-	1	Human	4.1	pKi	=	4.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm000007r
	CHEMBL41013	9247	15	None	-	1	Human	4.1	pKi	=	4.1	Functional	Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm000007r
	1310	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	None	-457	17	Rat	8.3	pEC50	=	8.3	Functional	NoneNone	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1310	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	None	-389	17	Human	8.2	pEC50	=	8.2	Functional	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	Drug Central	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	25195461	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	8946	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	CHEMBL3337527	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	DB12059	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Functional	Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTPγS binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.	Guide to Pharmacology	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	25692015
	1310	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	1369	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	33032	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	44272391	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	88747398	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	CHEMBL575060	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	DB00142	9095	110	None	-389	17	Human	5.1	pEC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10443583
	11281345	6901	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	411	8	1	5	3.3	CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1	15717213
	6258	6901	0	None	-	1	Human	5.7	pEC50	=	5.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	411	8	1	5	3.3	CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1	15717213
	25002940	7890	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	22364337
	6320	7890	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	22364337
	CHEMBL2029821	7890	0	None	-	1	Human	6.4	pEC50	=	6.4	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	5	4.8	CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C	22364337
	25125217	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	7678	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	CHEMBL3937907	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	DB16073	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	None
	46182736	7776	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	21155570
	6323	7776	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	21155570
	CHEMBL1651219	7776	0	None	-	1	Rat	6.8	pEC50	=	6.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	21155570
	46190878	8653	7	None	-	1	Human	6.9	pEC50	=	6.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	20005096
	6253	8653	7	None	-	1	Human	6.9	pEC50	=	6.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	20005096
	CHEMBL595759	8653	7	None	-	1	Human	6.9	pEC50	=	6.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	20005096
	3954	7451	60	None	6	2	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	16046122
	9868580	7451	60	None	6	2	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	16046122
	CHEMBL593013	7451	60	None	6	2	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	16046122
	3372	7600	0	None	-	1	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	4	4.0	N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1	15717213
	9864510	7600	0	None	-	1	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	4	4.0	N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1	15717213
	CHEMBL4303163	7600	0	None	-	1	Human	7.0	pEC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	377	6	0	4	4.0	N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1	15717213
	46830123	7859	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	20409708
	6321	7859	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	20409708
	CHEMBL1094763	7859	0	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	350	4	0	4	4.3	N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C	20409708
	46190877	8652	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	20005096
	6252	8652	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	20005096
	CHEMBL605836	8652	7	None	-	1	Human	7.1	pEC50	=	7.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	20005096
	6256	7796	0	None	-	1	Rat	7.2	pEC50	=	7.2	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2	18812259
	73755202	7796	0	None	-	1	Rat	7.2	pEC50	=	7.2	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2	18812259
	59234231	8924	4	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	8924	4	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	8924	4	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	8924	4	None	1	2	Rat	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	59234231	8924	4	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	8924	4	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	8924	4	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	8924	4	None	-1	2	Human	7.3	pEC50	=	7.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6255	7774	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	6	0	5	3.9	Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2	18812259
	73755201	7774	0	None	-	1	Rat	7.5	pEC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	6	0	5	3.9	Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2	18812259
	6254	7772	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2	18812259
	73755200	7772	0	None	-	1	Rat	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	382	6	0	5	3.5	Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2	18812259
	44335556	8082	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	15717213
	6257	8082	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	15717213
	CHEMBL321968	8082	0	None	-	1	Human	7.6	pEC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	15717213
	44595851	10574	4	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	6259	10574	4	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	CHEMBL4092105	10574	4	None	-3	2	Human	7.7	pEC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	49765871	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	6317	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	CHEMBL2179319	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	11362035	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	6328	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	6329	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	CHEMBL105296	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	15149652
	44595851	10574	4	None	3	2	Rat	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	6259	10574	4	None	3	2	Rat	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	CHEMBL4092105	10574	4	None	3	2	Rat	7.9	pEC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	20947638
	3335	9789	4	None	-1	2	Rat	5.1	pIC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	8667369
	5311344	9789	4	None	-1	2	Rat	5.1	pIC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	8667369
	CHEMBL39573	9789	4	None	-1	2	Rat	5.1	pIC50	=	5.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	8667369
	1402	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	1402	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	1402	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15149652
	1402	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	9825084	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	9825084	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	9825084	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15149652
	9825084	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	CHEMBL108939	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	CHEMBL108939	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	CHEMBL108939	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15149652
	CHEMBL108939	6910	44	None	-	1	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	49858117	7875	4	None	5	2	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	6223	7875	4	None	5	2	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	CHEMBL1630806	7875	4	None	5	2	Human	5.8	pIC50	=	5.8	Functional	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	49858118	7894	0	None	10	2	Human	6.0	pIC50	=	6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	6224	7894	0	None	10	2	Human	6.0	pIC50	=	6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	CHEMBL1630807	7894	0	None	10	2	Human	6.0	pIC50	=	6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	49836087	7847	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	6222	7847	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	CHEMBL1630805	7847	0	None	16	2	Human	6.1	pIC50	=	6.1	Functional	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	10428048	10134	31	None	3	2	Rat	7.0	pIC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10465539
	3955	10134	31	None	3	2	Rat	7.0	pIC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10465539
	CHEMBL305406	10134	31	None	3	2	Rat	7.0	pIC50	=	7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10465539
	6219	9363	0	None	-1	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	73755191	9363	0	None	-1	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	6221	9365	0	None	-2	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	73755193	9365	0	None	-2	3	Human	7.5	pIC50	=	7.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	11158623	10124	11	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	11158623	10124	11	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6226	10124	11	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	6226	10124	11	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	CHEMBL1629855	10124	11	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	CHEMBL1629855	10124	11	None	1	4	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6219	9363	0	None	1	3	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	73755191	9363	0	None	1	3	Rat	7.6	pIC50	=	7.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	401	1	1	3	4.0	N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I	17416742
	6220	9364	0	None	-1	3	Rat	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	73755192	9364	0	None	-1	3	Rat	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	6220	9364	0	None	1	3	Human	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	73755192	9364	0	None	1	3	Human	7.7	pIC50	=	7.7	Functional	UnclassifiedUnclassified	Guide to Pharmacology	405	2	1	3	5.4	O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1	17416742
	11158623	10124	11	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	6226	10124	11	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	CHEMBL1629855	10124	11	None	-7	4	Human	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	20971004
	6221	9365	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	73755193	9365	0	None	1	3	Rat	7.9	pIC50	=	7.9	Functional	UnclassifiedUnclassified	Guide to Pharmacology	354	1	1	4	3.6	N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br	17416742
	6324	10126	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	73755205	10126	0	None	-	1	Rat	8.3	pIC50	=	8.3	Functional	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	10047169	9998	1	None	-	1	Human	6.5	pIC50	None	6.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	15317469
	1403	9998	1	None	-	1	Human	6.5	pIC50	None	6.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	15317469
	CHEMBL182371	9998	1	None	-	1	Human	6.5	pIC50	None	6.5	Functional	UnclassifiedUnclassified	Guide to Pharmacology	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	15317469
	10275802	6895	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	10275802	6895	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	10275802	6895	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213
	1401	6895	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	12852748
	1401	6895	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	14500736
	1401	6895	0	None	-	1	Human	6.6	pIC50	None	6.6	Functional	UnclassifiedUnclassified	Guide to Pharmacology	452	8	0	5	4.8	COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	15717213

Get vendors

Ligands					Receptor			Assay information							Chemical information
Sel. page	Common name	GPCRdb ID	#Vendors	Reference ligand	Fold selectivity (Affinity)	# tested GPCRs (Affinity)	Species	p-value (-log)	Type	Activity Relation	Activity Value	Assay Type	Assay Description	Source	Mol weight	Rot Bonds	H don	H acc	LogP	Smiles	DOI
	9794208	96825	4	None	-	0	Human	9.8	pEC50	=	9.8	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	4	-1.3	N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	CHEMBL2381640	96825	4	None	-	0	Human	9.8	pEC50	=	9.8	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	4	-1.3	N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	139119037	96837	2	None	-	0	Human	9.3	pEC50	=	9.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	15479143	96837	2	None	-	0	Human	9.3	pEC50	=	9.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	CHEMBL2381652	96837	2	None	-	0	Human	9.3	pEC50	=	9.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	70051926	96826	2	None	-	0	Human	8.9	pEC50	=	8.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	197	2	3	3	-0.3	C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381641	96826	2	None	-	0	Human	8.9	pEC50	=	8.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	197	2	3	3	-0.3	C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	44335501	116434	0	None	-	0	Human	7.0	pEC50	=	7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL322465	116434	0	None	-	0	Human	7.0	pEC50	=	7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	50993966	64105	0	None	-	0	Rat	7.0	pEC50	=	7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	449	7	1	3	5.9	CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	CHEMBL1651212	64105	0	None	-	0	Rat	7.0	pEC50	=	7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	449	7	1	3	5.9	CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	24815976	206538	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593745	206538	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24815883	208241	0	None	-	2	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604993	208241	0	None	-	2	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225581	208766	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL608103	208766	0	None	-	3	Human	7.0	pEC50	=	7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	11768848	122030	11	None	-	1	Human	5.0	pEC50	=	5	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347671	122030	11	None	-	1	Human	5.0	pEC50	=	5	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	10198359	80733	9	None	-	1	Human	5.0	pEC50	=	5	Binding	Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1016/s0960-894x(98)00265-0
	CHEMBL2021372	80733	9	None	-	1	Human	5.0	pEC50	=	5	Binding	Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor	ChEMBL	221	3	3	3	-0.8	N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O	10.1016/s0960-894x(98)00265-0
	90643871	118641	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287693	118641	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	164617451	191731	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1	10.1016/j.bmcl.2021.128342
	CHEMBL4853794	191731	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1	10.1016/j.bmcl.2021.128342
	90643884	118667	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	CHEMBL3287719	118667	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	89735528	144775	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	10.1016/j.bmcl.2016.01.021
	CHEMBL3764544	144775	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1	10.1016/j.bmcl.2016.01.021
	90643857	118670	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287722	118670	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	10050046	72847	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	463	12	2	7	3.5	CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL183756	72847	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	463	12	2	7	3.5	CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	11656255	130089	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	498	8	1	5	6.9	CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361570	130089	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	498	8	1	5	6.9	CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643896	118652	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	CHEMBL3287704	118652	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	68109941	162901	0	None	-	1	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	162901	0	None	-	1	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	53390518	89469	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1	10.1021/jm3005306
	CHEMBL2179635	89469	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1	10.1021/jm3005306
	53390519	89470	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	441	6	1	3	5.8	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	CHEMBL2179636	89470	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	441	6	1	3	5.8	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	23521689	11615	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104248	11615	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	89735510	144675	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763263	144675	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21	10.1016/j.bmcl.2016.01.021
	164610619	191533	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4850952	191533	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	164627219	193160	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4875653	193160	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	44578904	188348	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	409	6	0	4	5.0	Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476791	188348	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	409	6	0	4	5.0	Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	90643904	118661	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287713	118661	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	90643900	118656	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O	10.1021/jm5000563
	CHEMBL3287708	118656	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O	10.1021/jm5000563
	71117141	154227	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	CHEMBL3930164	154227	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	435	4	0	8	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21	nan
	69929497	147066	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	434	3	0	7	2.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805900	147066	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	434	3	0	7	2.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21	10.1021/acsmedchemlett.5b00459
	90643881	118662	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287714	118662	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	11	2	6	4.5	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	11648184	69817	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	454	5	1	4	5.9	CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL178823	69817	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	454	5	1	4	5.9	CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	71681826	96836	0	None	-4	2	Human	5.9	pEC50	=	5.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	CHEMBL2381651	96836	0	None	-4	2	Human	5.9	pEC50	=	5.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm4000165
	162649186	190423	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1205	32	6	12	12.5	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4748285	190423	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1205	32	6	12	12.5	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802609	190423	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1205	32	6	12	12.5	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	1310	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	1369	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	33032	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	44272391	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	88747398	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	CHEMBL575060	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	DB00142	9095	110	None	-13	18	Rat	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	71681825	96830	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381645	96830	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	104766	6822	42	None	-11	11	Human	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	1365	6822	42	None	-11	11	Human	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	CHEMBL34453	6822	42	None	-11	11	Human	4.9	pEC50	=	4.9	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	11583075	70264	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	442	5	1	5	5.3	O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	CHEMBL179939	70264	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	442	5	1	5	5.3	O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	162647509	190416	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1134	27	6	12	10.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4744407	190416	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1134	27	6	12	10.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802513	190416	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1134	27	6	12	10.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	56929215	118624	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287671	118624	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	90643902	118659	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	390	10	2	5	4.4	CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	CHEMBL3287711	118659	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	390	10	2	5	4.4	CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	67056056	146979	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	429	2	0	7	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3804910	146979	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	429	2	0	7	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21	10.1021/acsmedchemlett.5b00459
	46190878	8653	7	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	6253	8653	7	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	CHEMBL595759	8653	7	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	342	3	0	6	2.3	Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2	10.1016/j.bmcl.2009.11.032
	46225407	206516	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593532	206516	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21	10.1016/j.bmcl.2009.11.032
	46225359	206608	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	418	5	0	6	3.9	Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	CHEMBL594236	206608	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	418	5	0	6	3.9	Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	46225334	206825	0	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595607	206825	0	None	-	1	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	358	3	0	4	3.7	Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225358	208641	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	485	5	0	5	5.5	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1	10.1016/j.bmcl.2009.11.032
	CHEMBL607195	208641	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	485	5	0	5	5.5	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1	10.1016/j.bmcl.2009.11.032
	24815439	208714	1	None	-	3	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607689	208714	1	None	-	3	Human	6.9	pEC50	=	6.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	323	3	0	3	4.1	Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225384	206676	4	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	328	3	1	5	2.3	Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	CHEMBL594673	206676	4	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	328	3	1	5	2.3	Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1	10.1016/j.bmcl.2009.11.032
	46225383	206876	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	395	3	1	4	4.0	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1	10.1016/j.bmcl.2009.11.032
	CHEMBL595991	206876	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	395	3	1	4	4.0	FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1	10.1016/j.bmcl.2009.11.032
	69929646	147097	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	329	2	1	6	1.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806226	147097	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	329	2	1	6	1.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21	10.1021/acsmedchemlett.5b00459
	127038185	144721	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	248	2	0	4	2.4	COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3763995	144721	0	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	248	2	0	4	2.4	COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	90643868	118638	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	CHEMBL3287690	118638	0	None	-	0	Rat	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	164608826	191246	0	None	-	0	Rat	7.9	pEC50	=	7.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4846872	191246	0	None	-	0	Rat	7.9	pEC50	=	7.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	11	2	6	5.3	COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	68108429	156458	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	448	5	0	4	5.7	FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3947590	156458	0	None	-	0	Human	7.9	pEC50	=	7.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	448	5	0	4	5.7	FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	53390677	89463	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	451	6	1	5	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179629	89463	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	451	6	1	5	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	53390520	89471	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	445	6	1	3	5.7	O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	CHEMBL2179637	89471	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	445	6	1	3	5.7	O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	6604704	108177	35	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970719q
	CHEMBL29726	108177	35	None	-	0	Human	4.9	pEC50	=	4.9	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1	10.1021/jm970719q
	49822195	152960	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3919978	152960	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	162657776	190462	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1176	30	6	12	11.7	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4759458	190462	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1176	30	6	12	11.7	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4803052	190462	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1176	30	6	12	11.7	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	25195461	8925	48	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	86765132	118673	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	428	10	2	5	5.6	Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287725	118673	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	428	10	2	5	5.6	Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	164613604	191963	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4857426	191963	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	11362035	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	6328	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	6329	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	CHEMBL105296	6831	1	None	-	1	Human	7.9	pEC50	=	7.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	10.1016/j.bmcl.2004.04.017
	23521659	11618	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	6	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104260	11618	0	None	-	0	Human	6.9	pEC50	=	6.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	6	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	23521713	116546	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL323138	116546	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	49822116	153770	13	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	5.9	pEC50	=	5.9	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	44395191	73074	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.6	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL184838	73074	0	None	-	0	Human	5.9	pEC50	=	5.9	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.6	CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	164621278	192311	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4862801	192311	0	None	-	0	Rat	6.9	pEC50	=	6.9	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	25195461	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	49765871	8926	45	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1016/j.bmc.2022.116614
	6317	8926	45	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1016/j.bmc.2022.116614
	CHEMBL2179319	8926	45	None	-	1	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1016/j.bmc.2022.116614
	90643858	118643	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287695	118643	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	90643905	118663	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287715	118663	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O	10.1021/jm5000563
	67056141	146987	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	4	0	8	2.9	Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1	10.1021/acsmedchemlett.5b00459
	CHEMBL3805017	146987	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	4	0	8	2.9	Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1	10.1021/acsmedchemlett.5b00459
	68107810	152932	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3919807	152932	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	432	5	0	4	5.2	Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	68108457	155335	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3938796	155335	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	127039577	144743	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	462	6	1	5	5.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764173	144743	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	462	6	1	5	5.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21	10.1016/j.bmcl.2016.01.021
	9885608	11623	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1021/jm034015u
	CHEMBL104296	11623	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1021/jm034015u
	9885608	11623	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL104296	11623	1	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	90643863	118633	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287683	118633	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	90643865	118635	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287687	118635	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	418	11	2	5	5.0	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	90643878	118649	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287701	118649	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	90668092	116314	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	CHEMBL3221831	116314	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay	ChEMBL	306	6	1	3	4.1	CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O	10.1039/C0MD00200C
	46225371	206602	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	453	6	0	6	4.1	COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594204	206602	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	453	6	0	6	4.1	COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225372	208144	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	356	4	0	6	2.8	CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604472	208144	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	356	4	0	6	2.8	CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225582	208394	0	None	-	2	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL605831	208394	0	None	-	2	Human	6.8	pEC50	=	6.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	3461070	124124	1	None	-	0	Human	4.8	pEC50	=	4.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	307	3	0	5	2.3	Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL339714	124124	1	None	-	0	Human	4.8	pEC50	=	4.8	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	307	3	0	5	2.3	Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44335554	116000	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL321746	116000	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.5	CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	71479388	147001	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805139	147001	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	23521708	11597	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104191	11597	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	23521727	11674	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL104541	11674	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	44335514	11723	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.3	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104785	11723	0	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.3	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	44404948	77329	0	None	-	1	Rat	4.8	pEC50	=	4.8	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	CHEMBL194787	77329	0	None	-	1	Rat	4.8	pEC50	=	4.8	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	1310	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	9095	110	None	-13	18	Rat	4.8	pEC50	=	4.8	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	90643895	118651	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	CHEMBL3287703	118651	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	388	10	2	6	3.8	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C	10.1021/jm5000563
	90643880	118657	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	CHEMBL3287709	118657	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	402	11	2	6	4.2	CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O	10.1021/jm5000563
	24905705	190801	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL482081	190801	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	25195461	8925	48	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	5.8	pEC50	=	5.8	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	164616255	191727	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	445	10	2	5	5.1	CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F	10.1016/j.bmcl.2021.128342
	CHEMBL4853748	191727	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	445	10	2	5	5.1	CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F	10.1016/j.bmcl.2021.128342
	11663312	70243	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	497	7	0	4	7.8	O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	CHEMBL179839	70243	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	497	7	0	4	7.8	O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1	10.1016/j.bmcl.2005.01.077
	24905705	190801	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL482081	190801	1	None	-	0	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	219	7	4	4	-0.6	N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	44335555	11808	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.4	CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105193	11808	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	416	9	0	4	4.4	CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	49765871	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	134156113	157650	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	483	5	0	5	5.3	FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3957311	157650	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	483	5	0	5	5.3	FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	71117730	150709	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	CHEMBL3902193	150709	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21	nan
	46182736	7776	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm3005306
	6323	7776	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm3005306
	CHEMBL1651219	7776	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm3005306
	53390521	89472	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O	10.1021/jm3005306
	CHEMBL2179638	89472	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O	10.1021/jm3005306
	46182736	7776	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm1012165
	6323	7776	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm1012165
	CHEMBL1651219	7776	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	479	6	1	5	6.8	OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1	10.1021/jm1012165
	1402	6910	44	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.08.020
	9825084	6910	44	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.08.020
	CHEMBL108939	6910	44	None	-	0	Human	5.8	pEC50	=	5.8	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1016/j.bmcl.2004.08.020
	90643882	118664	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	10	2	5	4.6	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O	10.1021/jm5000563
	CHEMBL3287716	118664	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	10	2	5	4.6	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O	10.1021/jm5000563
	90643876	118647	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287699	118647	0	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	44335578	116451	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.2	CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL322588	116451	0	None	-	0	Human	7.8	pEC50	=	7.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.2	CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	66787355	163004	0	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	163004	0	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	23521698	115323	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	384	7	0	3	4.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL320151	115323	0	None	-	0	Human	6.8	pEC50	=	6.8	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	384	7	0	3	4.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	11648824	64100	1	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	488	6	1	3	7.4	Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1021/jm1012165
	CHEMBL1651207	64100	1	None	-	0	Rat	6.8	pEC50	=	6.8	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	488	6	1	3	7.4	Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1021/jm1012165
	1310	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	1369	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	33032	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	44272391	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	88747398	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	CHEMBL575060	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	DB00142	9095	110	None	-22	18	Human	5.8	pEC50	=	5.8	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	1310	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	9095	110	None	-13	18	Rat	5.8	pEC50	=	5.8	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	89497771	144772	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764530	144772	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	1	5	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21	10.1016/j.bmcl.2016.01.021
	1310	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	1369	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	33032	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	44272391	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	88747398	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	CHEMBL575060	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	DB00142	9095	110	None	-13	18	Rat	5.7	pEC50	=	5.7	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/acs.jmedchem.5b01333
	10407808	73449	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	386	11	2	5	4.5	CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185419	73449	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	386	11	2	5	4.5	CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	90643887	118671	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287723	118671	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	89735344	144822	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	0	5	3.5	COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765257	144822	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	325	3	0	5	3.5	COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	11213605	71239	3	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	8	0	4	7.4	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL181364	71239	3	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	8	0	4	7.4	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	127042771	144831	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3765337	144831	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21	10.1016/j.bmcl.2016.01.021
	90643869	118639	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287691	118639	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	89497792	144814	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3765103	144814	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21	10.1016/j.bmcl.2016.01.021
	164611067	191395	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4849142	191395	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	11633075	72164	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	5	1	5	4.8	CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL182946	72164	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	5	1	5	4.8	CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	25125217	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	7678	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3937907	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	DB16073	7343	25	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.6b00913
	24815434	206475	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593196	206475	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	305	3	0	3	4.0	Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225335	206826	0	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595608	206826	0	None	-	1	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225583	206953	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596527	206953	0	None	-	3	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	362	3	0	5	4.6	Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225408	208653	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607313	208653	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	427	3	0	5	4.1	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21	10.1016/j.bmcl.2009.11.032
	46225387	206542	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	477	3	0	5	5.0	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593756	206542	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	477	3	0	5	5.0	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21	10.1016/j.bmcl.2009.11.032
	56968082	150689	0	None	-	0	Human	8.6	pEC50	=	8.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	428	5	0	4	5.3	CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1	10.1021/acs.jmedchem.6b00913
	CHEMBL3901998	150689	0	None	-	0	Human	8.6	pEC50	=	8.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	428	5	0	4	5.3	CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1	10.1021/acs.jmedchem.6b00913
	25051025	189246	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL478646	189246	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	53390433	89466	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	443	6	2	4	5.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O	10.1021/jm3005306
	CHEMBL2179632	89466	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	443	6	2	4	5.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O	10.1021/jm3005306
	66799514	89478	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	431	4	1	2	6.3	O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179646	89478	0	None	-	0	Rat	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	431	4	1	2	6.3	O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	23521677	114231	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL318309	114231	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1	10.1016/j.bmcl.2004.04.017
	53390754	89475	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	490	7	1	7	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1	10.1021/jm3005306
	CHEMBL2179643	89475	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	490	7	1	7	6.0	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1	10.1021/jm3005306
	90643897	118653	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287705	118653	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	104766	6822	42	None	-11	11	Human	5.7	pEC50	=	5.7	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970719q
	1365	6822	42	None	-11	11	Human	5.7	pEC50	=	5.7	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970719q
	CHEMBL34453	6822	42	None	-11	11	Human	5.7	pEC50	=	5.7	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm970719q
	25195461	8925	48	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	10002415	172805	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	423	11	2	7	4.0	CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL425540	172805	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	423	11	2	7	4.0	CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	90643889	118674	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1021/jm5000563
	CHEMBL3287726	118674	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1021/jm5000563
	49822115	8927	21	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	8947	8927	21	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL3947764	8927	21	None	-	1	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	11275666	96832	1	None	-15	2	Human	7.7	pEC50	=	7.7	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381647	96832	1	None	-15	2	Human	7.7	pEC50	=	7.7	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	164627946	193163	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4875695	193163	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	44335500	11894	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.0	COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105671	11894	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	360	6	0	4	3.0	COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	23521734	116537	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL323080	116537	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	25051018	191128	0	None	-	0	Rat	5.7	pEC50	=	5.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	334	5	0	5	2.7	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21	10.1016/j.bmcl.2008.09.026
	CHEMBL484398	191128	0	None	-	0	Rat	5.7	pEC50	=	5.7	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	334	5	0	5	2.7	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21	10.1016/j.bmcl.2008.09.026
	54761054	144859	0	None	-	2	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	144859	0	None	-	2	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	71136691	150399	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	CHEMBL3899706	150399	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	394	3	0	5	3.2	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21	nan
	134157889	160995	0	None	-	0	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	465	5	0	5	4.7	Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3985987	160995	0	None	-	0	Human	7.7	pEC50	=	7.7	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	465	5	0	5	4.7	Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	50993967	64106	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	433	6	1	3	5.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651213	64106	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	433	6	1	3	5.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	51037131	147062	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	356	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805883	147062	0	None	-	0	Human	5.7	pEC50	=	5.7	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	356	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21	10.1021/acsmedchemlett.5b00459
	90643860	118626	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287675	118626	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	164611059	191358	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4848600	191358	0	None	-	0	Rat	6.7	pEC50	=	6.7	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	11496256	70560	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL180186	70560	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	11656483	130381	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	514	9	1	6	6.3	CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361837	130381	0	None	-	0	Human	6.7	pEC50	=	6.7	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	514	9	1	6	6.3	CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643873	118644	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	13	2	6	5.4	Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287696	118644	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	13	2	6	5.4	Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	9979770	73112	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185054	73112	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.3	Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	49765871	8926	45	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	44335614	12059	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	446	9	0	6	3.3	CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL106561	12059	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	446	9	0	6	3.3	CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	45082292	122029	2	None	-3	3	Human	4.6	pEC50	=	4.6	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347670	122029	2	None	-3	3	Human	4.6	pEC50	=	4.6	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	90643906	118665	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287717	118665	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	10	2	5	4.8	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C	10.1021/jm5000563
	49822116	153770	13	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	90643875	118646	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287698	118646	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	44578992	188401	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	333	5	0	4	3.3	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL477376	188401	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	333	5	0	4	3.3	Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	44335556	8082	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	10.1016/j.bmcl.2004.04.017
	6257	8082	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	10.1016/j.bmcl.2004.04.017
	CHEMBL321968	8082	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	414	7	0	4	4.3	FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F	10.1016/j.bmcl.2004.04.017
	53390753	89476	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F	10.1021/jm3005306
	CHEMBL2179644	89476	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F	10.1021/jm3005306
	44395327	73699	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	438	11	2	7	4.7	CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL186584	73699	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	438	11	2	7	4.7	CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	90643862	118632	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	458	11	1	4	6.7	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	CHEMBL3287682	118632	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	458	11	1	4	6.7	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	44401995	76851	4	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	13	3	6	4.9	Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL193982	76851	4	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	13	3	6	4.9	Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	71117222	152863	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3919237	152863	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.6	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	53390676	89460	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	7	1	5	6.1	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179626	89460	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	7	1	5	6.1	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	54761054	144859	0	None	-	2	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	144859	0	None	-	2	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	44335650	11574	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	7	1	4	3.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104129	11574	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	7	1	4	3.5	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	25050850	198567	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL519817	198567	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	46225385	208142	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	439	4	0	6	4.0	COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C	10.1016/j.bmcl.2009.11.032
	CHEMBL604469	208142	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	439	4	0	6	4.0	COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C	10.1016/j.bmcl.2009.11.032
	46225375	208652	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	437	5	0	5	4.8	CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL607311	208652	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	437	5	0	5	4.8	CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	60096211	96834	0	None	-5	2	Human	6.6	pEC50	=	6.6	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL2381649	96834	0	None	-5	2	Human	6.6	pEC50	=	6.6	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	164619969	192308	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4862778	192308	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	25195461	8925	48	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	90643891	118629	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	424	11	1	4	6.0	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	CHEMBL3287678	118629	0	None	-	0	Rat	5.6	pEC50	=	5.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	424	11	1	4	6.0	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C	10.1021/jm5000563
	90643898	118654	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	376	9	2	5	4.0	CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	CHEMBL3287706	118654	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	376	9	2	5	4.0	CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	44578946	188381	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	375	6	0	4	4.5	CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL477169	188381	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	375	6	0	4	4.5	CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	44578947	188382	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	367	5	0	4	4.0	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL477170	188382	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	367	5	0	4	4.0	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	25110722	196316	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL514218	196316	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	68108294	154065	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	444	6	0	5	4.8	COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3928875	154065	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	444	6	0	5	4.8	COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	68108567	160532	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3981882	160532	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	89735130	144728	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764057	144728	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	71128768	151358	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3907644	151358	0	None	-	0	Human	7.6	pEC50	=	7.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	441	4	0	7	2.7	Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	50993968	64107	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	469	6	1	3	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651214	64107	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	469	6	1	3	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	164619502	192979	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4872955	192979	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	25195461	8925	48	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	44335577	12654	3	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.0	CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL107948	12654	3	None	-	0	Human	7.6	pEC50	=	7.6	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	402	8	0	4	4.0	CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	49765871	8926	45	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	7.6	pEC50	=	7.6	Binding	Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	11677757	72875	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	500	8	1	6	6.0	CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183911	72875	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	500	8	1	6	6.0	CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	1402	6910	44	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1021/jm034015u
	9825084	6910	44	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1021/jm034015u
	CHEMBL108939	6910	44	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2	ChEMBL	452	8	0	5	4.8	COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1	10.1021/jm034015u
	50994049	64108	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.6	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651215	64108	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.6	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	11598292	136953	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	486	7	1	6	5.6	CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL367823	136953	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	486	7	1	6	5.6	CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	164611777	191704	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4853369	191704	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	164621310	192344	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	429	10	2	6	5.0	Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4863303	192344	0	None	-	0	Rat	7.6	pEC50	=	7.6	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	429	10	2	6	5.0	Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O	10.1016/j.bmcl.2021.128342
	11344646	133554	1	None	-1	2	Human	7.5	pEC50	=	7.5	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	CHEMBL365368	133554	1	None	-1	2	Human	7.5	pEC50	=	7.5	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm4000165
	162650303	190427	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1064	22	6	12	8.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4748549	190427	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1064	22	6	12	8.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802664	190427	0	None	-	0	Rat	6.6	pEC50	=	6.6	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1064	22	6	12	8.6	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	11625861	72634	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	6	1	5	4.9	CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183541	72634	0	None	-	0	Human	6.6	pEC50	=	6.6	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	416	6	1	5	4.9	CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	71136188	152533	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	CHEMBL3916627	152533	0	None	-	0	Human	5.6	pEC50	=	5.6	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	384	3	1	6	1.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21	nan
	44335626	12166	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	4.7	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL107114	12166	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	428	7	0	4	4.7	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1	10.1016/j.bmcl.2004.04.017
	51036108	147005	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805203	147005	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	127052897	147086	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806137	147086	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	1310	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	1369	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	33032	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	44272391	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	88747398	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	CHEMBL575060	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	DB00142	9095	110	None	-22	18	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm970719q
	11697718	70956	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	431	8	0	4	6.7	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL180871	70956	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	431	8	0	4	6.7	CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O	10.1016/j.bmcl.2005.01.077
	164624801	192990	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4873125	192990	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	9	2	5	5.3	Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	71136186	158848	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	CHEMBL3967432	158848	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	431	3	0	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21	nan
	25110723	196418	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL515034	196418	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	1377	8122	26	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm00009a001
	5310979	8122	26	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm00009a001
	CHEMBL284193	8122	26	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm00009a001
	50994823	64112	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651221	64112	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	475	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	44578996	188364	0	None	-	0	Rat	5.5	pEC50	=	5.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	6	0	4	4.1	c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL476965	188364	0	None	-	0	Rat	5.5	pEC50	=	5.5	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	6	0	4	4.1	c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	10251009	73555	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.1	CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185911	73555	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.1	CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	164611874	191893	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	CHEMBL4856242	191893	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O	10.1016/j.bmcl.2021.128342
	56651050	144736	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	294	2	0	3	4.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764108	144736	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	294	2	0	3	4.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21	10.1016/j.bmcl.2016.01.021
	44335670	11735	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104818	11735	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	366	7	0	3	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	50994757	64111	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651220	64111	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	6	1	5	6.3	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl	10.1021/jm1012165
	89735684	144804	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1	10.1016/j.bmcl.2016.01.021
	CHEMBL3764850	144804	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1	10.1016/j.bmcl.2016.01.021
	46225336	206827	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595609	206827	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	363	3	0	6	3.5	Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225320	207962	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL603443	207962	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	374	3	0	4	3.9	Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225569	208141	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL604467	208141	0	None	-	1	Human	6.5	pEC50	=	6.5	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	373	3	0	3	5.0	Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44335573	11596	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	388	7	0	4	3.8	CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL104190	11596	0	None	-	0	Human	7.5	pEC50	=	7.5	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	388	7	0	4	3.8	CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	10846649	108008	4	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O	10.1021/jm970719q
	CHEMBL296054	108008	4	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O	10.1021/jm970719q
	11743092	71364	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	12	2	7	4.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL181648	71364	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	12	2	7	4.4	CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	51036916	147091	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	350	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806176	147091	0	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	350	2	0	5	3.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21	10.1021/acsmedchemlett.5b00459
	90643893	118631	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287680	118631	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	9999945	73912	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	382	9	2	7	3.3	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187537	73912	0	None	-	0	Human	5.5	pEC50	=	5.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	382	9	2	7	3.3	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	90643883	118666	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O	10.1021/jm5000563
	CHEMBL3287718	118666	0	None	-	0	Rat	7.5	pEC50	=	7.5	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	416	12	2	6	4.6	CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O	10.1021/jm5000563
	10047169	9998	1	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.08.020
	1403	9998	1	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.08.020
	CHEMBL182371	9998	1	None	-	0	Human	6.5	pEC50	=	6.5	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	410	11	2	7	4.0	CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C	10.1016/j.bmcl.2004.08.020
	1377	8122	26	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	5310979	8122	26	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL284193	8122	26	None	-1	6	Rat	6.5	pEC50	=	6.5	Binding	Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	53321382	64109	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	551	7	1	3	7.5	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651216	64109	0	None	-	0	Rat	6.5	pEC50	=	6.5	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	551	7	1	3	7.5	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	59066632	213349	89	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm020122x
	92136	213349	89	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm020122x
	CHEMBL88804	213349	89	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm020122x
	6603885	108978	23	None	-	0	Rat	4.5	pEC50	=	4.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	158	2	3	5	-0.5	N[C@H](C(=O)O)c1cc(O)no1	10.1021/jm00009a001
	6971208	108978	23	None	-	0	Rat	4.5	pEC50	=	4.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	158	2	3	5	-0.5	N[C@H](C(=O)O)c1cc(O)no1	10.1021/jm00009a001
	CHEMBL30285	108978	23	None	-	0	Rat	4.5	pEC50	=	4.5	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	158	2	3	5	-0.5	N[C@H](C(=O)O)c1cc(O)no1	10.1021/jm00009a001
	59066632	213349	89	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9703597
	92136	213349	89	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9703597
	CHEMBL88804	213349	89	None	-	1	Rat	4.5	pEC50	=	4.5	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	161	5	3	3	-0.3	N[C@@H](CCCC(=O)O)C(=O)O	10.1021/jm9703597
	23521697	11799	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	400	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105151	11799	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	400	7	0	4	3.9	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1	10.1016/j.bmcl.2004.04.017
	69930179	147050	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	433	3	0	6	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805718	147050	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	433	3	0	6	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21	10.1021/acsmedchemlett.5b00459
	23521709	171244	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL421406	171244	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	368	7	0	4	4.2	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	44404948	77329	0	None	-	1	Rat	4.4	pEC50	=	4.4	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	CHEMBL194787	77329	0	None	-	1	Rat	4.4	pEC50	=	4.4	Binding	Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells	ChEMBL	214	2	3	5	-1.0	NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1	10.1021/jm0504499
	69929785	146973	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	407	3	0	8	2.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3804845	146973	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	407	3	0	8	2.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21	10.1021/acsmedchemlett.5b00459
	9837114	122043	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	CHEMBL334842	122043	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	9837114	122043	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	CHEMBL334842	122043	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	11691077	71468	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL181869	71468	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	456	5	1	5	5.7	CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	164624284	192808	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4870631	192808	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	54761055	144665	1	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763172	144665	1	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21	10.1016/j.bmcl.2016.01.021
	69092138	149573	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3892865	149573	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	1368	9070	37	None	-3	11	Human	6.4	pEC50	=	6.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	5310956	9070	37	None	-3	11	Human	6.4	pEC50	=	6.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	CHEMBL280563	9070	37	None	-3	11	Human	6.4	pEC50	=	6.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	10318576	73487	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.7	CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185602	73487	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	396	10	2	7	3.7	CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O	10.1016/j.bmcl.2004.08.020
	3954	7451	60	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm3005306
	9868580	7451	60	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm3005306
	CHEMBL593013	7451	60	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm3005306
	3954	7451	60	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm1012165
	9868580	7451	60	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm1012165
	CHEMBL593013	7451	60	None	-	1	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/jm1012165
	10560963	171296	1	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	CHEMBL42148	171296	1	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	164610692	191681	0	None	-	0	Rat	5.4	pEC50	=	5.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	459	10	1	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4853089	191681	0	None	-	0	Rat	5.4	pEC50	=	5.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	459	10	1	5	5.4	Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	49765871	8926	45	None	-	1	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	46225584	206454	0	None	-	3	Human	7.4	pEC50	=	7.4	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593056	206454	0	None	-	3	Human	7.4	pEC50	=	7.4	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	408	3	0	4	5.0	Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	49765871	8926	45	None	-	1	Human	8.3	pEC50	=	8.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	8.3	pEC50	=	8.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	8.3	pEC50	=	8.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	90643858	118643	0	None	-	0	Rat	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287695	118643	0	None	-	0	Rat	7.4	pEC50	=	7.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	430	12	2	6	4.9	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	71116701	151637	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	CHEMBL3909811	151637	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	387	4	1	4	2.4	CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O	nan
	1310	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	1369	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	33032	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	44272391	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	88747398	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	CHEMBL575060	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	DB00142	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm020122x
	1310	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	1369	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	33032	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	44272391	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	88747398	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	CHEMBL575060	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	DB00142	9095	110	None	-13	18	Rat	5.4	pEC50	=	5.4	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	139054390	211702	106	None	-1	5	Rat	5.4	pEC50	=	5.4	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	10.1021/jm9703597
	23327	211702	106	None	-1	5	Rat	5.4	pEC50	=	5.4	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	10.1021/jm9703597
	CHEMBL76232	211702	106	None	-1	5	Rat	5.4	pEC50	=	5.4	Binding	Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	10.1021/jm9703597
	10465478	28557	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	CHEMBL131922	28557	0	None	-	0	Human	4.4	pEC50	=	4.4	Binding	Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1039/C1MD00186H
	10465478	28557	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	CHEMBL131922	28557	0	None	-	0	Rat	4.4	pEC50	=	4.4	Binding	Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2	ChEMBL	203	4	3	6	-0.4	N[C@@H](CCc1nsnc1O)C(=O)O	10.1021/jm020122x
	90643892	118630	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287679	118630	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	25050849	191021	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21	10.1016/j.bmcl.2008.09.026
	CHEMBL483569	191021	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	402	5	0	5	3.7	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21	10.1016/j.bmcl.2008.09.026
	23521725	12472	0	None	-	0	Human	5.4	pEC50	=	5.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL107806	12472	0	None	-	0	Human	5.4	pEC50	=	5.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	4	3.7	CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1	10.1016/j.bmcl.2004.04.017
	10026879	73803	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	13	2	7	5.0	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187077	73803	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	452	13	2	7	5.0	CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O	10.1016/j.bmcl.2004.08.020
	90643879	118650	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	12	2	6	5.4	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	CHEMBL3287702	118650	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	456	12	2	6	5.4	COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	51036701	146977	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	302	2	0	5	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3804903	146977	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	302	2	0	5	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21	10.1021/acsmedchemlett.5b00459
	71116772	154447	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	CHEMBL3931730	154447	0	None	-	0	Human	7.4	pEC50	=	7.4	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	456	4	1	8	3.7	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21	nan
	23521693	12127	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL106909	12127	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	382	8	0	4	4.0	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	11496550	70665	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	473	5	1	4	5.8	CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1	10.1016/j.bmcl.2005.01.077
	CHEMBL180455	70665	0	None	-	0	Human	6.4	pEC50	=	6.4	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	473	5	1	4	5.8	CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1	10.1016/j.bmcl.2005.01.077
	164615875	192223	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4861618	192223	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	9	2	5	5.4	Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	49822116	153770	13	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	90643861	118627	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287676	118627	0	None	-	0	Rat	6.4	pEC50	=	6.4	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	90643867	118637	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287689	118637	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	414	11	2	5	5.2	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C	10.1021/jm5000563
	49765871	8926	45	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	127038550	144841	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3765412	144841	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	373	3	0	6	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21	10.1016/j.bmcl.2016.01.021
	90643888	118672	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	CHEMBL3287724	118672	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	6	5.3	COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1021/jm5000563
	71681824	96831	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	CHEMBL2381646	96831	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	200	2	4	4	-1.6	N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	53390605	89462	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	467	7	1	5	6.3	CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	CHEMBL2179628	89462	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	467	7	1	5	6.3	CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	1310	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	1369	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	33032	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	44272391	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	88747398	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	CHEMBL575060	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	DB00142	9095	110	None	-22	18	Human	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm00009a001
	164623088	192264	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4862244	192264	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	71574840	93046	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL2312685	93046	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	89497505	144706	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	378	3	1	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763754	144706	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	378	3	1	6	3.5	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21	10.1016/j.bmcl.2016.01.021
	164610947	192030	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	415	10	2	6	4.7	Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4858387	192030	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	415	10	2	6	4.7	Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	71574840	93046	0	None	-	0	Rat	4.3	pEC50	=	4.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	CHEMBL2312685	93046	0	None	-	0	Rat	4.3	pEC50	=	4.3	Binding	Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay	ChEMBL	204	7	4	4	-0.8	NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O	10.1021/acs.jmedchem.5b01333
	44395282	129935	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL361248	129935	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	46182745	64101	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL1651208	64101	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm3005306
	46182745	64101	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651208	64101	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	461	6	1	3	6.2	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	90643899	118655	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287707	118655	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	372	9	2	5	4.1	CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	164620553	192548	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4866466	192548	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	9	2	5	5.8	Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	46225386	206541	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	434	3	0	6	3.8	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593755	206541	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	434	3	0	6	3.8	Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21	10.1016/j.bmcl.2009.11.032
	11690041	71642	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	408	6	1	5	4.5	CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL182138	71642	0	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	408	6	1	5	4.5	CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	104766	6822	42	None	-3	11	Rat	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	1365	6822	42	None	-3	11	Rat	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	CHEMBL34453	6822	42	None	-3	11	Rat	5.3	pEC50	=	5.3	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	46225373	206603	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	386	6	0	7	2.4	COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594205	206603	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	386	6	0	7	2.4	COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225337	206756	0	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL595151	206756	0	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	375	3	0	5	3.3	Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	851990	206484	4	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	306	3	0	4	2.9	Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593300	206484	4	None	-	0	Human	5.3	pEC50	=	5.3	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	306	3	0	4	2.9	Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	164618046	192241	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	471	10	1	6	5.1	COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4861837	192241	0	None	-	0	Rat	5.3	pEC50	=	5.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	471	10	1	6	5.1	COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	71116730	155841	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	CHEMBL3942904	155841	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	424	3	1	6	2.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21	nan
	90643864	118634	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287684	118634	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	460	11	2	5	6.1	Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	44578997	188365	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476966	188365	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	164625596	192521	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4866163	192521	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	428	10	2	5	5.6	Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	11699129	138743	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	509	6	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL369526	138743	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	509	6	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643885	118668	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287720	118668	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	400	11	2	5	4.9	CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	117972250	149090	3	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885379	149090	3	None	-	1	Human	6.3	pEC50	=	6.3	Binding	Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	71128783	146986	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	397	3	0	7	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805005	146986	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	397	3	0	7	2.8	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21	10.1021/acsmedchemlett.5b00459
	162677305	190572	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1078	23	6	12	9.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4800093	190572	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1078	23	6	12	9.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4804159	190572	0	None	-	0	Rat	7.3	pEC50	=	7.3	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1078	23	6	12	9.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	71116952	154092	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	CHEMBL3929070	154092	0	None	-	0	Human	7.3	pEC50	=	7.3	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	2.9	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21	nan
	10775369	185144	1	None	-	0	Human	4.3	pEC50	=	4.3	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	CHEMBL46527	185144	1	None	-	0	Human	4.3	pEC50	=	4.3	Binding	Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).	ChEMBL	185	2	3	3	-0.5	N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O	10.1021/jm970719q
	11684927	70250	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	511	7	0	4	8.2	CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL179876	70250	0	None	-	0	Human	6.3	pEC50	=	6.3	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	511	7	0	4	8.2	CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	90643877	118648	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	CHEMBL3287700	118648	0	None	-	0	Rat	6.3	pEC50	=	6.3	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O	10.1021/jm5000563
	68108604	154182	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	480	7	0	5	5.2	Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3929786	154182	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	480	7	0	5	5.2	Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	68107740	158322	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	466	6	0	5	5.0	Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3963034	158322	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	466	6	0	5	5.0	Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	89735006	144723	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3764005	144723	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	309	2	0	4	3.8	Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	88593167	157538	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	482	5	0	4	5.8	FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3956434	157538	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	482	5	0	4	5.8	FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	53390675	89461	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	6	1	5	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179627	89461	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	465	6	1	5	6.4	O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	11676185	72364	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	422	7	1	5	4.8	CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183234	72364	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	422	7	1	5	4.8	CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	44390403	129114	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	457	7	0	4	7.1	Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2005.01.077
	CHEMBL359909	129114	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	457	7	0	4	7.1	Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2005.01.077
	50994051	64110	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	8	1	3	6.3	CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	CHEMBL1651217	64110	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	463	8	1	3	6.3	CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	11663353	130016	1	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	499	6	2	6	5.1	CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361358	130016	1	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	499	6	2	6	5.1	CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	54761054	144859	0	None	-	2	Human	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	144859	0	None	-	2	Human	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	90643870	118640	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	CHEMBL3287692	118640	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	440	11	2	5	5.7	Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C	10.1021/jm5000563
	54761054	144859	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765778	144859	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	11691314	188679	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	470	6	2	4	6.5	Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	CHEMBL4779278	188679	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	470	6	2	4	6.5	Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	162660656	190485	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1120	26	6	12	10.2	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4762369	190485	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1120	26	6	12	10.2	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4803219	190485	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1120	26	6	12	10.2	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	90643901	118658	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287710	118658	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O	10.1021/jm5000563
	23521692	115350	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	436	8	0	4	4.6	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL320292	115350	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	436	8	0	4	4.6	O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	11691221	130105	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	464	5	1	5	5.4	CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL361633	130105	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	464	5	1	5	5.4	CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	54761054	144859	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1021/acsmedchemlett.5b00459
	CHEMBL3765778	144859	0	None	-	2	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	367	3	1	5	4.0	Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1021/acsmedchemlett.5b00459
	164616933	191844	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4855540	191844	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	444	10	2	6	5.1	COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	46225357	206576	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	423	4	0	5	4.4	CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594011	206576	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	423	4	0	5	4.4	CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	11310142	9200	19	None	1	2	Human	7.2	pEC50	=	7.2	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm4000165
	11614	9200	19	None	1	2	Human	7.2	pEC50	=	7.2	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm4000165
	CHEMBL192051	9200	19	None	1	2	Human	7.2	pEC50	=	7.2	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm4000165
	51036108	147005	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3805203	147005	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	441	3	0	9	2.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21	10.1021/acsmedchemlett.5b00459
	90643872	118642	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287694	118642	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	25050844	191022	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL483570	191022	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21	10.1016/j.bmcl.2008.09.026
	44335613	175919	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	432	9	0	6	2.9	CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL440328	175919	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	432	9	0	6	2.9	CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	53390678	89459	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	425	5	1	5	5.2	Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	CHEMBL2179625	89459	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	425	5	1	5	5.2	Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	69093542	154205	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	CHEMBL3929950	154205	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.6b00913
	25195461	8925	48	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	53390604	89464	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	481	8	1	5	6.7	CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	CHEMBL2179630	89464	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	481	8	1	5	6.7	CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O	10.1021/jm3005306
	49822116	153770	13	None	-	1	Human	5.2	pEC50	=	5.2	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	5.2	pEC50	=	5.2	Binding	Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	127052897	147086	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806137	147086	0	None	-	0	Human	6.2	pEC50	=	6.2	Binding	Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	11568710	187199	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	CHEMBL4752318	187199	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2	10.1016/j.bmcl.2020.127212
	71116726	152054	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	CHEMBL3912982	152054	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	438	3	0	8	3.0	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21	nan
	90643866	118636	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287688	118636	0	None	-	0	Rat	6.2	pEC50	=	6.2	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	444	11	2	5	5.5	Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	44578905	188367	0	None	-	0	Rat	8.2	pEC50	=	8.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	5	0	4	3.6	Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476998	188367	0	None	-	0	Rat	8.2	pEC50	=	8.2	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	369	5	0	4	3.6	Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	11084869	96828	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	CHEMBL2381643	96828	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	70052526	96827	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	CHEMBL2381642	96827	2	None	-	1	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/jm4000165
	50993963	64102	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	435	6	1	3	5.6	CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	CHEMBL1651209	64102	0	None	-	0	Rat	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	435	6	1	3	5.6	CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O	10.1021/jm1012165
	89735186	144680	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	295	2	0	4	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3763395	144680	0	None	-	0	Human	7.2	pEC50	=	7.2	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	295	2	0	4	3.4	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21	10.1016/j.bmcl.2016.01.021
	10249222	11783	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL105065	11783	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	380	7	0	3	4.6	CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1	10.1016/j.bmcl.2004.04.017
	90643886	118669	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	11	2	5	4.8	CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	CHEMBL3287721	118669	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	404	11	2	5	4.8	CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O	10.1021/jm5000563
	53390680	89474	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	459	6	1	5	6.4	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1	10.1021/jm3005306
	CHEMBL2179642	89474	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	459	6	1	5	6.4	Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1	10.1021/jm3005306
	1310	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	1369	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	33032	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	44272391	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	88747398	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	CHEMBL575060	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	DB00142	9095	110	None	-22	18	Human	5.1	pEC50	=	5.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/s0960-894x(01)00656-4
	127052897	147086	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	CHEMBL3806137	147086	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay	ChEMBL	424	3	0	8	2.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21	10.1021/acsmedchemlett.5b00459
	164614107	191909	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4856556	191909	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	1368	9070	37	None	1	11	Rat	6.1	pEC50	=	6.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	5310956	9070	37	None	1	11	Rat	6.1	pEC50	=	6.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	CHEMBL280563	9070	37	None	1	11	Rat	6.1	pEC50	=	6.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10.1021/jm00009a001
	44395381	72913	0	None	-	0	Human	5.1	pEC50	=	5.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	10	2	8	3.5	CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL184098	72913	0	None	-	0	Human	5.1	pEC50	=	5.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	10	2	8	3.5	CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	11539379	72372	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	436	8	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL183286	72372	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	436	8	1	5	5.2	CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	25195461	8925	48	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	104766	6822	42	None	-3	11	Rat	5.1	pEC50	=	5.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	1365	6822	42	None	-3	11	Rat	5.1	pEC50	=	5.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	CHEMBL34453	6822	42	None	-3	11	Rat	5.1	pEC50	=	5.1	Binding	Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat	ChEMBL	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10.1021/jm00009a001
	49822116	153770	13	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	168278157	197138	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	435	4	0	3	6.4	Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1016/j.bmc.2022.116614
	CHEMBL5177038	197138	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	435	4	0	3	6.4	Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1016/j.bmc.2022.116614
	164616491	192170	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	CHEMBL4860693	192170	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	430	9	2	6	4.9	COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C	10.1016/j.bmcl.2021.128342
	23521714	11578	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1	10.1016/j.bmcl.2004.04.017
	CHEMBL104140	11578	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	378	7	0	3	4.5	C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1	10.1016/j.bmcl.2004.04.017
	11516962	70671	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	402	4	1	5	4.5	CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL180488	70671	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	402	4	1	5	4.5	CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	46190877	8652	7	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	6252	8652	7	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	CHEMBL605836	8652	7	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	409	3	0	5	4.0	Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F	10.1016/j.bmcl.2009.11.032
	24849462	206537	0	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL593744	206537	0	None	-	3	Human	7.1	pEC50	=	7.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	339	3	0	3	4.6	Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	46225374	206633	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	370	5	0	6	3.2	CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL594428	206633	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	370	5	0	6	3.2	CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	24849789	206913	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596270	206913	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	324	3	0	4	3.0	Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	798232	206914	9	None	-	1	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	340	3	0	4	3.5	Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	CHEMBL596271	206914	9	None	-	1	Human	6.1	pEC50	=	6.1	Binding	Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay	ChEMBL	340	3	0	4	3.5	Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21	10.1016/j.bmcl.2009.11.032
	44578948	188400	0	None	-	0	Rat	8.1	pEC50	=	8.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	385	5	0	4	4.1	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL477375	188400	0	None	-	0	Rat	8.1	pEC50	=	8.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	385	5	0	4	4.1	Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	71681823	96829	0	None	-	0	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	CHEMBL2381644	96829	0	None	-	0	Human	8.1	pEC50	=	8.1	Binding	Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay	ChEMBL	226	3	3	4	-0.2	[N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21	10.1021/jm4000165
	66799669	89465	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	CHEMBL2179631	89465	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	457	7	1	4	5.5	COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	53390432	89467	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	487	8	1	5	5.5	COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	CHEMBL2179633	89467	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	487	8	1	5	5.5	COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1	10.1021/jm3005306
	50993964	64103	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	7	1	3	5.7	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651210	64103	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	7	1	3	5.7	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	89735530	144801	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764820	144801	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	320	2	0	5	3.3	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21	10.1016/j.bmcl.2016.01.021
	164620998	192652	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4868114	192652	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	432	10	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	89735654	144726	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	313	2	0	4	3.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21	10.1016/j.bmcl.2016.01.021
	CHEMBL3764024	144726	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	313	2	0	4	3.6	Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21	10.1016/j.bmcl.2016.01.021
	90643903	118660	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	CHEMBL3287712	118660	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	386	10	2	5	4.5	CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O	10.1021/jm5000563
	90643859	118625	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	CHEMBL3287672	118625	0	None	-	0	Rat	6.1	pEC50	=	6.1	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	426	11	2	5	5.4	Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O	10.1021/jm5000563
	69092138	155514	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3940264	155514	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	464	6	1	4	5.8	Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	164612248	191669	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4852903	191669	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	418	8	2	5	5.0	Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	11648510	70042	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	7	0	4	7.3	CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL179171	70042	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	471	7	0	4	7.3	CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	11712790	188035	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	484	7	1	4	6.8	COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O	10.1016/j.bmcl.2020.127212
	CHEMBL4761801	188035	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	484	7	1	4	6.8	COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O	10.1016/j.bmcl.2020.127212
	44578949	188322	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	401	5	0	4	4.3	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL476551	188322	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	401	5	0	4	4.3	Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21	10.1016/j.bmcl.2008.09.026
	25050845	191167	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	CHEMBL484578	191167	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	368	5	0	5	3.4	Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21	10.1016/j.bmcl.2008.09.026
	86691853	144852	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	339	3	1	5	3.2	Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	CHEMBL3765537	144852	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay	ChEMBL	339	3	1	5	3.2	Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C	10.1016/j.bmcl.2016.01.021
	164609025	191220	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	10	2	5	5.9	Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	CHEMBL4846460	191220	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay	ChEMBL	448	10	2	5	5.9	Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O	10.1016/j.bmcl.2021.128342
	10343566	73474	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	446	9	2	7	3.8	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL185529	73474	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	446	9	2	7	3.8	CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	44335615	116843	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	460	9	0	6	3.7	CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	CHEMBL323541	116843	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2	ChEMBL	460	9	0	6	3.7	CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1	10.1016/j.bmcl.2004.04.017
	71119170	155551	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	CHEMBL3940610	155551	0	None	-	0	Human	7.1	pEC50	=	7.1	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	468	4	1	5	1.9	CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O	nan
	66786069	163240	0	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	163240	0	None	-	1	Human	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	11654949	54245	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	432	5	1	3	6.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	CHEMBL154542	54245	0	None	-	0	Human	6.1	pEC50	=	6.1	Binding	Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2	ChEMBL	432	5	1	3	6.2	CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O	10.1016/j.bmcl.2005.01.077
	71136746	155379	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	CHEMBL3939174	155379	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).	ChEMBL	421	3	0	7	3.1	Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21	nan
	68107813	151769	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	CHEMBL3910866	151769	0	None	-	0	Human	8.0	pEC50	=	8.0	Binding	Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method	ChEMBL	450	5	0	4	5.4	Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1	10.1021/acs.jmedchem.6b00913
	53390517	89468	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	CHEMBL2179634	89468	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	461	6	1	3	6.2	O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1	10.1021/jm3005306
	50993965	64104	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	6	1	3	5.8	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	CHEMBL1651211	64104	0	None	-	0	Rat	7.1	pEC50	=	7.1	Binding	Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels	ChEMBL	447	6	1	3	5.8	O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl	10.1021/jm1012165
	44395299	73824	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187151	73824	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	424	11	2	7	4.4	CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	162644103	190398	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1106	25	6	12	9.8	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4777845	190398	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1106	25	6	12	9.8	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802343	190398	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1106	25	6	12	9.8	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	10413231	131815	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	488	11	2	7	4.8	CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL364324	131815	0	None	-	0	Human	7.0	pEC50	=	7.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	488	11	2	7	4.8	CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O	10.1016/j.bmcl.2004.08.020
	10070087	74011	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	409	11	3	7	4.0	CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	CHEMBL187959	74011	0	None	-	0	Human	6.0	pEC50	=	6.0	Binding	Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay	ChEMBL	409	11	3	7	4.0	CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O	10.1016/j.bmcl.2004.08.020
	162646759	190411	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1148	28	6	12	11.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4740929	190411	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1148	28	6	12	11.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4802473	190411	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1148	28	6	12	11.0	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	90643874	118645	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	CHEMBL3287697	118645	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	434	11	2	5	5.5	Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O	10.1021/jm5000563
	44578903	188347	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	3.7	c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL476790	188347	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	359	5	0	4	3.7	c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	44578995	188345	0	None	-	0	Rat	5.0	pEC50	=	5.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	330	5	0	3	4.0	c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	CHEMBL476756	188345	0	None	-	0	Rat	5.0	pEC50	=	5.0	Binding	Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate	ChEMBL	330	5	0	3	4.0	c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1	10.1016/j.bmcl.2008.09.026
	90643890	118628	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	398	11	1	4	5.5	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C	10.1021/jm5000563
	CHEMBL3287677	118628	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay	ChEMBL	398	11	1	4	5.5	Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C	10.1021/jm5000563
	49822116	153770	13	None	-	1	Human	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	162666879	190512	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1092	24	6	12	9.4	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4786847	190512	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1092	24	6	12	9.4	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	CHEMBL4803552	190512	0	None	-	0	Rat	7.0	pEC50	=	7.0	Binding	Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay	ChEMBL	1092	24	6	12	9.4	COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl	10.1016/j.bmcl.2020.127212
	53390837	89477	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	506	6	0	5	6.8	CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	CHEMBL2179645	89477	0	None	-	0	Rat	6.0	pEC50	=	6.0	Binding	Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay	ChEMBL	506	6	0	5	6.8	CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl	10.1021/jm3005306
	89554832	149579	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	484	7	2	6	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3892899	149579	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	484	7	2	6	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71565964	151028	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	CHEMBL3904730	151028	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	124201729	153340	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	CHEMBL3922857	153340	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	89554927	153660	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	1	5	3.7	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1	nan
	CHEMBL3925389	153660	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	1	5	3.7	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1	nan
	71566125	153828	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	CHEMBL3926942	153828	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	89554857	154877	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	CHEMBL3935153	154877	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	71565965	155063	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	CHEMBL3936681	155063	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	71566127	155416	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	CHEMBL3939455	155416	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	89554768	156230	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	CHEMBL3946016	156230	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	71566207	157133	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3953157	157133	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554874	160250	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1	nan
	CHEMBL3979547	160250	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1	nan
	89554726	167490	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL4113710	167490	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	156012009	184136	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4637618	184136	0	None	-	0	Human	8.0	pIC50	=	8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22317767	63064	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629847	63064	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11269030	63078	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629861	63078	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	381	2	1	3	5.2	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2010.09.125
	22317741	63186	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631863	63186	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317279	63188	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631865	63188	0	None	-	0	Rat	8.0	pIC50	=	8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566440	150420	0	None	-	0	Human	7.0	pIC50	=	7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1	nan
	CHEMBL3899883	150420	0	None	-	0	Human	7.0	pIC50	=	7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1	nan
	22224818	153456	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	4	3.9	CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1	10.1016/j.bmcl.2007.10.026
	CHEMBL392381	153456	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	4	3.9	CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1	10.1016/j.bmcl.2007.10.026
	71565597	160735	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	4	1	4	2.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1	nan
	CHEMBL3983624	160735	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	4	1	4	2.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1	nan
	9905849	210832	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL69970	210832	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	71565672	158043	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	3	3.0	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3960294	158043	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	3	3.0	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554824	159316	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	6	4.3	CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3971590	159316	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	6	4.3	CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	89554770	150869	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3903459	150869	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554787	156688	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	455	5	1	6	3.4	NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3949371	156688	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	455	5	1	6	3.4	NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554900	157935	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	CHEMBL3959588	157935	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	89554749	158784	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	CHEMBL3966866	158784	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	89554828	166996	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1	nan
	CHEMBL4109697	166996	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1	nan
	89545222	167157	3	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4111091	167157	3	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	10115228	102948	0	None	-	0	Rat	8.0	pIC50	=	8.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260642	102948	0	None	-	0	Rat	8.0	pIC50	=	8.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	456	5	1	6	4.8	CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	57459488	90678	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206441	90678	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	57459494	90679	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206442	90679	0	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	414	5	0	5	4.9	COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	10428048	10134	31	None	-	1	Rat	7.0	pIC50	=	7.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	3955	10134	31	None	-	1	Rat	7.0	pIC50	=	7.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	CHEMBL305406	10134	31	None	-	1	Rat	7.0	pIC50	=	7.0	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	71566276	151202	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	381	5	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1	nan
	CHEMBL3906311	151202	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	381	5	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1	nan
	117642007	152509	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3916486	152509	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554827	160107	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1	nan
	CHEMBL3978247	160107	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1	nan
	89554725	167604	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL4114602	167604	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	44309100	109408	0	None	-	0	Rat	4.9	pIC50	=	4.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/s0960-894x(99)00346-7
	CHEMBL304285	109408	0	None	-	0	Rat	4.9	pIC50	=	4.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	297	4	0	4	4.0	CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl	10.1016/s0960-894x(99)00346-7
	89554830	158649	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3965612	158649	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554917	149914	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	3.6	CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL3895775	149914	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	3.6	CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	89554812	151354	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	3	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1	nan
	CHEMBL3907626	151354	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	3	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1	nan
	89554781	166772	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1	nan
	CHEMBL4107730	166772	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1	nan
	53320741	63189	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	471	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631866	63189	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	471	3	1	3	7.2	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566277	149543	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	5	1	5	4.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3892604	149543	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	5	1	5	4.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1	nan
	71566125	153828	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	CHEMBL3926942	153828	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	6	1	4	5.1	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1	nan
	89554755	158647	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3965606	158647	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	89554749	158784	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	CHEMBL3966866	158784	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	89554734	166940	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL4109210	166940	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1	nan
	22224657	102947	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260636	102947	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	18548739	167144	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL411095	167144	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	156016312	184512	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642428	184512	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22317847	63184	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631861	63184	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	420	2	1	4	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9952648	103083	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	103083	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	18548739	167144	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL411095	167144	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	89554801	149642	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL3893351	149642	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.9	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	18548785	63180	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	415	3	2	6	3.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631857	63180	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	415	3	2	6	3.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2	10.1016/j.bmcl.2010.09.125
	44309123	210649	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	365	4	0	4	5.7	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL68739	210649	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	365	4	0	4	5.7	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	71565668	157198	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1	nan
	CHEMBL3953821	157198	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1	nan
	71566518	159067	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	CHEMBL3969392	159067	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	71566202	159148	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	3	1	3	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1	nan
	CHEMBL3970177	159148	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	3	1	3	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1	nan
	53323293	63068	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629851	63068	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71565594	149805	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	2	4	4.2	CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3894815	149805	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	2	4	4.2	CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	123632099	150180	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	4	4.9	[C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3897968	150180	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	4	4.9	[C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1	nan
	89554871	150354	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	5	3.6	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3899261	150354	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	5	3.6	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	71565883	154345	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1	nan
	CHEMBL3930893	154345	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1	nan
	89554967	155458	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	0	5	3.6	COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1	nan
	CHEMBL3939827	155458	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	0	5	3.6	COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1	nan
	89554841	155675	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	382	4	1	4	4.0	N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3941663	155675	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	382	4	1	4	4.0	N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554833	167574	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1	nan
	CHEMBL4114374	167574	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1	nan
	89554925	167590	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	5	1	6	3.7	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4114497	167590	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	5	1	6	3.7	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	9909080	162061	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL402886	162061	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	402	2	1	4	4.7	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	156015264	184321	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4640203	184321	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22317724	63062	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629845	63062	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	11212447	63191	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631868	63191	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	2	4	5.0	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317620	63192	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631869	63192	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.7	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	53326017	63195	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631872	63195	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	44450454	102895	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	381	2	1	5	3.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260343	102895	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	381	2	1	5	3.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	11347391	73626	0	None	2	2	Rat	6.9	pIC50	=	6.9	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186214	73626	0	None	2	2	Rat	6.9	pIC50	=	6.9	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	71566520	151326	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1	nan
	CHEMBL3907349	151326	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1	nan
	89554899	154298	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	364	4	2	4	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1	nan
	CHEMBL3930631	154298	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	364	4	2	4	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1	nan
	89554784	149529	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	3.3	COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3892501	149529	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	3.3	COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	156010547	183943	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	280	1	1	4	2.4	O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12	10.1016/j.bmcl.2020.127066
	CHEMBL4634351	183943	0	None	-	0	Human	5.9	pIC50	=	5.9	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	280	1	1	4	2.4	O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12	10.1016/j.bmcl.2020.127066
	117642134	153838	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	4	3.4	CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	CHEMBL3927029	153838	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	4	3.4	CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	44309303	210842	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.0	FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1	10.1016/s0960-894x(99)00346-7
	CHEMBL70026	210842	0	None	-	0	Rat	5.9	pIC50	=	5.9	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.0	FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1	10.1016/s0960-894x(99)00346-7
	117644742	154412	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	3	1	3	3.1	COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	CHEMBL3931394	154412	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	3	1	3	3.1	COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1	nan
	89554852	154917	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3935453	154917	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1	nan
	89554870	155018	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	1	6	3.2	COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	CHEMBL3936247	155018	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	1	6	3.2	COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	71566126	155561	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	CHEMBL3940665	155561	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	89554745	156369	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3946940	156369	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	71566207	157133	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3953157	157133	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	5	3.5	COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554909	167113	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	468	5	1	6	4.1	C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4110690	167113	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	468	5	1	6	4.1	C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	89554960	167494	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1	nan
	CHEMBL4113735	167494	0	None	-	0	Human	7.9	pIC50	=	7.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1	nan
	22317185	63065	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629848	63065	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	410	2	2	4	5.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22317918	63074	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629858	63074	0	None	-	0	Rat	7.9	pIC50	=	7.9	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	3	2	4	5.3	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1	10.1016/j.bmcl.2010.09.125
	22448874	102073	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	493	5	2	6	4.3	CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL256424	102073	0	None	-	0	Rat	6.9	pIC50	=	6.9	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	493	5	2	6	4.3	CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	89554836	167403	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	4	2	7	3.2	C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4113073	167403	0	None	-	0	Human	6.9	pIC50	=	6.9	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	451	4	2	7	3.2	C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	156017916	184584	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4643527	184584	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554840	157293	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	3	0	5	4.5	Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3954534	157293	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	3	0	5	4.5	Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	89554892	157380	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL3955188	157380	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	71566275	158419	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1	nan
	CHEMBL3963813	158419	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1	nan
	117642068	161054	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1	nan
	CHEMBL3986471	161054	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1	nan
	71566522	156122	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3945170	156122	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	10.1016/j.bmcl.2020.127066
	49765871	8926	45	None	-	1	Human	7.8	pIC50	=	7.8	Binding	Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	6317	8926	45	None	-	1	Human	7.8	pIC50	=	7.8	Binding	Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	CHEMBL2179319	8926	45	None	-	1	Human	7.8	pIC50	=	7.8	Binding	Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/jm3010724
	89554911	149772	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	149772	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	89554889	151582	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	368	4	1	6	2.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1	nan
	CHEMBL3909377	151582	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	368	4	1	6	2.6	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1	nan
	89554788	153161	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1	nan
	CHEMBL3921588	153161	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1	nan
	89554753	153552	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3924490	153552	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	117642146	155266	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3938177	155266	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71566048	157503	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	CHEMBL3956202	157503	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	89554977	157920	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1	nan
	CHEMBL3959505	157920	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1	nan
	117641924	159186	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3970507	159186	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	71565961	160274	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	3.0	CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3979694	160274	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	3.0	CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	124201730	167181	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	CHEMBL4111267	167181	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	2	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1	nan
	44434257	158206	0	None	-	0	Rat	5.8	pIC50	=	5.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	318	1	1	2	4.5	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL396181	158206	0	None	-	0	Rat	5.8	pIC50	=	5.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	318	1	1	2	4.5	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2	10.1016/j.bmcl.2007.10.026
	22224695	95479	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	1	1	2	5.2	O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL236035	95479	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	1	1	2	5.2	O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	89543901	157353	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3955040	157353	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71565963	159491	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	487	5	1	6	3.5	NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3973004	159491	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	487	5	1	6	3.5	NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554753	153552	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3924490	153552	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	89554752	154161	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3929631	154161	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	502	7	2	6	4.6	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71565525	156695	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	4	1	4	2.9	NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3949476	156695	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	4	1	4	2.9	NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	71566048	157503	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	CHEMBL3956202	157503	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1	nan
	89554891	167439	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	CHEMBL4113348	167439	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	9952648	103083	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261288	103083	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	9952648	103083	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL261288	103083	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2010.09.125
	89554732	166949	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4109248	166949	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	156017027	184506	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642338	184506	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	53325611	63190	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631867	63190	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	485	4	1	3	7.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22448864	95957	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	494	2	1	6	3.7	N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236669	95957	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	494	2	1	6	3.7	N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554793	153119	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	2	4	4.0	CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	CHEMBL3921230	153119	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	2	4	4.0	CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1	nan
	89554846	149927	0	None	-	0	Human	5.8	pIC50	=	5.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	6	3.1	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1	nan
	CHEMBL3895854	149927	0	None	-	0	Human	5.8	pIC50	=	5.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	6	3.1	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1	nan
	89545189	159674	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	nan
	CHEMBL3974648	159674	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	nan
	71565885	160213	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	6	1	7	1.6	COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3979211	160213	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	6	1	7	1.6	COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	89554890	167644	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL4114982	167644	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	71566522	156122	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	nan
	CHEMBL3945170	156122	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	266	2	1	2	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1	nan
	89554932	156698	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	2.8	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1	nan
	CHEMBL3949512	156698	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	2.8	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1	nan
	71566349	160947	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1	nan
	CHEMBL3985577	160947	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1	nan
	89554829	149729	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL3894162	149729	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	71565596	151570	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.3	CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	CHEMBL3909273	151570	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.3	CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	89554881	155027	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	CHEMBL3936318	155027	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1	nan
	89554933	158202	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	490	6	2	5	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	CHEMBL3961788	158202	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	490	6	2	5	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	22224852	102639	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259054	102639	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	18548908	103039	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261051	103039	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	404	2	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	22224670	103042	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261081	103042	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	3	1	5	4.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	89554950	154997	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	443	5	1	5	4.5	Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1	nan
	CHEMBL3936050	154997	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	443	5	1	5	4.5	Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1	nan
	117642183	160154	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	354	4	0	4	4.5	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	CHEMBL3978639	160154	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	354	4	0	4	4.5	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	22224972	104471	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	430	2	1	4	5.4	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1	10.1016/j.bmcl.2007.12.005
	CHEMBL271319	104471	0	None	-	0	Rat	6.8	pIC50	=	6.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	430	2	1	4	5.4	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1	10.1016/j.bmcl.2007.12.005
	11503055	9179	3	None	-	0	Human	4.8	pIC50	=	4.8	Binding	Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1016/j.bmcl.2012.04.112
	9694	9179	3	None	-	0	Human	4.8	pIC50	=	4.8	Binding	Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1016/j.bmcl.2012.04.112
	CHEMBL2204436	9179	3	None	-	0	Human	4.8	pIC50	=	4.8	Binding	Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay	ChEMBL	400	4	1	4	3.9	Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br	10.1016/j.bmcl.2012.04.112
	71566435	159433	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	318	2	1	2	3.9	NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1	nan
	CHEMBL3972482	159433	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	318	2	1	2	3.9	NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1	nan
	89554799	167575	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1	nan
	CHEMBL4114381	167575	0	None	-	0	Human	6.8	pIC50	=	6.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1	nan
	89554919	150568	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	6	3.2	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3901084	150568	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	435	4	1	6	3.2	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1	nan
	71566204	155471	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1	nan
	CHEMBL3939934	155471	0	None	-	0	Human	7.8	pIC50	=	7.8	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1	nan
	22448830	96212	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	416	3	1	5	4.3	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL237091	96212	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	416	3	1	5	4.3	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	22448689	104331	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL270616	104331	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	457	4	1	6	4.6	N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	22317408	63067	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629850	63067	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11211597	63082	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629865	63082	0	None	-	0	Rat	7.8	pIC50	=	7.8	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	89554780	152161	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	3	4.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1	nan
	CHEMBL3913806	152161	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	3	4.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1	nan
	89554777	152075	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	2.9	CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	CHEMBL3913090	152075	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	5	2	4	2.9	CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	89554839	160171	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	5	1	6	3.3	NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3978791	160171	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	5	1	6	3.3	NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	89554772	151569	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1	nan
	CHEMBL3909260	151569	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1	nan
	89554745	156369	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3946940	156369	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	2	4	4.1	Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554794	159178	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3970463	159178	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554732	166949	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL4109248	166949	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	472	6	2	5	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	10297067	103079	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261263	103079	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	441	5	2	5	5.4	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	156016312	184512	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642428	184512	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	487	6	2	6	4.5	CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	156018942	184649	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	507	6	2	6	4.6	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4644424	184649	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	507	6	2	6	4.6	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554861	156603	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3948794	156603	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	287	2	1	3	3.2	Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1	nan
	71565804	150693	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	444	6	2	5	4.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1	nan
	CHEMBL3902047	150693	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	444	6	2	5	4.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1	nan
	89554886	166661	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL4106809	166661	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	11158623	10124	11	None	8	2	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	6226	10124	11	None	8	2	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	CHEMBL1629855	10124	11	None	8	2	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2010.09.125
	11351088	63072	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629856	63072	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.4	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	22317928	63073	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629857	63073	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	449	3	1	3	6.7	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1	10.1016/j.bmcl.2010.09.125
	11406781	63199	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631876	63199	0	None	-	0	Rat	8.7	pIC50	=	8.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	1378	9195	54	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	1399	9195	54	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	9819927	9195	54	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	CHEMBL432038	9195	54	None	-2	10	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/j.bmc.2008.02.066
	89554746	150533	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3900813	150533	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554931	154334	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	5	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1	nan
	CHEMBL3930820	154334	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	5	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1	nan
	1397	9307	15	None	-1	5	Rat	7.7	pIC50	=	7.7	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	9886034	9307	15	None	-1	5	Rat	7.7	pIC50	=	7.7	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186453	9307	15	None	-1	5	Rat	7.7	pIC50	=	7.7	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	22224970	162271	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404080	162271	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1	10.1016/j.bmcl.2007.12.005
	135544097	162444	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL404886	162444	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	437	2	2	6	4.0	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22317715	63071	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629854	63071	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9885546	117315	0	None	-	1	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL325140	117315	0	None	-	1	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	1378	9195	54	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	1399	9195	54	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	9819927	9195	54	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	CHEMBL432038	9195	54	None	-2	10	Human	6.7	pIC50	=	6.7	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1016/s0960-894x(01)00656-4
	44309302	210841	0	None	-	0	Rat	5.7	pIC50	=	5.7	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	345	5	0	4	4.8	Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1	10.1016/s0960-894x(99)00346-7
	CHEMBL70025	210841	0	None	-	0	Rat	5.7	pIC50	=	5.7	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	345	5	0	4	4.8	Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1	10.1016/s0960-894x(99)00346-7
	89554729	153173	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	514	8	2	7	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3921665	153173	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	514	8	2	7	4.4	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	121447916	176727	3	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	409	4	1	5	2.8	C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	CHEMBL4441595	176727	3	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	409	4	1	5	2.8	C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1	10.1021/acs.jmedchem.8b01266
	66791078	149452	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	489	6	2	6	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3891986	149452	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	489	6	2	6	4.5	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554746	150533	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3900813	150533	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	5	1	3	4.9	CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71566596	150924	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	4	1	4	2.5	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3903901	150924	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	4	1	4	2.5	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554855	153320	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F	nan
	CHEMBL3922719	153320	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F	nan
	89554970	153992	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1	nan
	CHEMBL3928272	153992	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	4	0	7	3.3	COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1	nan
	71566599	154084	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.8	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1	nan
	CHEMBL3929001	154084	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.8	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1	nan
	89554806	155996	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F	nan
	CHEMBL3944124	155996	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F	nan
	89554883	156980	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3951983	156980	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1	nan
	71566130	158660	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	384	5	1	6	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	CHEMBL3965748	158660	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	384	5	1	6	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	89554794	159178	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3970463	159178	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	5	1	3	5.2	Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	89554759	166825	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL4108213	166825	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	71566672	159608	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3973949	159608	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	22224962	103078	0	None	-	0	Rat	6.7	pIC50	=	6.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	342	3	1	4	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261251	103078	0	None	-	0	Rat	6.7	pIC50	=	6.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	342	3	1	4	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1	10.1016/j.bmcl.2008.02.076
	11559750	102730	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	CHEMBL259435	102730	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	89554860	152149	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1	nan
	CHEMBL3913733	152149	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1	nan
	71566519	160622	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	292	3	1	3	3.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	CHEMBL3982696	160622	0	None	-	0	Human	6.7	pIC50	=	6.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	292	3	1	3	3.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	89554797	149893	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	1	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1	nan
	CHEMBL3895570	149893	0	None	-	0	Human	7.7	pIC50	=	7.7	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	1	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1	nan
	22448579	162557	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL405895	162557	0	None	-	0	Rat	7.7	pIC50	=	7.7	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	412	3	2	5	4.8	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	11084869	96828	2	None	-	1	Human	7.7	pIC50	=	7.7	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL2381643	96828	2	None	-	1	Human	7.7	pIC50	=	7.7	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	11405687	73231	0	None	2	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185210	73231	0	None	2	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	117646988	156260	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	5	2.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1	nan
	CHEMBL3946311	156260	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	5	2.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1	nan
	10192719	72888	0	None	2	2	Rat	6.6	pIC50	=	6.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL183956	72888	0	None	2	2	Rat	6.6	pIC50	=	6.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	89554911	149772	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	149772	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	71565881	149803	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	380	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1	nan
	CHEMBL3894799	149803	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	380	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1	nan
	71566672	159608	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	nan
	CHEMBL3973949	159608	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	4	1	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1	nan
	89554767	160194	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3978978	160194	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1	nan
	9891158	162365	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL404463	162365	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	476	6	1	6	4.8	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2007.12.005
	22317491	63070	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629853	63070	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	1378	9195	54	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	1399	9195	54	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	9819927	9195	54	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	CHEMBL432038	9195	54	None	-1	10	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	89554965	151301	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1	nan
	CHEMBL3907125	151301	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	432	4	2	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1	nan
	89554894	156884	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1	nan
	CHEMBL3951081	156884	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1	nan
	89554916	160708	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1	nan
	CHEMBL3983396	160708	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1	nan
	156014599	183952	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	1	6	5.0	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4634754	183952	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	472	6	1	6	5.0	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554911	149772	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	149772	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	71565884	150203	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	4	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3898121	150203	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	4	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	71565736	159352	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	nan
	CHEMBL3971819	159352	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F	nan
	89554728	159653	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3974406	159653	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	89554776	159932	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	478	5	1	4	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1	nan
	CHEMBL3976706	159932	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	478	5	1	4	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1	nan
	11257636	175151	0	None	1	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL434536	175151	0	None	1	2	Rat	7.6	pIC50	=	7.6	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	22448659	161381	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	434	4	2	5	3.3	N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL399186	161381	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	434	4	2	5	3.3	N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89555004	150409	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	7	1	4	3.2	COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3899807	150409	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	7	1	4	3.2	COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554821	154128	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1	nan
	CHEMBL3929361	154128	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	367	4	1	5	2.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1	nan
	89554837	154617	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1	nan
	CHEMBL3933004	154617	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	375	4	1	5	3.1	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1	nan
	117641885	149794	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3894759	149794	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	6	2.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1	nan
	89554923	153224	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	5	3.3	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1	nan
	CHEMBL3922052	153224	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	5	3.3	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1	nan
	89554968	156366	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	4	1	5	3.4	CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3946909	156366	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	4	1	5	3.4	CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554820	156653	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3949126	156653	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	417	4	1	5	3.5	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1	nan
	89554792	157176	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	CHEMBL3953648	157176	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	89554765	158242	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3962095	158242	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	22224729	102904	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260415	102904	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	396	3	1	4	5.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1	10.1016/j.bmcl.2008.02.076
	156020940	184886	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	489	6	2	6	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4647980	184886	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	489	6	2	6	4.5	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554884	149986	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3896344	149986	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	89554835	156301	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	4	2.9	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1	nan
	CHEMBL3946509	156301	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	4	2.9	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1	nan
	44309103	109650	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	323	4	0	4	4.5	Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL305799	109650	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	323	4	0	4	4.5	Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	9845873	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL411440	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	44434259	95429	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	336	1	1	2	4.5	O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL235806	95429	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	336	1	1	2	4.5	O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	22448890	96094	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	490	4	2	5	4.7	CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236883	96094	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	490	4	2	5	4.7	CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	9845873	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL411440	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	9845873	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	22317318	63198	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631875	63198	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9845873	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL411440	167578	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	436	2	2	5	4.6	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2010.09.125
	89554791	166623	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	2	5	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4106552	166623	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	2	5	2.9	C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	22224765	95534	0	None	-	0	Rat	4.6	pIC50	=	4.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	343	1	2	4	3.1	CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236258	95534	0	None	-	0	Rat	4.6	pIC50	=	4.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	343	1	2	4	3.1	CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	71565962	156419	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	462	5	1	6	4.1	NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3947299	156419	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	462	5	1	6	4.1	NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1	nan
	22224583	161382	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	1	1	2	5.6	O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL399187	161382	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	1	1	2	5.6	O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	44309086	210713	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	346	5	0	5	4.2	Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL69204	210713	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	346	5	0	5	4.2	Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	71566597	156651	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	1	4	3.4	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3949122	156651	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	1	4	3.4	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554867	156863	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	1	5	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C	nan
	CHEMBL3950864	156863	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	412	6	1	5	4.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C	nan
	71565671	157288	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	5	1	5	2.7	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	CHEMBL3954513	157288	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	5	1	5	2.7	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	89554775	160614	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	476	5	2	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1	nan
	CHEMBL3982636	160614	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	476	5	2	6	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1	nan
	18548766	102638	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259053	102638	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	405	2	1	5	4.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	156019727	184771	0	None	-	0	Human	5.6	pIC50	=	5.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	497	7	2	6	4.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4646222	184771	0	None	-	0	Human	5.6	pIC50	=	5.6	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	497	7	2	6	4.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554914	167393	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C	nan
	CHEMBL4112966	167393	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C	nan
	89554778	150131	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	408	5	3	5	1.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1	nan
	CHEMBL3897537	150131	0	None	-	0	Human	6.6	pIC50	=	6.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	408	5	3	5	1.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1	nan
	53320742	63194	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	452	4	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631871	63194	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	452	4	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	9868835	155731	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	459	2	1	5	4.2	CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	CHEMBL394201	155731	0	None	-	0	Rat	6.6	pIC50	=	6.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	459	2	1	5	4.2	CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	89554888	149387	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1	nan
	CHEMBL3891468	149387	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1	nan
	89554859	156806	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	4	1	5	3.9	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1	nan
	CHEMBL3950438	156806	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	4	1	5	3.9	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1	nan
	71565521	157263	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1	nan
	CHEMBL3954371	157263	0	None	-	0	Human	7.6	pIC50	=	7.6	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	4	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1	nan
	22448614	96092	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	5	1	5	4.4	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236881	96092	0	None	-	0	Rat	7.6	pIC50	=	7.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	5	1	5	4.4	COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	44434256	95380	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	284	1	1	2	4.1	Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL235599	95380	0	None	-	0	Rat	5.6	pIC50	=	5.6	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	284	1	1	2	4.1	Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2	10.1016/j.bmcl.2007.10.026
	71565526	158225	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3961948	158225	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	18548910	102709	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259340	102709	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	3	1	6	3.8	COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	22317258	63197	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	480	3	1	5	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631874	63197	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	480	3	1	5	5.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11279365	74334	0	None	1	2	Rat	7.5	pIC50	=	7.5	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189814	74334	0	None	1	2	Rat	7.5	pIC50	=	7.5	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	44434258	95381	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	275	1	1	3	3.3	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL235600	95381	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	275	1	1	3	3.3	Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	11158623	10124	11	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2012.04.112
	6226	10124	11	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2012.04.112
	CHEMBL1629855	10124	11	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1016/j.bmcl.2012.04.112
	11158623	10124	11	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1021/jm400439t
	6226	10124	11	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1021/jm400439t
	CHEMBL1629855	10124	11	None	-8	2	Human	6.5	pIC50	=	6.5	Binding	Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)	ChEMBL	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	10.1021/jm400439t
	89543886	155553	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	3	1	3	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1	nan
	CHEMBL3940628	155553	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	363	3	1	3	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1	nan
	44452714	166047	0	None	-	0	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	CHEMBL409928	166047	0	None	-	0	Human	8.5	pIC50	=	8.5	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	71566669	152262	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	5	1	4	3.8	CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3914560	152262	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	5	1	4	3.8	CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	89554938	153453	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1	nan
	CHEMBL3923798	153453	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	5	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1	nan
	89554823	155811	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1	nan
	CHEMBL3942629	155811	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1	nan
	22224615	96839	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL238167	96839	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	22224975	95532	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	368	1	1	5	3.9	N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236256	95532	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	368	1	1	5	3.9	N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	10359073	161753	1	None	-2	2	Human	5.5	pIC50	=	5.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	CHEMBL40123	161753	1	None	-2	2	Human	5.5	pIC50	=	5.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	327	8	3	3	2.7	N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	89554903	159429	0	None	-	0	Human	5.5	pIC50	=	5.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	345	3	0	3	4.0	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	nan
	CHEMBL3972456	159429	0	None	-	0	Human	5.5	pIC50	=	5.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	345	3	0	3	4.0	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	nan
	71566274	153670	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	3	4.4	Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3925507	153670	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	4	1	3	4.4	Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71565738	157043	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	6	1	5	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1	nan
	CHEMBL3952509	157043	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	6	1	5	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1	nan
	71565805	159097	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	CHEMBL3969686	159097	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	1	6	3.2	COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	71566206	160426	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	CHEMBL3981039	160426	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	1	4	4.1	COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	89554764	160734	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	4	4.5	CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3983614	160734	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	388	5	1	4	4.5	CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	22224825	165773	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL409638	165773	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	397	3	1	5	4.5	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2008.02.076
	44309101	210343	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	278	6	0	5	3.1	CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1	10.1016/s0960-894x(99)00346-7
	CHEMBL66701	210343	0	None	-	0	Rat	5.5	pIC50	=	5.5	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	278	6	0	5	3.1	CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1	10.1016/s0960-894x(99)00346-7
	22224682	96384	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	367	1	1	4	4.5	N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL237523	96384	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	367	1	1	4	4.5	N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554733	149318	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	5	1	7	3.2	COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3890866	149318	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	452	5	1	7	3.2	COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	71566126	155561	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	CHEMBL3940665	155561	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	2	5	4.5	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1	nan
	89554774	160655	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	1	4	3.3	CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	CHEMBL3982968	160655	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	1	4	3.3	CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1	nan
	89543925	159204	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	284	2	1	2	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1	nan
	CHEMBL3970688	159204	0	None	-	0	Human	6.5	pIC50	=	6.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	284	2	1	2	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1	nan
	89554911	149772	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	CHEMBL3894556	149772	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1	nan
	89554971	154062	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	6	2.8	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1	nan
	CHEMBL3928860	154062	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	1	6	2.8	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1	nan
	9820321	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	9820321	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2008.02.076
	CHEMBL401446	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL401446	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2008.02.076
	22224841	96838	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL238166	96838	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	1	1	3	4.6	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	9820321	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL401446	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	9820321	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL401446	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	9820321	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL401446	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	44285839	106928	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	353	4	3	4	2.9	CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21	10.1021/jm980571q
	CHEMBL287831	106928	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	353	4	3	4	2.9	CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21	10.1021/jm980571q
	9820321	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL401446	161787	0	None	-	0	Rat	7.5	pIC50	=	7.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	361	1	1	3	4.4	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	117642059	150487	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	4	1	4	4.5	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3900371	150487	0	None	-	0	Human	7.5	pIC50	=	7.5	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	4	1	4	4.5	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1	nan
	53318106	63178	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	4	5.1	Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631855	63178	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	4	5.1	Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1	10.1016/j.bmcl.2010.09.125
	22224908	95526	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	2	2	3	3.6	NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236244	95526	0	None	-	0	Rat	6.5	pIC50	=	6.5	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	379	2	2	3	3.6	NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	117642047	149312	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	6	2	6	3.9	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3890814	149312	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	6	2	6	3.9	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554868	156121	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	402	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	CHEMBL3945166	156121	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	402	5	1	6	3.1	Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1	nan
	10204007	104293	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	446	3	1	6	4.2	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL270402	104293	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	446	3	1	6	4.2	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2007.12.005
	89554759	166825	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4108213	166825	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	156015207	184352	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4640529	184352	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	473	6	2	6	3.9	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	22224803	96690	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	449	2	1	4	4.0	O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL237938	96690	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	449	2	1	4	4.0	O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	156013741	184045	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	282	1	1	4	2.3	O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12	10.1016/j.bmcl.2020.127066
	CHEMBL4636186	184045	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	282	1	1	4	2.3	O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12	10.1016/j.bmcl.2020.127066
	71566438	159640	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12	nan
	CHEMBL3974279	159640	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12	nan
	89554845	153187	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1	nan
	CHEMBL3921799	153187	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	296	2	1	2	4.0	Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1	nan
	22448617	95825	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	446	2	1	5	4.3	N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236467	95825	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	446	2	1	5	4.3	N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	136152920	101988	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	467	3	3	7	3.5	O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256008	101988	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	467	3	3	7	3.5	O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	71566600	152975	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1	nan
	CHEMBL3920092	152975	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1	nan
	89554814	159662	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	4	1	5	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1	nan
	CHEMBL3974523	159662	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	4	1	5	4.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1	nan
	18613455	102825	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL259924	102825	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	6	3.8	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	89554808	152002	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1	nan
	CHEMBL3912631	152002	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1	nan
	89554869	151444	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	4	1	5	3.5	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	CHEMBL3908309	151444	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	389	4	1	5	3.5	Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1	nan
	89554849	157734	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1	nan
	CHEMBL3958094	157734	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	1	6	2.9	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1	nan
	22224570	102690	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL259269	102690	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	378	3	1	4	5.0	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1	10.1016/j.bmcl.2008.02.076
	53316798	63179	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631856	63179	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	384	2	1	4	4.6	Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2010.09.125
	89554811	154640	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1	nan
	CHEMBL3933190	154640	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	2	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1	nan
	71566521	150105	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1	nan
	CHEMBL3897268	150105	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	280	2	1	2	3.4	Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1	nan
	89554885	151081	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL3905282	151081	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	1	6	2.0	C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	89554951	161052	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	361	3	0	5	3.4	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1	nan
	CHEMBL3986465	161052	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	361	3	0	5	3.4	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1	nan
	89554872	156177	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	CHEMBL3945590	156177	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F	nan
	44450479	103038	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL261050	103038	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	398	3	1	4	4.9	CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	11235624	63079	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629862	63079	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	4	1	4	5.6	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11304010	63081	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629864	63081	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	11474913	63181	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631858	63181	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	395	2	1	3	5.5	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11281280	63182	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631859	63182	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	409	2	1	3	5.8	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	22317431	63187	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631864	63187	0	None	-	0	Rat	8.4	pIC50	=	8.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	437	3	1	3	6.7	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11559750	102730	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	CHEMBL259435	102730	0	None	-	0	Human	8.4	pIC50	=	8.4	Binding	Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells	ChEMBL	371	5	3	4	2.9	NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O	10.1016/j.bmc.2008.02.066
	71565740	151347	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	418	6	1	6	3.6	CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	CHEMBL3907527	151347	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	418	6	1	6	3.6	CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1	nan
	22448643	95826	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	5	5.0	N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236468	95826	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	462	2	1	5	5.0	N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	53324715	63193	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631870	63193	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	3	2	4	5.8	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11382367	73711	0	None	1	2	Rat	7.4	pIC50	=	7.4	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186630	73711	0	None	1	2	Rat	7.4	pIC50	=	7.4	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	22224567	174190	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	325	1	1	3	3.9	C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL429629	174190	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	325	1	1	3	3.9	C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	6324634	154722	11	None	-1	2	Human	6.4	pIC50	=	6.4	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	CHEMBL39338	154722	11	None	-1	2	Human	6.4	pIC50	=	6.4	Binding	Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2	ChEMBL	355	10	3	3	3.5	N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O	10.1021/jm980571q
	156009702	183950	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	277	1	1	1	3.9	O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21	10.1016/j.bmcl.2020.127066
	CHEMBL4634600	183950	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	277	1	1	1	3.9	O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21	10.1016/j.bmcl.2020.127066
	71566442	152025	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	276	2	1	2	3.6	Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	CHEMBL3912824	152025	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	276	2	1	2	3.6	Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1	nan
	156017399	184493	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	5	1	6	4.7	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4642255	184493	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	5	1	6	4.7	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	117642070	157828	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	5	1	7	2.1	COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3958736	157828	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	5	1	7	2.1	COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	71566668	151003	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	359	3	0	4	3.6	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3904529	151003	0	None	-	0	Human	6.4	pIC50	=	6.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	359	3	0	4	3.6	N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	89554730	149792	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1	nan
	CHEMBL3894724	149792	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	4	3.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1	nan
	89554897	152193	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1	nan
	CHEMBL3914040	152193	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1	nan
	89554771	156439	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1	nan
	CHEMBL3947441	156439	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	473	5	1	5	5.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1	nan
	89554802	159431	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3972468	159431	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1	nan
	18613373	102949	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL260643	102949	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	442	5	2	6	4.8	CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	71565807	149609	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	424	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1	nan
	CHEMBL3893078	149609	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	424	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1	nan
	44450484	103455	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	370	2	1	4	4.4	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL263906	103455	0	None	-	0	Rat	7.4	pIC50	=	7.4	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	370	2	1	4	4.4	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	89554879	160499	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1	nan
	CHEMBL3981623	160499	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1	nan
	22448569	95956	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	478	2	1	5	4.0	N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236668	95956	0	None	-	0	Rat	6.4	pIC50	=	6.4	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	478	2	1	5	4.0	N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	71565669	149740	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL3894283	149740	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	CHEMBL4515671	149740	0	None	-	0	Human	7.4	pIC50	=	7.4	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	10.1021/acs.jmedchem.8b01266
	71565522	149728	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	495	4	1	6	5.8	CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C	nan
	CHEMBL3894156	149728	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	495	4	1	6	5.8	CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C	nan
	89554819	155094	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	1	4	4.8	Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3936939	155094	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	410	4	1	4	4.8	Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554826	157264	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1	nan
	CHEMBL3954377	157264	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	5	3.0	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1	nan
	71566278	159021	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	4	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1	nan
	CHEMBL3968939	159021	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	4	1	4	4.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1	nan
	89554896	166741	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL4107449	166741	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	22448868	162076	0	None	-	0	Rat	7.3	pIC50	=	7.3	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	480	5	2	6	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL402963	162076	0	None	-	0	Rat	7.3	pIC50	=	7.3	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	480	5	2	6	4.2	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	44450455	174347	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	345	3	1	5	3.9	CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL430053	174347	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	345	3	1	5	3.9	CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	89554847	151699	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	357	4	1	3	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1	nan
	CHEMBL3910265	151699	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	357	4	1	3	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1	nan
	89554756	156495	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.7	CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	CHEMBL3947898	156495	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	3.7	CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	71565803	160085	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	6	1	6	4.6	CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F	nan
	CHEMBL3978058	160085	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	6	1	6	4.6	CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F	nan
	44309314	210756	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	CHEMBL69461	210756	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	351	4	0	4	5.3	Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1	10.1016/s0960-894x(99)00346-7
	89554962	159877	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	3	0	4	4.6	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1	nan
	CHEMBL3976206	159877	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	401	3	0	4	4.6	CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1	nan
	10130658	73527	0	None	2	2	Rat	6.3	pIC50	=	6.3	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185822	73527	0	None	2	2	Rat	6.3	pIC50	=	6.3	Binding	Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	89554743	157730	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	4	1	4	3.6	N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3958048	157730	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	4	1	4	3.6	N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554738	157738	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3958113	157738	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	89554921	160576	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	5	1	6	2.7	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	CHEMBL3982294	160576	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	5	1	6	2.7	COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1	nan
	22224756	154730	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	397	1	1	3	4.7	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL393385	154730	0	None	-	0	Rat	6.3	pIC50	=	6.3	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	397	1	1	3	4.7	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554738	157738	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3958113	157738	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	89554866	153373	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3923126	153373	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	434	6	1	5	4.2	COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	89554768	156230	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	CHEMBL3946016	156230	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	6	1	4	4.8	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1	nan
	89554800	158523	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1	nan
	CHEMBL3964644	158523	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1	nan
	71552551	159294	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	4	1	4	3.0	Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	CHEMBL3971388	159294	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	373	4	1	4	3.0	Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1	nan
	22317744	63061	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629844	63061	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	425	3	1	4	5.5	COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	18548795	63175	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631757	63175	0	None	-	0	Rat	8.3	pIC50	=	8.3	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	399	2	1	4	5.4	Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1	10.1016/j.bmcl.2010.09.125
	69093928	90684	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206447	90684	0	None	-	0	Human	8.3	pIC50	=	8.3	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	89554792	157176	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	CHEMBL3953648	157176	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	414	5	2	4	3.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1	nan
	10428048	10134	31	None	-	1	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	3955	10134	31	None	-	1	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	CHEMBL305406	10134	31	None	-	1	Rat	6.3	pIC50	=	6.3	Binding	Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells	ChEMBL	351	4	0	4	5.3	Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl	10.1016/s0960-894x(99)00346-7
	71566525	155461	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	3	1	4	3.2	NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1	nan
	CHEMBL3939839	155461	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	3	1	4	3.2	NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1	nan
	89554842	166666	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	CHEMBL4106872	166666	0	None	-	0	Human	6.3	pIC50	=	6.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	405	4	2	5	2.5	NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	89554876	154937	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	5	4.5	COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1	nan
	CHEMBL3935571	154937	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	426	6	1	5	4.5	COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1	nan
	89554795	160222	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	2.9	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3979288	160222	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	5	1	6	2.9	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1	nan
	89554817	150889	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1	nan
	CHEMBL3903609	150889	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	5	1	6	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1	nan
	89554934	166947	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	5	1	6	4.5	C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	CHEMBL4109232	166947	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	486	5	1	6	4.5	C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1	nan
	71565808	158042	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	360	4	1	4	3.7	Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3960284	158042	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	360	4	1	4	3.7	Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554773	150468	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1	nan
	CHEMBL3900236	150468	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1	nan
	89554798	151982	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	6	2.3	CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	CHEMBL3912490	151982	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	5	1	6	2.3	CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1	nan
	117644752	153229	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	4	3.7	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1	nan
	CHEMBL3922089	153229	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	393	4	1	4	3.7	CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1	nan
	89544007	153824	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	358	4	1	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1	nan
	CHEMBL3926904	153824	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	358	4	1	4	3.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1	nan
	71566128	154348	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	1	4	4.8	COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl	nan
	CHEMBL3930919	154348	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	421	5	1	4	4.8	COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl	nan
	89554803	159028	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1	nan
	CHEMBL3968972	159028	0	None	-	0	Human	7.3	pIC50	=	7.3	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	413	4	1	5	2.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1	nan
	89554805	155493	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3940116	155493	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	4	3.4	C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71566439	150854	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1	nan
	CHEMBL3903327	150854	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	300	2	1	2	3.8	NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1	nan
	71565735	157164	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3953417	157164	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	44309315	109037	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1	10.1016/s0960-894x(99)00346-7
	CHEMBL303193	109037	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	337	4	0	4	4.9	Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1	10.1016/s0960-894x(99)00346-7
	71565523	160105	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	3	0	4	3.3	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O	nan
	CHEMBL3978239	160105	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	374	3	0	4	3.3	CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O	nan
	71566671	157148	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	4	2	4	3.0	CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3953282	157148	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	406	4	2	4	3.0	CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	71565735	157164	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	nan
	CHEMBL3953417	157164	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	3	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1	nan
	89554738	157738	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	CHEMBL3958113	157738	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	431	4	1	3	4.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1	nan
	53324292	63196	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	460	3	1	4	6.3	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631873	63196	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	460	3	1	4	6.3	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	89554993	155707	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	427	6	1	6	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1	nan
	CHEMBL3941863	155707	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	427	6	1	6	3.6	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1	nan
	89554892	157380	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3955188	157380	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	1	5	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1	nan
	89554749	158784	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	CHEMBL3966866	158784	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	6	2	5	4.3	COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1	nan
	71565966	159579	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3973721	159579	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	89554893	160760	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3983863	160760	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	411	4	1	5	3.7	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1	nan
	22224854	102159	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256812	102159	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22317728	63063	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629846	63063	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	435	3	1	3	6.4	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	53320632	63069	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629852	63069	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	396	2	1	4	4.9	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11442010	63083	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629866	63083	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	439	4	1	4	5.9	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	44450453	162677	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	337	2	1	5	3.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL406061	162677	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	337	2	1	5	3.4	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2008.02.076
	18613404	95824	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	2	1	4	4.5	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236466	95824	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	404	2	1	4	4.5	CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	22448865	96093	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	4	2	5	3.9	N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236882	96093	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	435	4	2	5	3.9	N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	44450444	102908	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	353	3	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL260455	102908	0	None	-	0	Rat	6.2	pIC50	=	6.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	353	3	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	89554779	152871	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	nan
	CHEMBL3919306	152871	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	nan
	89554779	152871	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3919306	152871	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	385	4	1	3	4.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1	10.1016/j.bmcl.2020.127066
	71565737	150750	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1	nan
	CHEMBL3902679	150750	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1	nan
	89554831	154282	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	1	4	3.8	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	CHEMBL3930529	154282	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	1	4	3.8	CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	71566670	153686	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	4	3.3	CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	CHEMBL3925652	153686	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	420	4	1	4	3.3	CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C	nan
	89554761	157346	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	346	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1	nan
	CHEMBL3954993	157346	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	346	4	1	4	3.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1	nan
	22224809	160766	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	375	1	1	3	4.7	Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	CHEMBL398392	160766	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	375	1	1	3	4.7	Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	9847181	101826	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	462	5	2	6	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL255151	101826	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	462	5	2	6	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.12.005
	10089411	14299	0	None	-	1	Human	5.2	pIC50	=	5.2	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL108735	14299	0	None	-	1	Human	5.2	pIC50	=	5.2	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	353213	155837	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2007.12.005
	353213	155837	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL394287	155837	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2007.12.005
	CHEMBL394287	155837	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2008.02.076
	353213	155837	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL394287	155837	16	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells	ChEMBL	250	1	1	2	3.5	Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2	10.1016/j.bmcl.2010.09.125
	71566437	154254	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	268	2	1	3	3.4	Cc1cscc1-c1cc(C(N)=O)nc2ccccc12	nan
	CHEMBL3930346	154254	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	268	2	1	3	3.4	Cc1cscc1-c1cc(C(N)=O)nc2ccccc12	nan
	44434255	95379	0	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	280	2	1	3	3.5	COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL235598	95379	0	None	-	0	Rat	5.2	pIC50	=	5.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	280	2	1	3	3.5	COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554731	158890	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	438	5	1	4	5.7	CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3967755	158890	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	438	5	1	4	5.7	CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554972	160964	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	460	5	1	4	4.2	CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	CHEMBL3985765	160964	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	460	5	1	4	4.2	CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F	nan
	22317369	63185	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	2	1	3	6.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631862	63185	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	463	2	1	3	6.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71566346	156266	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	4	1	3	3.6	NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1	nan
	CHEMBL3946344	156266	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	314	4	1	3	3.6	NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1	nan
	71566348	157718	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	328	3	1	4	3.5	Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1	nan
	CHEMBL3957842	157718	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	328	3	1	4	3.5	Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1	nan
	89554750	149306	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	498	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	CHEMBL3890746	149306	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	498	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F	nan
	71566347	155476	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	252	2	1	4	1.7	Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1	nan
	CHEMBL3939979	155476	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	252	2	1	4	1.7	Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1	nan
	25195461	8925	48	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	8946	8925	48	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	CHEMBL3337527	8925	48	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	DB12059	8925	48	None	-	1	Human	7.2	pIC50	=	7.2	Binding	Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/jm500496m
	22224822	96691	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	CHEMBL237944	96691	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1	10.1016/j.bmcl.2007.10.026
	89545189	159674	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3974648	159674	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	365	4	1	4	3.0	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1	10.1016/j.bmcl.2020.127066
	156011740	184203	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	6	2	6	3.8	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	CHEMBL4638570	184203	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	455	6	2	6	3.8	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	10.1016/j.bmcl.2020.127066
	89554955	151959	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1	nan
	CHEMBL3912345	151959	0	None	-	0	Human	6.2	pIC50	=	6.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	326	2	1	2	3.8	NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1	nan
	89554762	159292	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1	nan
	CHEMBL3971379	159292	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	397	4	1	5	3.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1	nan
	1393	8321	64	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	1396	8321	64	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	213056	8321	64	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL8759	8321	64	None	-2	6	Human	8.2	pIC50	=	8.2	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	89554982	153630	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	6	2	6	3.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1	nan
	CHEMBL3925177	153630	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	399	6	2	6	3.2	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1	nan
	89554981	155237	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	409	6	1	6	3.5	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1	nan
	CHEMBL3937970	155237	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	409	6	1	6	3.5	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1	nan
	89554880	156823	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	372	5	1	4	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	CHEMBL3950572	156823	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	372	5	1	4	3.7	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1	nan
	71565593	157740	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	3.2	CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	CHEMBL3958138	157740	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	3.2	CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1	nan
	89554910	158173	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	4	1	5	4.4	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1	nan
	CHEMBL3961599	158173	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	445	4	1	5	4.4	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1	nan
	71565966	159579	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	CHEMBL3973721	159579	0	None	-	0	Human	8.2	pIC50	=	8.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	430	6	1	5	4.6	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1	nan
	18548862	164718	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408455	164718	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	415	4	1	6	4.1	CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	44450391	175614	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL437835	175614	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	414	3	1	4	5.3	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1	10.1016/j.bmcl.2008.02.076
	22317892	63077	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629860	63077	0	None	-	0	Rat	8.2	pIC50	=	8.2	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	477	2	1	3	6.9	Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	69093344	90683	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206446	90683	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	44450434	174476	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	4	1	6	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL430231	174476	0	None	-	0	Rat	7.2	pIC50	=	7.2	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	401	4	1	6	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	44431050	149122	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Antagonist activity at human mGlur2Antagonist activity at human mGlur2	ChEMBL	363	2	3	2	3.6	O=C1NCCc2c1[nH]c1ccc(NC(=O)C34CC5CC(CC(C5)C3)C4)cc21	10.1021/acs.jmedchem.0c01887
	CHEMBL388669	149122	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Antagonist activity at human mGlur2Antagonist activity at human mGlur2	ChEMBL	363	2	3	2	3.6	O=C1NCCc2c1[nH]c1ccc(NC(=O)C34CC5CC(CC(C5)C3)C4)cc21	10.1021/acs.jmedchem.0c01887
	71566601	157003	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	467	5	1	4	4.4	CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	CHEMBL3952222	157003	0	None	-	0	Human	7.2	pIC50	=	7.2	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	467	5	1	4	4.4	CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O	nan
	44450483	175585	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	380	2	1	4	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL437646	175585	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	380	2	1	4	4.1	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1	10.1016/j.bmcl.2008.02.076
	9845127	174557	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	422	2	1	6	3.7	O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL430408	174557	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	422	2	1	6	3.7	O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	71565886	150826	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL3903111	150826	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	6	1	6	3.0	CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	89554822	151420	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	5	1	4	5.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1	nan
	CHEMBL3908110	151420	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	5	1	4	5.4	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1	nan
	44453878	102452	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	416	2	1	4	5.0	Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	CHEMBL258113	102452	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	416	2	1	4	5.0	Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.12.005
	89554929	157116	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3953060	157116	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	395	4	1	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1	nan
	89554907	167381	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL4112899	167381	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	474	6	2	7	3.3	CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	44309080	210820	0	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	265	4	0	4	2.9	CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F	10.1016/s0960-894x(99)00346-7
	CHEMBL69869	210820	0	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells	ChEMBL	265	4	0	4	2.9	CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F	10.1016/s0960-894x(99)00346-7
	89554959	150117	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	362	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1	nan
	CHEMBL3897362	150117	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	362	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1	nan
	71566205	159075	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	386	5	1	3	4.7	COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1	nan
	CHEMBL3969476	159075	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	386	5	1	3	4.7	COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1	nan
	89554739	166685	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL4107013	166685	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	4	1	6	3.9	Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1	nan
	22224639	168549	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	395	1	1	3	5.1	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL413979	168549	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	395	1	1	3	5.1	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	1439	9247	15	None	-	2	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm980571q
	5311457	9247	15	None	-	2	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm980571q
	CHEMBL41013	9247	15	None	-	2	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	173	3	3	3	-0.5	OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C	10.1021/jm980571q
	89554782	156813	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	2	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1	nan
	CHEMBL3950507	156813	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	392	5	2	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1	nan
	122539788	169324	15	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	326	5	1	5	2.3	Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1	10.1021/acs.jmedchem.8b01266
	CHEMBL4168094	169324	15	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)	ChEMBL	326	5	1	5	2.3	Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1	10.1021/acs.jmedchem.8b01266
	71565669	149740	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	nan
	CHEMBL3894283	149740	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	nan
	CHEMBL4515671	149740	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	407	5	1	5	2.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1	nan
	71565964	151028	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	CHEMBL3904730	151028	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	429	7	1	4	5.2	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1	nan
	89554964	152001	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL3912615	152001	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	89554887	155110	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1	nan
	CHEMBL3937038	155110	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	387	5	2	4	3.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1	nan
	71566127	155416	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	CHEMBL3939455	155416	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	415	6	1	4	4.9	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1	nan
	89554858	157878	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	CHEMBL3959134	157878	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	520	7	2	6	4.7	CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F	nan
	89554984	159300	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	423	6	1	6	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1	nan
	CHEMBL3971450	159300	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	423	6	1	6	4.0	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1	nan
	89554790	166646	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1	nan
	CHEMBL4106729	166646	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1	nan
	89554915	166880	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	CHEMBL4108673	166880	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	4	1	6	3.2	Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	89554961	167063	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	CHEMBL4110317	167063	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	433	4	1	6	2.9	C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1	nan
	53317987	63075	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629859	63075	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	453	4	1	4	6.0	COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1	10.1016/j.bmcl.2010.09.125
	11484819	63080	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629863	63080	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	347	2	1	3	4.9	O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1	10.1016/j.bmcl.2010.09.125
	18548737	63177	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1631854	63177	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	11362246	63183	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1631860	63183	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1	10.1016/j.bmcl.2010.09.125
	70052526	96827	2	None	-	1	Human	8.1	pIC50	=	8.1	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL2381642	96827	2	None	-	1	Human	8.1	pIC50	=	8.1	Binding	Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	71566598	149468	15	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	149468	15	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	89554908	149244	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	5	2	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1	nan
	CHEMBL3890277	149244	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	396	5	2	4	2.9	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1	nan
	9864190	95430	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	370	1	1	2	5.2	O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	CHEMBL235807	95430	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	370	1	1	2	5.2	O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1	10.1016/j.bmcl.2007.10.026
	89554895	157013	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	4	5.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1	nan
	CHEMBL3952287	157013	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	4	5.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1	nan
	89554978	157484	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	5	1	6	3.5	CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	CHEMBL3956019	157484	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	5	1	6	3.5	CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1	nan
	89555003	152003	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	339	5	1	4	3.1	CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3912634	152003	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	339	5	1	4	3.1	CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554744	155117	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1	nan
	CHEMBL3937068	155117	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	378	4	2	4	2.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1	nan
	22448756	161380	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	474	3	1	5	5.0	COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	CHEMBL399185	161380	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	474	3	1	5	5.0	COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1	10.1016/j.bmcl.2007.10.026
	89554949	154960	0	None	-	0	Human	6.1	pIC50	=	6.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	238	2	1	2	2.9	NC(=O)c1cc(C2=CCCC2)c2ccccc2n1	nan
	CHEMBL3935751	154960	0	None	-	0	Human	6.1	pIC50	=	6.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	238	2	1	2	2.9	NC(=O)c1cc(C2=CCCC2)c2ccccc2n1	nan
	89554741	153985	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	366	6	2	4	2.1	CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3928211	153985	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	366	6	2	4	2.1	CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	89554957	157156	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	2	6	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1	nan
	CHEMBL3953345	157156	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	391	5	2	6	2.5	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1	nan
	117642124	154119	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	6	2	6	4.1	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	CHEMBL3929304	154119	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	469	6	2	6	4.1	CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F	nan
	89554862	150762	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1	nan
	CHEMBL3902752	150762	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	371	5	1	3	4.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1	nan
	89554838	167714	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	461	4	1	6	3.5	Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	CHEMBL4115433	167714	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	461	4	1	6	3.5	Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12	nan
	22318000	63066	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	438	3	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL1629849	63066	0	None	-	0	Rat	7.1	pIC50	=	7.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	438	3	1	4	5.6	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2	10.1016/j.bmcl.2010.09.125
	22224608	95533	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	362	1	1	4	3.8	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL236257	95533	0	None	-	0	Rat	6.1	pIC50	=	6.1	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	362	1	1	4	3.8	N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554735	153406	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1	nan
	CHEMBL3923360	153406	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	4	1	6	2.3	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1	nan
	1408	7053	31	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	6604820	7053	31	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	CHEMBL285043	7053	31	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	CHEMBL288635	7053	31	None	-	0	Rat	4.1	pIC50	=	4.1	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	217	3	4	4	-1.0	OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O	10.1021/jm980571q
	89554810	158094	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	4	6.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1	nan
	CHEMBL3960845	158094	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	464	5	1	4	6.2	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1	nan
	71566598	149468	15	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	CHEMBL3892073	149468	15	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	nan
	89554770	150869	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	CHEMBL3903459	150869	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	446	4	2	4	3.9	C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1	nan
	71565965	155063	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	CHEMBL3936681	155063	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	447	7	1	4	5.4	COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1	nan
	89554985	157218	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1	nan
	CHEMBL3954035	157218	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	416	6	2	5	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1	nan
	89554980	160756	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	2	5	3.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1	nan
	CHEMBL3983820	160756	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	398	6	2	5	3.8	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1	nan
	89554809	160977	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	4	1	6	3.5	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3985872	160977	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	436	4	1	6	3.5	Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	89554789	166981	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	CHEMBL4109555	166981	0	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	437	5	1	6	2.9	NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1	nan
	10201802	103422	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL263649	103422	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	413	3	1	5	4.4	CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2	10.1016/j.bmcl.2008.02.076
	18548824	164515	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	CHEMBL408229	164515	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2008.02.076
	9888376	101990	1	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL256011	101990	1	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	420	2	1	4	4.9	O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	71566598	149468	15	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL3892073	149468	15	None	-	0	Human	8.1	pIC50	=	8.1	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	377	4	1	4	2.8	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	53316736	63058	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	CHEMBL1629715	63058	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	423	3	1	3	6.1	CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2010.09.125
	18548824	164515	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	CHEMBL408229	164515	0	None	-	0	Rat	8.1	pIC50	=	8.1	Binding	Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2	ChEMBL	385	2	1	5	4.1	Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2	10.1016/j.bmcl.2010.09.125
	71461395	90682	1	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	CHEMBL2206445	90682	1	None	-	0	Human	8.0	pIC50	=	8.0	Binding	Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting	ChEMBL	432	5	0	5	5.0	COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1	10.1021/jm300912k
	89554912	152752	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	2	4	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1	nan
	CHEMBL3918313	152752	0	None	-	0	Human	7.1	pIC50	=	7.1	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	404	5	2	4	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1	nan
	89554815	151924	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	6	3.8	CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	CHEMBL3912111	151924	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	450	5	1	6	3.8	CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1	nan
	71565670	183999	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	363	4	1	3	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	CHEMBL4635528	183999	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay	ChEMBL	363	4	1	3	3.3	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1	10.1016/j.bmcl.2020.127066
	44450445	103051	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	371	2	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	CHEMBL261128	103051	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2	ChEMBL	371	2	1	5	3.7	O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1	10.1016/j.bmcl.2008.02.076
	9886745	95958	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	CHEMBL236670	95958	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	391	2	1	4	4.4	COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2	10.1016/j.bmcl.2007.10.026
	117641966	153322	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1	nan
	CHEMBL3922743	153322	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	419	4	1	4	4.1	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1	nan
	89554924	149486	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1	nan
	CHEMBL3892213	149486	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	365	4	2	6	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1	nan
	117642073	155754	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	7	1	6	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC	nan
	CHEMBL3942209	155754	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	428	7	1	6	3.9	COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC	nan
	22224730	161523	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	366	2	1	3	4.6	COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	CHEMBL400018	161523	0	None	-	0	Rat	6.0	pIC50	=	6.0	Binding	Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells	ChEMBL	366	2	1	3	4.6	COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1	10.1016/j.bmcl.2007.10.026
	89554920	152341	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	439	5	1	7	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1	nan
	CHEMBL3915181	152341	0	None	-	0	Human	7.0	pIC50	=	7.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	439	5	1	7	1.7	Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1	nan
	9931956	101862	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	CHEMBL255356	101862	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	421	2	1	5	4.3	O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1	10.1016/j.bmcl.2007.12.005
	22224761	173394	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	434	2	1	4	5.2	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2007.12.005
	CHEMBL428066	173394	0	None	-	0	Rat	7.0	pIC50	=	7.0	Binding	Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells	ChEMBL	434	2	1	4	5.2	Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1	10.1016/j.bmcl.2007.12.005
	71566203	155414	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	3	1	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1	nan
	CHEMBL3939409	155414	0	None	-	0	Human	6.0	pIC50	=	6.0	Binding	Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.	ChEMBL	379	3	1	4	2.6	NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1	nan
	3335	9789	4	None	-	1	Rat	5.0	pIC50	=	5	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm980571q
	5311344	9789	4	None	-	1	Rat	5.0	pIC50	=	5	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm980571q
	CHEMBL39573	9789	4	None	-	1	Rat	5.0	pIC50	=	5	Binding	Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.	ChEMBL	235	4	3	3	0.5	OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N	10.1021/jm980571q
	68109335	163890	0	None	-	1	Human	9.0	pKd	=	9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074664	163890	0	None	-	1	Human	9.0	pKd	=	9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785087	164919	0	None	-	1	Human	9.0	pKd	=	9.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4087196	164919	0	None	-	1	Human	9.0	pKd	=	9.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	49801370	163814	0	None	-	1	Human	8.9	pKd	=	8.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4073628	163814	0	None	-	1	Human	8.9	pKd	=	8.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	68109941	162901	0	None	-	1	Human	8.8	pKd	=	8.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	162901	0	None	-	1	Human	8.8	pKd	=	8.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66786131	163945	0	None	-	1	Human	8.0	pKd	=	8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075417	163945	0	None	-	1	Human	8.0	pKd	=	8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66786493	164039	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076639	164039	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	137652500	163968	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075697	163968	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109677	163972	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075762	163972	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	44595851	10574	4	None	-	1	Human	7.0	pKd	=	7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	6259	10574	4	None	-	1	Human	7.0	pKd	=	7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	CHEMBL4092105	10574	4	None	-	1	Human	7.0	pKd	=	7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	68109605	165169	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089955	165169	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	66786069	163240	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	163240	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	66784529	163872	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074421	163872	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66785027	165117	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089416	165117	0	None	-	1	Human	7.9	pKd	=	7.9	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	66785551	163932	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075258	163932	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785393	163673	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072134	163673	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	66784675	163953	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075537	163953	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	68109333	164408	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4081244	164408	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66784246	163143	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4066051	163143	0	None	-	1	Human	7.8	pKd	=	7.8	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109272	165397	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4092275	165397	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	3954	7451	60	None	-	1	Human	6.7	pKd	=	6.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	9868580	7451	60	None	-	1	Human	6.7	pKd	=	6.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL593013	7451	60	None	-	1	Human	6.7	pKd	=	6.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	66785780	165523	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093657	165523	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	66787433	163242	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067298	163242	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	66784262	165010	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4088239	165010	0	None	-	1	Human	8.7	pKd	=	8.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	70209638	164388	0	None	-	1	Human	8.6	pKd	=	8.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4080973	164388	0	None	-	1	Human	8.6	pKd	=	8.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109580	165304	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4091370	165304	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	66784890	162829	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4062535	162829	0	None	-	1	Human	7.7	pKd	=	7.7	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	66785101	164824	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4085882	164824	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	66786816	165135	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4089612	165135	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	68109425	165069	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4088960	165069	0	None	-	1	Human	7.6	pKd	=	7.6	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	68108857	164117	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4077609	164117	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66786493	166458	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4104081	166458	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	49801369	165528	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093792	165528	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	66785300	163251	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	CHEMBL4067421	163251	0	None	-	1	Human	8.5	pKd	=	8.5	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	66787355	163004	0	None	-	1	Human	8.4	pKd	=	8.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	163004	0	None	-	1	Human	8.4	pKd	=	8.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	49801371	165520	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093620	165520	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	66785182	163957	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075593	163957	0	None	-	1	Human	7.4	pKd	=	7.4	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	59234231	8924	4	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6330	8924	4	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6331	8924	4	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	CHEMBL3337510	8924	4	None	-2	2	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	68109379	164004	0	None	-	1	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4076286	164004	0	None	-	1	Human	7.3	pKd	=	7.3	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	66785010	162642	0	None	-	1	Human	8.2	pKd	=	8.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4060306	162642	0	None	-	1	Human	8.2	pKd	=	8.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	25125217	7343	25	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	7678	7343	25	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL3937907	7343	25	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	DB16073	7343	25	None	-	1	Human	6.2	pKd	=	6.2	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	66786902	166240	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4101354	166240	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109333	166171	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4100691	166171	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66784572	163687	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072262	163687	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	137652320	164053	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076786	164053	0	None	-	1	Human	8.1	pKd	=	8.1	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	49801368	166437	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4103808	166437	0	None	-	1	Human	8.0	pKd	=	8.0	Binding	Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	68109941	162901	0	None	-	1	Human	9.1	pKi	=	9.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4063313	162901	0	None	-	1	Human	9.1	pKi	=	9.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	504	6	2	5	6.5	O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	117972250	149090	3	None	-	1	Human	9.0	pKi	=	9	Binding	Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	CHEMBL3885379	149090	3	None	-	1	Human	9.0	pKi	=	9	Binding	Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method	ChEMBL	421	6	0	4	5.5	FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12	10.1016/j.bmc.2016.11.018
	11325656	133547	0	None	-	1	Rat	9.0	pKi	=	9.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	6	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL365305	133547	0	None	-	1	Rat	9.0	pKi	=	9.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	6	4	5	0.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11211507	72221	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL182972	72221	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11339150	133931	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL365680	133931	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	66786902	166240	0	None	-	1	Human	8.8	pKi	=	8.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4101354	166240	0	None	-	1	Human	8.8	pKi	=	8.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	5	0	5	6.8	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	11177216	73097	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL184983	73097	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11383191	103379	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	CHEMBL263312	103379	0	None	-	1	Rat	8.8	pKi	=	8.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	68108857	164117	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4077609	164117	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	465	5	1	5	5.7	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66785551	163932	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075258	163932	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	5	0	5	5.9	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109605	165169	0	None	-	1	Human	8.0	pKi	=	8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089955	165169	0	None	-	1	Human	8.0	pKi	=	8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1	10.1021/acs.jmedchem.7b00669
	66785027	165117	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4089416	165117	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	356	5	1	4	4.7	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	67637138	190397	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4776989	190397	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802329	190397	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	49836087	7847	0	None	-	1	Human	6.0	pKi	=	6	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	6222	7847	0	None	-	1	Human	6.0	pKi	=	6	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	CHEMBL1630805	7847	0	None	-	1	Human	6.0	pKi	=	6	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	10.1021/jm101069m
	15461589	107205	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL290416	107205	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	11756841	168097	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41242	168097	0	None	-	1	Rat	6.0	pKi	=	6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	11768848	122030	11	None	-	1	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347671	122030	11	None	-	1	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@H]1CC(=O)O	10.1039/C1MD00186H
	11195342	130812	0	None	-	1	Rat	7.0	pKi	=	7.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363034	130812	0	None	-	1	Rat	7.0	pKi	=	7.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	68109333	164408	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4081244	164408	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	66787433	163242	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067298	163242	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	460	6	0	6	5.9	CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	66784675	163953	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075537	163953	0	None	-	1	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	472	7	0	6	5.5	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	11188098	129875	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL361024	129875	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1377	8122	26	None	-2	6	Human	7.0	pKi	=	7.0	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm010323l
	5310979	8122	26	None	-2	6	Human	7.0	pKi	=	7.0	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm010323l
	CHEMBL284193	8122	26	None	-2	6	Human	7.0	pKi	=	7.0	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10.1021/jm010323l
	1310	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	1369	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	33032	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	44272391	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	88747398	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	CHEMBL575060	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	DB00142	9095	110	None	-22	18	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm070322e
	71476419	130187	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616860	130187	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	155533313	178631	0	None	-	1	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4468977	178631	0	None	-	1	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	60096194	163367	0	None	-10	2	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068679	163367	0	None	-10	2	Human	5.0	pKi	=	5.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	290	5	4	4	0.3	N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11462089	74116	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188532	74116	0	None	-	1	Rat	7.9	pKi	=	7.9	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1310	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	1369	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	33032	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	44272391	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	88747398	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	CHEMBL575060	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	DB00142	9095	110	None	-22	18	Human	5.9	pKi	=	5.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1021/jm010323l
	162652146	186992	0	None	-1	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4749728	186992	0	None	-1	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	289	5	4	5	-0.2	CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O	10.1021/acs.jmedchem.6b01119
	71135411	130175	0	None	-1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616848	130175	0	None	-1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	71681826	96836	0	None	-4	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381651	96836	0	None	-4	2	Human	5.9	pKi	=	5.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	1393	8321	64	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	1396	8321	64	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	213056	8321	64	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	CHEMBL8759	8321	64	None	-2	6	Human	7.9	pKi	=	7.9	Binding	Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm010323l
	71131322	130184	0	None	4	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616857	130184	0	None	4	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	60096250	165700	0	None	-60	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095567	165700	0	None	-60	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	10197984	9199	44	None	2	5	Human	7.9	pKi	=	7.9	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	9199	44	None	2	5	Human	7.9	pKi	=	7.9	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	9199	44	None	2	5	Human	7.9	pKi	=	7.9	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	10197984	9199	44	None	2	5	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	1394	9199	44	None	2	5	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL275079	9199	44	None	2	5	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm060917u
	69669646	190458	0	None	1	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4757159	190458	0	None	1	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	CHEMBL4802990	190458	0	None	1	2	Human	7.9	pKi	=	7.9	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	351	5	4	5	1.1	Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C	10.1021/acs.jmedchem.6b01119
	11348518	133072	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL365018	133072	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66784246	163143	0	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4066051	163143	0	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	418	5	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	71136640	130180	0	None	1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616853	130180	0	None	1	2	Human	6.9	pKi	=	6.9	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	53240406	130174	17	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616847	130174	17	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	9834591	144378	69	None	-1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL375611	144378	69	None	-1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	235	2	3	5	-2.1	N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	49765871	8926	45	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	6317	8926	45	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	CHEMBL2179319	8926	45	None	-	1	Human	7.8	pKi	=	7.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.6b00913
	11393152	73769	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	324	5	4	5	0.4	Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL186891	73769	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	324	5	4	5	0.4	Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	49822116	153770	13	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	CHEMBL3926416	153770	13	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	451	5	0	5	4.3	Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1	10.1021/acs.jmedchem.6b00913
	9914583	148743	0	None	-	1	Rat	5.8	pKi	=	5.8	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL38729	148743	0	None	-	1	Rat	5.8	pKi	=	5.8	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	60096183	166063	0	None	-6	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL4099470	166063	0	None	-6	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	137635882	162673	0	None	-1	2	Human	5.8	pKi	=	5.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4060567	162673	0	None	-1	2	Human	5.8	pKi	=	5.8	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	310	4	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11310142	9200	19	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	9200	19	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	9200	19	None	1	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	155533313	178631	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4468977	178631	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	70052526	96827	2	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL2381642	96827	2	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	11164815	129129	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL359973	129129	0	None	-	1	Rat	7.8	pKi	=	7.8	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	71137008	130182	0	None	-2	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616855	130182	0	None	-2	2	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	298	4	4	6	-0.3	Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	155548817	180619	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	66785101	164824	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4085882	164824	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	422	6	0	5	5.9	CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	25195461	8925	48	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	8946	8925	48	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	CHEMBL3337527	8925	48	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	DB12059	8925	48	None	-	1	Human	6.8	pKi	=	6.8	Binding	Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)	ChEMBL	344	5	0	3	4.7	CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.6b00913
	1310	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	1369	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	33032	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	44272391	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	88747398	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	CHEMBL575060	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	DB00142	9095	110	None	-22	18	Human	5.7	pKi	=	5.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1039/C1MD00186H
	60096246	162726	0	None	-40	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	CHEMBL4061162	162726	0	None	-40	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1	10.1021/acs.jmedchem.7b01481
	11172339	73130	0	None	-	1	Rat	6.7	pKi	=	6.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185135	73130	0	None	-	1	Rat	6.7	pKi	=	6.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	11326253	72090	0	None	-	1	Rat	8.7	pKi	=	8.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	CHEMBL182899	72090	0	None	-	1	Rat	8.7	pKi	=	8.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	373	5	3	4	2.5	C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1	10.1021/jm0400294
	68109580	165304	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4091370	165304	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	471	7	1	6	5.5	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1	10.1021/acs.jmedchem.7b00669
	66786493	166458	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4104081	166458	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	1397	9307	15	None	1	5	Human	8.7	pKi	=	8.7	Binding	Binding affinity to mGLUR2Binding affinity to mGLUR2	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	9886034	9307	15	None	1	5	Human	8.7	pKi	=	8.7	Binding	Binding affinity to mGLUR2Binding affinity to mGLUR2	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	CHEMBL186453	9307	15	None	1	5	Human	8.7	pKi	=	8.7	Binding	Binding affinity to mGLUR2Binding affinity to mGLUR2	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1016/j.bmcl.2012.01.039
	49801370	163814	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4073628	163814	0	None	-	1	Human	8.7	pKi	=	8.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	406	5	1	4	5.6	FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	11382367	73711	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186630	73711	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1397	9307	15	None	-1	5	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	9886034	9307	15	None	-1	5	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186453	9307	15	None	-1	5	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11405687	73231	0	None	2	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185210	73231	0	None	2	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	70209638	164388	0	None	-	1	Human	8.6	pKi	=	8.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4080973	164388	0	None	-	1	Human	8.6	pKi	=	8.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	456	5	0	5	6.3	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	11257636	175151	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL434536	175151	0	None	1	2	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.4	N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11375886	131134	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	521	6	3	4	5.0	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363724	131134	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	521	6	3	4	5.0	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11198402	133863	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	334	5	3	5	0.7	N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL365647	133863	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	334	5	3	5	0.7	N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	57338826	156406	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3947221	156406	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	11259548	73461	0	None	-	1	Rat	7.7	pKi	=	7.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185456	73461	0	None	-	1	Rat	7.7	pKi	=	7.7	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	162658340	190465	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4760856	190465	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803084	190465	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	405	6	4	5	1.9	N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	10197984	9199	44	None	2	5	Human	5.7	pKi	=	5.7	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	9199	44	None	2	5	Human	5.7	pKi	=	5.7	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	9199	44	None	2	5	Human	5.7	pKi	=	5.7	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	15518713	107044	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1	10.1016/s0960-894x(99)00227-9
	CHEMBL288902	107044	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1	10.1016/s0960-894x(99)00227-9
	15461591	168676	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	521	6	0	6	6.5	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41513	168676	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	521	6	0	6	6.5	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	15461594	169950	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.6	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41808	169950	0	None	-	1	Rat	5.7	pKi	=	5.7	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.6	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	162658781	190470	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4759209	190470	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803105	190470	0	None	-1	2	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	66786131	163945	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075417	163945	0	None	-	1	Human	7.7	pKi	=	7.7	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	402	5	0	5	5.6	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	60096190	165292	0	None	-102	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091203	165292	0	None	-102	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	60096236	165201	0	None	-38	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4090293	165201	0	None	-38	2	Human	6.7	pKi	=	6.7	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	9815617	121277	7	None	1	2	Rat	7.7	pKi	=	7.7	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	CHEMBL333519	121277	7	None	1	2	Rat	7.7	pKi	=	7.7	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.4	N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm000346k
	68109425	165069	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4088960	165069	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	417	5	0	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1	10.1021/acs.jmedchem.7b00669
	45082292	122029	2	None	-3	3	Human	4.7	pKi	=	4.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	CHEMBL3347670	122029	2	None	-3	3	Human	4.7	pKi	=	4.7	Binding	Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells	ChEMBL	159	3	3	3	-0.7	N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O	10.1039/C1MD00186H
	44361401	38115	0	None	-7	2	Human	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	CHEMBL140197	38115	0	None	-7	2	Human	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined	ChEMBL	175	3	4	4	-1.9	N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O	10.1021/jm030967o
	1393	8321	64	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	1396	8321	64	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	213056	8321	64	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	CHEMBL8759	8321	64	None	1	6	Rat	7.6	pKi	=	7.6	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm000346k
	11084869	96828	2	None	-	1	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL2381643	96828	2	None	-	1	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	201	2	4	4	-1.5	N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	155548817	180619	0	None	-	1	Human	6.6	pKi	=	6.6	Binding	Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	6.6	pKi	=	6.6	Binding	Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	69669702	190454	0	None	1	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4756556	190454	0	None	1	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4802948	190454	0	None	1	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	354	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	15518714	107100	0	None	-	1	Rat	5.6	pKi	=	5.6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL289394	107100	0	None	-	1	Rat	5.6	pKi	=	5.6	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	137652500	163968	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075697	163968	0	None	-	1	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	6	0	5	6.4	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	11361140	131096	0	None	-	1	Rat	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363526	131096	0	None	-	1	Rat	7.6	pKi	=	7.6	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	59234231	8924	4	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6330	8924	4	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	6331	8924	4	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	CHEMBL3337510	8924	4	None	-2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	10.1021/acs.jmedchem.7b00669
	71136655	130179	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616852	130179	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	162644419	190401	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4778355	190401	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802356	190401	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	71137011	130185	0	None	2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616858	130185	0	None	2	2	Human	7.6	pKi	=	7.6	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	10089411	14299	0	None	-	1	Human	5.6	pKi	=	5.6	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL108735	14299	0	None	-	1	Human	5.6	pKi	=	5.6	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	353	5	3	4	2.7	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	162663798	190498	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4779554	190498	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	CHEMBL4803378	190498	0	None	-1	2	Human	6.6	pKi	=	6.6	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1	10.1021/acs.jmedchem.6b01119
	11220424	165740	0	None	-43	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4095995	165740	0	None	-43	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	304	4	4	4	-0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	66784529	163872	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074421	163872	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	430	5	2	5	5.4	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	11200955	71381	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL181710	71381	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	419	7	3	4	3.4	CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11177217	73450	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL185423	73450	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	405	6	3	4	3.1	CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	1378	9195	54	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	1399	9195	54	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	9819927	9195	54	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	CHEMBL432038	9195	54	None	-1	10	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/jm0400294
	66785780	165523	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093657	165523	0	None	-	1	Human	8.5	pKi	=	8.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	453	7	1	6	5.4	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	11279365	74334	0	None	1	2	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189814	74334	0	None	1	2	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11221617	74165	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188787	74165	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1395	9306	15	None	2	2	Rat	8.5	pKi	=	8.5	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	9837317	9306	15	None	2	2	Rat	8.5	pKi	=	8.5	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	CHEMBL121053	9306	15	None	2	2	Rat	8.5	pKi	=	8.5	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	10.1021/jm000346k
	11314439	128804	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL359491	128804	0	None	-	1	Rat	8.5	pKi	=	8.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66784572	163687	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072262	163687	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	468	6	0	5	6.6	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	66785087	164919	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4087196	164919	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	390	5	1	4	5.1	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	11418500	129113	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	411	5	3	4	2.8	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL359905	129113	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	411	5	3	4	2.8	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	10807972	42591	1	None	1	2	Rat	8.4	pKi	=	8.4	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	CHEMBL144151	42591	1	None	1	2	Rat	8.4	pKi	=	8.4	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	353	5	3	4	2.8	N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O	10.1021/jm000346k
	11248009	133329	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL365244	133329	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	453	6	3	4	3.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11153780	130609	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	399	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL362459	130609	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	399	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11212336	131130	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	421	6	3	4	2.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363696	131130	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	421	6	3	4	2.7	N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11485742	176253	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL442967	176253	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66785300	163251	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	CHEMBL4067421	163251	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	1	4	5.8	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl	10.1021/acs.jmedchem.7b00669
	162665071	190507	0	None	-1	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4781638	190507	0	None	-1	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803454	190507	0	None	-1	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	323	5	4	5	0.5	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	15518719	175259	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL435174	175259	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	531	8	0	7	6.2	CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	60096201	165347	0	None	-13	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4091735	165347	0	None	-13	2	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	68109333	166171	0	None	-	1	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4100691	166171	0	None	-	1	Human	7.5	pKi	=	7.5	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	459	4	1	5	5.5	O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	10130658	73527	0	None	2	2	Rat	7.5	pKi	=	7.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185822	73527	0	None	2	2	Rat	7.5	pKi	=	7.5	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	219	2	4	4	-1.4	N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	15518717	170152	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	505	6	0	6	6.0	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL41932	170152	0	None	-	1	Rat	5.5	pKi	=	5.5	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	505	6	0	6	6.0	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	60096204	162903	0	None	-75	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4063336	162903	0	None	-75	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	322	4	4	4	0.1	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	71136654	130186	0	None	-4	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616859	130186	0	None	-4	2	Human	6.5	pKi	=	6.5	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	326	5	4	6	0.5	CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	10197984	9199	44	None	2	5	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	1394	9199	44	None	2	5	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL275079	9199	44	None	2	5	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10.1021/jm980616n
	25125217	7343	25	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	7678	7343	25	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL3937907	7343	25	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	DB16073	7343	25	None	-	1	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	487	6	1	7	3.5	Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1	10.1021/acs.jmedchem.7b00669
	68109272	165397	0	None	-	1	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4092275	165397	0	None	-	1	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	416	5	1	5	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1	10.1021/acs.jmedchem.7b00669
	10192719	72888	0	None	2	2	Rat	7.4	pKi	=	7.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL183956	72888	0	None	2	2	Rat	7.4	pKi	=	7.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	233	3	3	4	-0.8	CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	137659992	166015	0	None	-14	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4098939	166015	0	None	-14	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	11360426	130581	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL362325	130581	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	361	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11749464	131814	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL364320	131814	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	155567633	182779	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4589377	182779	0	None	-	1	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	11484738	173056	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL426983	173056	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11268934	73901	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL187482	73901	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	1378	9195	54	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	1399	9195	54	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	9819927	9195	54	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	CHEMBL432038	9195	54	None	-2	10	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10.1021/acs.jmedchem.6b01119
	11188099	73601	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186107	73601	0	None	-	1	Rat	8.4	pKi	=	8.4	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	10353365	90022	1	None	-5	2	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	90022	1	None	-5	2	Human	8.4	pKi	=	8.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	11255753	129053	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	323	5	3	4	1.1	Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL359805	129053	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	323	5	3	4	1.1	Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	11290903	74112	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188511	74112	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11188380	74240	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	387	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189186	74240	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	387	5	3	4	1.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11163717	130448	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL362092	130448	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	343	5	3	4	1.5	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	10198133	213287	12	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	213287	12	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	10198133	213287	12	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL8839	213287	12	None	-6	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	15518715	107097	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.5	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL289388	107097	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	545	8	0	7	6.5	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21	10.1016/s0960-894x(99)00227-9
	15518712	107270	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	483	7	0	7	5.2	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21	10.1016/s0960-894x(99)00227-9
	CHEMBL291017	107270	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	483	7	0	7	5.2	COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21	10.1016/s0960-894x(99)00227-9
	15392100	175874	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	474	5	0	6	6.3	CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC	10.1016/s0960-894x(99)00227-9
	CHEMBL439925	175874	0	None	-	1	Rat	5.4	pKi	=	5.4	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	474	5	0	6	6.3	CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC	10.1016/s0960-894x(99)00227-9
	11310142	9200	19	None	1	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	11614	9200	19	None	1	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	CHEMBL192051	9200	19	None	1	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	10.1021/jm040222y
	60096231	164434	15	None	-446	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	CHEMBL4081453	164434	15	None	-446	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	5	-0.1	COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1	10.1021/acs.jmedchem.7b01481
	10979251	96835	0	None	-3	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL2381650	96835	0	None	-3	2	Human	6.4	pKi	=	6.4	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	293	4	3	4	1.3	N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	162666357	190510	0	None	-1	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4784701	190510	0	None	-1	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4803523	190510	0	None	-1	2	Human	7.4	pKi	=	7.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	11275666	96832	1	None	-15	2	Human	5.4	pKi	=	5.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381647	96832	1	None	-15	2	Human	5.4	pKi	=	5.4	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	200	2	4	4	-1.6	N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	9815616	121578	6	None	1	2	Rat	7.3	pKi	=	7.3	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	CHEMBL334014	121578	6	None	1	2	Rat	7.3	pKi	=	7.3	Binding	Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand	ChEMBL	203	2	3	3	-0.5	N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm000346k
	66787355	163004	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4064589	163004	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	5	1	5	5.6	FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	11196276	175119	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	261	5	3	4	0.0	CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL434338	175119	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	261	5	3	4	0.0	CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	67637415	190466	0	None	-1	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4759992	190466	0	None	-1	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803099	190466	0	None	-1	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	438	7	4	7	1.9	Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	66786069	163240	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4067290	163240	0	None	-	1	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	451	5	0	5	5.6	FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	69669747	190432	11	None	-2	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4751065	190432	11	None	-2	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802733	190432	11	None	-2	2	Human	8.3	pKi	=	8.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	359	5	4	5	0.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	11268363	131517	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL364201	131517	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	359	5	3	4	2.0	N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11450243	74232	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	327	5	3	4	0.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189139	74232	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	327	5	3	4	0.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11451742	131223	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363980	131223	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	2.1	N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11349412	74318	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	1.8	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL189710	74318	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	377	5	3	4	1.8	N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	155567633	182779	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4589377	182779	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	532	7	1	6	5.0	O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	11338331	72308	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	CHEMBL183073	72308	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	391	5	3	4	2.7	C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1	10.1021/jm0400294
	11313770	130653	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	339	6	3	5	0.8	COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	CHEMBL362708	130653	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	339	6	3	5	0.8	COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1	10.1021/jm0400294
	10353365	90022	1	None	-5	2	Human	6.3	pKi	=	6.3	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	CHEMBL218710	90022	1	None	-5	2	Human	6.3	pKi	=	6.3	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	219	2	3	4	-1.8	N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm060917u
	66785182	163957	0	None	-	1	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075593	163957	0	None	-	1	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	434	6	0	5	6.2	Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1	10.1021/acs.jmedchem.7b00669
	60096228	163566	0	None	-5	2	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4070866	163566	0	None	-5	2	Human	7.3	pKi	=	7.3	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	60096224	163324	0	None	-32	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4068189	163324	0	None	-32	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	320	4	5	5	-0.4	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL5076351	221209	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1	10.1021/acs.jmedchem.1c02004
	CHEMBL5076351	221209	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1	10.1021/acs.jmedchem.1c02004
	137634033	163420	0	None	-2	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4069251	163420	0	None	-2	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	332	6	4	4	0.2	N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	68109335	163890	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4074664	163890	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	438	5	0	5	6.5	Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1	10.1021/acs.jmedchem.7b00669
	68109677	163972	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4075762	163972	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	458	4	2	5	5.5	O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	155548817	180619	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	66786816	165135	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	CHEMBL4089612	165135	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	426	6	0	6	5.5	CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12	10.1021/acs.jmedchem.7b00669
	44396480	73611	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	275	5	3	4	0.4	CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186145	73611	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	275	5	3	4	0.4	CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	66785010	162642	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4060306	162642	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	372	5	1	4	5.2	Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1	10.1021/acs.jmedchem.7b00669
	3954	7451	60	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	9868580	7451	60	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	CHEMBL593013	7451	60	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	454	6	1	3	6.8	Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1	10.1021/acs.jmedchem.7b00669
	71136653	130181	0	None	2	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616854	130181	0	None	2	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	284	4	4	6	-0.6	N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	49858117	7875	4	None	-	1	Human	6.2	pKi	=	6.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	6223	7875	4	None	-	1	Human	6.2	pKi	=	6.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	CHEMBL1630806	7875	4	None	-	1	Human	6.2	pKi	=	6.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	10.1021/jm101069m
	66784890	162829	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4062535	162829	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	358	5	1	4	5.0	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F	10.1021/acs.jmedchem.7b00669
	68109379	164004	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	CHEMBL4076286	164004	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	6	1	5	5.3	FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12	10.1021/acs.jmedchem.7b00669
	155548817	180619	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	CHEMBL4538850	180619	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	518	6	1	6	5.3	O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1	10.1021/acs.jmedchem.8b00051
	137656301	165461	0	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4093017	165461	0	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	324	5	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL5089623	221996	2	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	CHEMBL5089623	221996	2	None	-	1	Human	7.2	pKi	=	7.2	Binding	Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay	ChEMBL		None	None	None		COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1	10.1021/acs.jmedchem.1c02004
	49801371	165520	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093620	165520	0	None	-	1	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	408	5	0	5	5.6	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	11344646	133554	1	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	CHEMBL365368	133554	1	None	-1	2	Human	6.2	pKi	=	6.2	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/jm040222y
	1310	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	1369	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	33032	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	44272391	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	88747398	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	CHEMBL575060	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	DB00142	9095	110	None	-22	18	Human	5.2	pKi	=	5.2	Binding	Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells	ChEMBL	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10.1016/j.bmc.2008.11.015
	49858116	63122	0	None	-	1	Human	5.2	pKi	=	5.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	312	2	2	4	2.8	O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2	10.1021/jm101069m
	CHEMBL1630804	63122	0	None	-	1	Human	5.2	pKi	=	5.2	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	312	2	2	4	2.8	O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2	10.1021/jm101069m
	71137012	130178	0	None	-1	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	CHEMBL3616851	130178	0	None	-1	2	Human	7.2	pKi	=	7.2	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	299	4	5	7	-1.0	Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1	10.1021/acs.jmedchem.5b01124
	10198133	213287	12	None	-6	2	Human	7.2	pKi	=	7.2	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	213287	12	None	-6	2	Human	7.2	pKi	=	7.2	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	11484739	129880	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL361051	129880	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	345	5	3	4	1.1	N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11817779	72982	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	259	5	3	4	-0.2	C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL184441	72982	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	259	5	3	4	-0.2	C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O	10.1021/jm0400294
	49801368	166437	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4103808	166437	0	None	-	1	Human	8.2	pKi	=	8.2	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	442	5	0	5	6.0	Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1	10.1021/acs.jmedchem.7b00669
	11347391	73626	0	None	2	2	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186214	73626	0	None	2	2	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	309	5	3	4	0.8	N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11258119	74094	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	401	7	3	5	2.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL188425	74094	0	None	-	1	Rat	8.2	pKi	=	8.2	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	401	7	3	5	2.6	N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	66785393	163673	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4072134	163673	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	419	7	1	6	5.0	COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1	10.1021/acs.jmedchem.7b00669
	67705089	159034	0	None	-2	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	CHEMBL3969063	159034	0	None	-2	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	458	7	4	7	1.9	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1016/j.bmcl.2016.10.067
	49822115	8927	21	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	8947	8927	21	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	CHEMBL3947764	8927	21	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	49822115	8927	21	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	8947	8927	21	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	CHEMBL3947764	8927	21	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method	ChEMBL	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	10.1021/acs.jmedchem.8b00051
	11772601	134286	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	354	6	3	6	0.7	N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL366152	134286	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	354	6	3	6	0.7	N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	49801369	165528	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	CHEMBL4093792	165528	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	450	4	0	5	6.1	Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1	10.1021/acs.jmedchem.7b00669
	15392101	107215	0	None	-	1	Rat	5.2	pKi	=	5.2	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/s0960-894x(99)00227-9
	CHEMBL290509	107215	0	None	-	1	Rat	5.2	pKi	=	5.2	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	517	7	0	7	5.8	COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1	10.1016/s0960-894x(99)00227-9
	1393	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1396	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	213056	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	CHEMBL8759	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.5b01124
	1393	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	1396	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	213056	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	CHEMBL8759	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/acs.jmedchem.7b01481
	162654849	190449	0	None	-1	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4755204	190449	0	None	-1	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802906	190449	0	None	-1	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	341	5	4	5	0.6	N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	1393	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	1396	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	213056	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	CHEMBL8759	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm040222y
	1393	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	1396	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	213056	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	CHEMBL8759	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm980616n
	1393	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	1396	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	213056	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	CHEMBL8759	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm060917u
	134132133	151567	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	CHEMBL3909237	151567	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method	ChEMBL	375	5	4	5	1.0	N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1016/j.bmcl.2016.10.067
	44595851	10574	4	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	6259	10574	4	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	CHEMBL4092105	10574	4	None	-	1	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method	ChEMBL	475	8	2	6	4.5	Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C	10.1021/acs.jmedchem.7b00669
	67633284	190426	0	None	1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4748699	190426	0	None	1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	CHEMBL4802655	190426	0	None	1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	391	5	4	5	1.8	N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O	10.1021/acs.jmedchem.6b01119
	90098428	130183	0	None	5	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616856	130183	0	None	5	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	11449064	131172	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	287	4	3	4	0.5	N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL363940	131172	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	287	4	3	4	0.5	N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	137652320	164053	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076786	164053	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	454	7	0	6	5.4	COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1	10.1021/acs.jmedchem.7b00669
	11267024	73433	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	315	5	3	5	0.9	N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL185335	73433	0	None	-	1	Rat	8.1	pKi	=	8.1	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	315	5	3	5	0.9	N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	67633340	190500	0	None	-1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4780402	190500	0	None	-1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	CHEMBL4803381	190500	0	None	-1	2	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	355	5	4	5	0.9	Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F	10.1021/acs.jmedchem.6b01119
	66784262	165010	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	CHEMBL4088239	165010	0	None	-	1	Human	8.1	pKi	=	8.1	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	392	5	1	4	5.3	CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F	10.1021/acs.jmedchem.7b00669
	49858118	7894	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	6224	7894	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	CHEMBL1630807	7894	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay	ChEMBL	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	10.1021/jm101069m
	15518718	106999	0	None	-	1	Rat	5.1	pKi	=	5.1	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	501	6	0	6	6.1	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	CHEMBL288472	106999	0	None	-	1	Rat	5.1	pKi	=	5.1	Binding	Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells	ChEMBL	501	6	0	6	6.1	CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1	10.1016/s0960-894x(99)00227-9
	10198133	213287	12	None	-6	2	Human	6.1	pKi	=	6.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	CHEMBL8839	213287	12	None	-6	2	Human	6.1	pKi	=	6.1	Binding	Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.	ChEMBL	203	2	3	4	-0.8	N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/jm980616n
	71137010	130176	0	None	-1	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616849	130176	0	None	-1	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	352	4	4	6	0.4	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	1393	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	1396	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	213056	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	CHEMBL8759	8321	64	None	-2	6	Human	7.1	pKi	=	7.1	Binding	Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors	ChEMBL	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10.1021/jm050235r
	9885546	117315	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	CHEMBL325140	117315	0	None	-	1	Human	7.1	pKi	=	7.1	Binding	Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2	ChEMBL	367	6	3	4	3.1	NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21	10.1016/s0960-894x(01)00656-4
	60096178	163660	0	None	-181	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	CHEMBL4071962	163660	0	None	-181	2	Human	7.1	pKi	=	7.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	338	4	4	4	0.6	N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.7b01481
	60096211	96834	0	None	-5	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	CHEMBL2381649	96834	0	None	-5	2	Human	6.1	pKi	=	6.1	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting	ChEMBL	242	3	4	4	-1.4	CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12	10.1021/acs.jmedchem.7b01481
	69669820	190419	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4746125	190419	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	CHEMBL4802570	190419	0	None	-1	2	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method	ChEMBL	396	6	4	5	1.1	CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1	10.1021/acs.jmedchem.6b01119
	66786493	164039	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	CHEMBL4076639	164039	0	None	-	1	Human	8.0	pKi	=	8.0	Binding	Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis	ChEMBL	464	5	2	5	5.7	O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1	10.1021/acs.jmedchem.7b00669
	11749463	72996	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL184504	72996	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	385	6	3	4	2.5	N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	11209918	73627	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	337	7	3	4	1.2	N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	CHEMBL186215	73627	0	None	-	1	Rat	8.0	pKi	=	8.0	Binding	Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008	ChEMBL	337	7	3	4	1.2	N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	10.1021/jm0400294
	71137034	130177	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	CHEMBL3616850	130177	0	None	-1	2	Human	7.0	pKi	=	7.0	Binding	Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting	ChEMBL	334	5	4	6	0.3	N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21	10.1021/acs.jmedchem.5b01124
	11298568	76150	1	None	-6	2	Human	6.0	pKi	=	6.0	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	CHEMBL192977	76150	1	None	-6	2	Human	6.0	pKi	=	6.0	Binding	Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2	ChEMBL	199	2	3	3	-0.2	C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O	10.1021/jm040222y
	49822115	8927	21	None	-	1	Human	8.8	pKd	=	8.8	Binding	Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	8947	8927	21	None	-	1	Human	8.8	pKd	=	8.8	Binding	Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	CHEMBL3947764	8927	21	None	-	1	Human	8.8	pKd	=	8.8	Binding	Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	59234231	8924	4	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	8924	4	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	8924	4	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	8924	4	None	-2	2	Human	7.9	pKd	=	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	59234231	8924	4	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6330	8924	4	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	6331	8924	4	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	CHEMBL3337510	8924	4	None	2	2	Rat	8.0	pKd	=	8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	333	4	0	4	3.5	N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1	23766542
	11362035	6831	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	6328	6831	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	6329	6831	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	CHEMBL105296	6831	1	None	-	1	Rat	8.4	pKd	=	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	416	9	0	4	4.5	CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C	21470207
	1393	8321	64	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1396	8321	64	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	213056	8321	64	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	CHEMBL8759	8321	64	None	1	6	Rat	7.7	pKd	None	7.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1378	9195	54	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	1399	9195	54	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	9819927	9195	54	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	CHEMBL432038	9195	54	None	-2	10	Human	8.8	pKd	None	8.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	None	223112	0	3H-LY354740	-	1	Rat	8.0	pKi	=	8	Binding	NoneNone	PDSP KiDatabase	323	5	5	9	-1.3	C1C(C1C(CN2C=NC3=C2N=C(N=C3O)O)(C(=O)O)N)C(=O)O	None
	12310764	8751	64	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	12310764	8751	64	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	12310764	8751	64	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1233	8751	64	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1233	8751	64	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1233	8751	64	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1371	8751	64	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1371	8751	64	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1371	8751	64	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	CHEMBL284895	8751	64	Functional	-14	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	CHEMBL284895	8751	64	3H-LY354740	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	CHEMBL284895	8751	64	Functional	-14	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	158	2	3	4	-0.9	OC(=O)C(c1o[nH]c(=O)c1)N	None
	1310	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	Functional	-13	18	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	134	9292	24	Functional	-8511	67	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	1775	9292	24	Functional	-8511	67	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	9681	9292	24	Functional	-8511	67	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	CHEMBL1065	9292	24	Functional	-8511	67	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	DB00247	9292	24	Functional	-8511	67	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	353	4	2	4	1.9	CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO	None
	15897	9637	0	Functional	-354	36	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	203	2	1	1	2.6	CC(Cc1cccc(c1)C(F)(F)F)N	None
	215	9637	0	Functional	-354	36	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	203	2	1	1	2.6	CC(Cc1cccc(c1)C(F)(F)F)N	None
	CHEMBL1979333	9637	0	Functional	-354	36	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	203	2	1	1	2.6	CC(Cc1cccc(c1)C(F)(F)F)N	None
	1370	10037	67	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	1370	10037	67	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	1372	10037	67	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	1372	10037	67	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	40539	10037	67	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	40539	10037	67	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	6971145	10037	67	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	6971145	10037	67	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	CHEMBL279956	10037	67	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	CHEMBL279956	10037	67	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	DB02999	10037	67	Functional	-602	8	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	DB02999	10037	67	3H-LY354740	-602	8	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	189	3	3	6	-2.5	OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N	None
	128563	10237	33	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	1666	10237	33	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	CHEMBL445332	10237	33	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	DB12327	10237	33	Functional	-2398	42	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	432	3	0	8	3.0	COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1	None
	10297	33885	30	Functional	-38	43	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	C[C@H](N)[C@H](O)c1ccccc1	None
	CHEMBL136560	33885	30	Functional	-38	43	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	C[C@H](N)[C@H](O)c1ccccc1	None
	2207	106641	63	3H-LY354740	-25	7	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	183	4	4	3	-1.0	NC(CCP(=O)(O)O)C(=O)O	None
	CHEMBL285843	106641	63	3H-LY354740	-25	7	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	183	4	4	3	-1.0	NC(CCP(=O)(O)O)C(=O)O	None
	1222	108514	63	Functional	5	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL299683	108514	63	Functional	5	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	209	3	3	3	0.6	CC(N)(C(=O)O)c1ccc(C(=O)O)cc1	None
	5115	118824	47	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	5115	118824	47	3H-GLUTAMATE	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	5115	118824	47	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL328984	118824	47	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL328984	118824	47	3H-GLUTAMATE	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	CHEMBL328984	118824	47	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	195	3	3	3	0.5	NC(C(=O)O)c1ccc(C(=O)O)cc1	None
	446220	140299	14	Functional	-1778	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	303	3	0	5	1.9	COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C	None
	CHEMBL370805	140299	14	Functional	-1778	45	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	303	3	0	5	1.9	COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C	None
	19702198	168101	16	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	19702198	168101	16	3H-LY354740	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	19702198	168101	16	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	CHEMBL412445	168101	16	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	CHEMBL412445	168101	16	3H-LY354740	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	CHEMBL412445	168101	16	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	3	3	3	-0.5	CC(N)(C(=O)O)C1CC1C(=O)O	None
	1615	174570	24	Functional	-26	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	193	3	1	3	1.6	CNC(C)Cc1ccc2c(c1)OCO2	None
	CHEMBL43048	174570	24	Functional	-26	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	193	3	1	3	1.6	CNC(C)Cc1ccc2c(c1)OCO2	None
	1297	177031	36	Functional	-1	4	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	1297	177031	36	Functional	-1	4	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	CHEMBL444589	177031	36	Functional	-1	4	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	CHEMBL444589	177031	36	Functional	-1	4	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	211	3	4	4	0.2	NC(C(=O)O)c1ccc(C(=O)O)c(O)c1	None
	162265	209053	22	Functional	-239	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	CC(N)C(O)c1ccccc1	None
	4786	209053	22	Functional	-239	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	CC(N)C(O)c1ccccc1	None
	CHEMBL61006	209053	22	Functional	-239	44	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	151	2	2	2	1.1	CC(N)C(O)c1ccccc1	None
	139054390	211702	106	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	139054390	211702	106	3H-LY354740	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	139054390	211702	106	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	23327	211702	106	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	23327	211702	106	3H-LY354740	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	23327	211702	106	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	CHEMBL76232	211702	106	Functional	1	5	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	CHEMBL76232	211702	106	3H-LY354740	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	CHEMBL76232	211702	106	Functional	-1	5	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	N[C@H](CCC(=O)O)C(=O)O	None
	3337	213146	27	Functional	-1513	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)Cc1cccc(C(F)(F)F)c1	None
	65801	213146	27	Functional	-1513	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)Cc1cccc(C(F)(F)F)c1	None
	66264	213146	27	Functional	-1513	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)Cc1cccc(C(F)(F)F)c1	None
	91452	213146	27	Functional	-1513	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)Cc1cccc(C(F)(F)F)c1	None
	CHEMBL87493	213146	27	Functional	-1513	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)Cc1cccc(C(F)(F)F)c1	None
	DB00574	213146	27	Functional	-1513	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	231	4	1	1	3.2	CCNC(C)Cc1cccc(C(F)(F)F)c1	None
	11954224	222732	0	Functional	-141253	59	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	581	4	3	6	2.0	CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C	None
	6971132	222788	0	3H-LY341495	-2570	14	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	268	1	2	2	2.1	CN1CC(C=C2C1CC3=CNC4=CC=CC2=C34)C(=O)O	None
	None	222951	0	Functional	-2	7	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	None	222951	0	Functional	1	7	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	25137849	222958	0	Functional	-4	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	165	3	2	2	1.3	CC(C(C1=CC=CC=C1)O)NC	None
	71290	222958	0	Functional	-4	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	165	3	2	2	1.3	CC(C(C1=CC=CC=C1)O)NC	None
	None	223095	0	Functional	-1	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	153	3	3	3	-1.4	C(C(C(=O)O)N)S(=O)O	None
	None	223096	0	Functional	-1	39	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	169	3	3	4	-1.7	C(C(C(=O)O)N)S(=O)(=O)O	None
	None	223104	0	Functional	-13	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	149	2	1	2	1.2	CC(C(=O)C1=CC=CC=C1)N	None
	1576	223105	0	Functional	-16	40	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	163	3	1	2	1.5	CC(C(=O)C1=CC=CC=C1)NC	None
	177120	223115	0	3H-LY354740	-	1	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	169	3	4	3	-1.4	C(C(C(=O)O)N)P(=O)(O)O	None
	194385	223124	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	172	3	3	4	-1.1	C1=C(ONC1=O)CC(C(=O)O)N	None
	194385	223124	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	172	3	3	4	-1.1	C1=C(ONC1=O)CC(C(=O)O)N	None
	6604769	223141	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	145	2	3	3	-1.1	C1C(NC1C(=O)O)C(=O)O	None
	6604769	223141	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	145	2	3	3	-1.1	C1C(NC1C(=O)O)C(=O)O	None
	None	223142	0	Functional	1	3	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	245	3	3	4	0.2	CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N	None
	None	223142	0	Functional	-1	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	245	3	3	4	0.2	CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N	None
	None	223143	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	233	3	2	6	-0.1	CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N	None
	None	223143	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	233	3	2	6	-0.1	CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N	None
	None	223144	0	Functional	1	3	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	197	4	4	3	-0.6	CC(CCP(=O)(O)O)(C(=O)O)N	None
	None	223144	0	Functional	-1	3	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	197	4	4	3	-0.6	CC(CCP(=O)(O)O)(C(=O)O)N	None
	None	223179	0	Functional	-	1	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	396	2	0	4	4.7	CC(=O)C1(C(=C)CC2C1(CCC3C2CC(=C)C4=CC(=O)CCC34C)C)OC(=O)C	None
	None	223188	0	Functional	1	2	Human	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	250	3	3	4	-0.3	C(C1=C(C(=O)NO1)Br)C(C(=O)O)N	None
	None	223188	0	Functional	-1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	250	3	3	4	-0.3	C(C1=C(C(=O)NO1)Br)C(C(=O)O)N	None
	None	223269	0	Functional	1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	144	2	2	2	-0.7	CC(C(=O)NC)NC(=O)C	None
	None	223270	0	Functional	1	2	Rat	5.0	pKi	=	5	Binding	NoneNone	PDSP KiDatabase	161	5	3	3	-0.3	C(CC(C(=O)O)N)CC(=O)O	None
	1376	7109	55	3H-M-MPEP	91	2	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	221	2	3	3	0.6	OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O	None
	2071	7109	55	3H-M-MPEP	91	2	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	221	2	3	3	0.6	OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O	None
	CHEMBL313938	7109	55	3H-M-MPEP	91	2	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	221	2	3	3	0.6	OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O	None
	1310	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	3H-LY354740	-13	18	Rat	6.0	pKi	=	6.0	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1310	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	Functional	-13	18	Rat	5.9	pKi	=	5.9	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	None	222951	0	3H-LY354740	1	7	Rat	5.7	pKi	=	5.7	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	None	222951	0	Functional	1	7	Rat	5.7	pKi	=	5.7	Binding	NoneNone	PDSP KiDatabase	173	2	3	3	-0.3	C1CC(CC1C(=O)O)(C(=O)O)N	None
	None	223113	0	Functional	-5	3	Human	6.5	pKi	=	6.5	Binding	NoneNone	PDSP KiDatabase	203	4	4	4	-1.6	C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N	None
	None	223178	0	Functional	-	1	Human	5.5	pKi	=	5.5	Binding	NoneNone	PDSP KiDatabase	174	2	4	4	-1.8	C1C(NCC1(C(=O)O)N)C(=O)O	None
	1310	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	Functional	-22	18	Human	5.4	pKi	=	5.4	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	None	223113	0	3H-LY354740	3	3	Rat	7.2	pKi	=	7.2	Binding	NoneNone	PDSP KiDatabase	203	4	4	4	-1.6	C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N	None
	None	223114	0	3H-LY354740	-	1	Rat	7.2	pKi	=	7.2	Binding	NoneNone	PDSP KiDatabase	159	3	3	3	-0.9	C1C(C1C(=O)O)C(C(=O)O)N	None
	114827	223111	0	3H-LY341495	3	3	Rat	7.1	pKi	=	7.1	Binding	NoneNone	PDSP KiDatabase	185	2	3	3	-0.5	C1CC(C2C1C2C(=O)O)(C(=O)O)N	None
	114827	223111	0	3H-LY341495	-3	3	Human	7.1	pKi	=	7.1	Binding	NoneNone	PDSP KiDatabase	185	2	3	3	-0.5	C1CC(C2C1C2C(=O)O)(C(=O)O)N	None
	1310	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	1369	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	33032	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	44272391	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	88747398	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	CHEMBL575060	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	DB00142	9095	110	Functional	-13	18	Rat	5.1	pKi	=	5.1	Binding	NoneNone	PDSP KiDatabase	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	None
	114827	223111	0	3H-LY354740	3	3	Rat	8.1	pKi	=	8.1	Binding	NoneNone	PDSP KiDatabase	185	2	3	3	-0.5	C1CC(C2C1C2C(=O)O)(C(=O)O)N	None
	49822115	8927	21	None	-	1	Human	8.3	pKi	=	8.3	Binding	Homologous displacement assay.Homologous displacement assay.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	8947	8927	21	None	-	1	Human	8.3	pKi	=	8.3	Binding	Homologous displacement assay.Homologous displacement assay.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	CHEMBL3947764	8927	21	None	-	1	Human	8.3	pKi	=	8.3	Binding	Homologous displacement assay.Homologous displacement assay.	Guide to Pharmacology	414	5	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F	26589404
	49836087	7847	0	None	-	1	Human	6.0	pKi	=	6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	6222	7847	0	None	-	1	Human	6.0	pKi	=	6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	CHEMBL1630805	7847	0	None	-	1	Human	6.0	pKi	=	6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	328	2	2	4	3.3	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl	21105727
	49858118	7894	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	6224	7894	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	CHEMBL1630807	7894	0	None	-	1	Human	6.1	pKi	=	6.1	Binding	UnclassifiedUnclassified	Guide to Pharmacology	324	3	2	5	2.7	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC	21105727
	49858117	7875	4	None	-	1	Human	6.2	pKi	=	6.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	6223	7875	4	None	-	1	Human	6.2	pKi	=	6.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	CHEMBL1630806	7875	4	None	-	1	Human	6.2	pKi	=	6.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	308	2	2	4	3.0	O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C	21105727
	11310142	9200	19	None	1	2	Human	6.8	pKi	=	6.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	26341392
	11614	9200	19	None	1	2	Human	6.8	pKi	=	6.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	26341392
	CHEMBL192051	9200	19	None	1	2	Human	6.8	pKi	=	6.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	2	3	3	-0.2	C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O	26341392
	11158623	10124	11	None	-8	2	Human	7.3	pKi	=	7.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6226	10124	11	None	-8	2	Human	7.3	pKi	=	7.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	CHEMBL1629855	10124	11	None	-8	2	Human	7.3	pKi	=	7.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	49765871	8926	45	None	-	1	Human	7.8	pKi	=	7.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	6317	8926	45	None	-	1	Human	7.8	pKi	=	7.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	CHEMBL2179319	8926	45	None	-	1	Human	7.8	pKi	=	7.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	400	4	0	4	5.1	FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F	23072213
	11158623	10124	11	None	8	2	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6226	10124	11	None	8	2	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	CHEMBL1629855	10124	11	None	8	2	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	423	2	1	3	6.2	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C	22091727
	6325	10131	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	474	3	2	4	5.4	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O	21470207
	73755206	10131	0	None	-	1	Rat	8.3	pKi	=	8.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	474	3	2	4	5.4	O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O	21470207
	6324	10126	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	73755205	10126	0	None	-	1	Rat	8.6	pKi	=	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	512	2	1	6	4.5	FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F	21470207
	1373	9253	51	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	139055582	9253	51	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	446355	9253	51	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	CHEMBL257626	9253	51	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	DB04256	9253	51	None	-6	5	Human	3.8	pKi	None	3.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	10530814
	104766	6822	42	None	-11	11	Human	4.2	pKi	None	4.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10530814
	1365	6822	42	None	-11	11	Human	4.2	pKi	None	4.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10530814
	CHEMBL34453	6822	42	None	-11	11	Human	4.2	pKi	None	4.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10530814
	1400	8320	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	10884552
	1400	8320	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	9504391
	5311079	8320	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	10884552
	5311079	8320	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	9504391
	CHEMBL1450466	8320	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	10884552
	CHEMBL1450466	8320	0	None	-7	2	Rat	4.5	pKi	None	4.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	175	5	3	3	0.0	CC[C@@](C(=O)O)(CCC(=O)O)N	9504391
	1373	9253	51	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	139055582	9253	51	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	446355	9253	51	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	CHEMBL257626	9253	51	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	DB04256	9253	51	None	6	5	Rat	4.6	pKi	None	4.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	209	3	3	3	0.6	OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C	9504391
	1374	8862	35	None	-12	2	Rat	4.8	pKi	None	4.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	9504391
	5311455	8862	35	None	-12	2	Rat	4.8	pKi	None	4.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	9504391
	CHEMBL39372	8862	35	None	-12	2	Rat	4.8	pKi	None	4.8	Binding	UnclassifiedUnclassified	Guide to Pharmacology	211	3	4	4	0.2	N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O	9504391
	1310	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	1369	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	33032	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	44272391	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	88747398	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	CHEMBL575060	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	DB00142	9095	110	None	-22	18	Human	4.9	pKi	None	4.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10530814
	1392	6861	48	None	-1	2	Human	5.0	pKi	None	5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10530814
	5310984	6861	48	None	-1	2	Human	5.0	pKi	None	5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10530814
	CHEMBL40086	6861	48	None	-1	2	Human	5.0	pKi	None	5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	174	2	4	4	-1.8	OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O	10530814
	104766	6822	42	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10884552
	104766	6822	42	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	9504391
	1365	6822	42	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10884552
	1365	6822	42	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	9504391
	CHEMBL34453	6822	42	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	10884552
	CHEMBL34453	6822	42	None	-3	11	Rat	5.2	pKi	None	5.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	173	2	3	3	-0.3	OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O	9504391
	1398	7153	0	None	7	2	Rat	5.3	pKi	None	5.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	4	4	4	-1.1	OC(=O)C(COP(=O)(O)O)(N)C	9504391
	3964633	7153	0	None	7	2	Rat	5.3	pKi	None	5.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	4	4	4	-1.1	OC(=O)C(COP(=O)(O)O)(N)C	9504391
	CHEMBL1437137	7153	0	None	7	2	Rat	5.3	pKi	None	5.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	199	4	4	4	-1.1	OC(=O)C(COP(=O)(O)O)(N)C	9504391
	1310	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	1310	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	1369	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	1369	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	33032	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	33032	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	44272391	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	44272391	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	88747398	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	88747398	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	CHEMBL575060	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	CHEMBL575060	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	DB00142	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	10652549
	DB00142	9095	110	None	-13	18	Rat	5.7	pKi	None	5.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	147	4	3	3	-0.7	OC(=O)CC[C@@H](C(=O)O)N	8022410
	1368	9070	37	None	-3	11	Human	6.3	pKi	None	6.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10530814
	5310956	9070	37	None	-3	11	Human	6.3	pKi	None	6.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10530814
	CHEMBL280563	9070	37	None	-3	11	Human	6.3	pKi	None	6.3	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10530814
	1377	8122	26	None	-2	6	Human	6.5	pKi	None	6.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10530814
	5310979	8122	26	None	-2	6	Human	6.5	pKi	None	6.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10530814
	CHEMBL284193	8122	26	None	-2	6	Human	6.5	pKi	None	6.5	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10530814
	1368	9070	37	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10884552
	1368	9070	37	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	9504391
	5310956	9070	37	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10884552
	5310956	9070	37	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	9504391
	CHEMBL280563	9070	37	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	10884552
	CHEMBL280563	9070	37	None	1	11	Rat	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	159	3	3	3	-0.9	N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O	9504391
	1393	8321	64	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	1396	8321	64	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	213056	8321	64	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	CHEMBL8759	8321	64	None	-2	6	Human	6.9	pKi	None	6.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10530814
	1377	8122	26	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10884552
	1377	8122	26	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	9504391
	5310979	8122	26	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10884552
	5310979	8122	26	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	9504391
	CHEMBL284193	8122	26	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	10884552
	CHEMBL284193	8122	26	None	-1	6	Rat	7.0	pKi	None	7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	203	4	4	4	-1.6	N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O	9504391
	1393	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1393	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	1396	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	1396	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	213056	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	213056	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	CHEMBL8759	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	10884552
	CHEMBL8759	8321	64	None	1	6	Rat	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	185	2	3	3	-0.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O	9504391
	10197984	9199	44	None	2	5	Human	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10090786
	1394	9199	44	None	2	5	Human	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10090786
	CHEMBL275079	9199	44	None	2	5	Human	7.9	pKi	None	7.9	Binding	UnclassifiedUnclassified	Guide to Pharmacology	187	2	3	4	-1.5	OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O	10090786
	1378	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	1378	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	1399	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	1399	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	9819927	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	9819927	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	CHEMBL432038	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10884552
	CHEMBL432038	9195	54	None	-1	10	Rat	8.4	pKi	None	8.4	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	9504391
	1378	9195	54	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	1399	9195	54	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	9819927	9195	54	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	CHEMBL432038	9195	54	None	-2	10	Human	8.6	pKi	None	8.6	Binding	UnclassifiedUnclassified	Guide to Pharmacology	353	5	3	4	2.8	OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N	10530814
	1397	9307	15	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	14975669
	1397	9307	15	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	15317467
	9886034	9307	15	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	14975669
	9886034	9307	15	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	15317467
	CHEMBL186453	9307	15	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	14975669
	CHEMBL186453	9307	15	None	-1	5	Rat	8.7	pKi	None	8.7	Binding	UnclassifiedUnclassified	Guide to Pharmacology	377	5	3	4	2.1	OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O	15317467
	1395	9306	15	None	2	2	Rat	9.2	pKi	None	9.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	11123999
	9837317	9306	15	None	2	2	Rat	9.2	pKi	None	9.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	11123999
	CHEMBL121053	9306	15	None	2	2	Rat	9.2	pKi	None	9.2	Binding	UnclassifiedUnclassified	Guide to Pharmacology	217	2	3	4	-1.2	O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O	11123999

Join us

Cite us

Main reference

Ligand source activities (1 row/activity)