PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17884634-4	2007	We further demonstrate that the effects of P-Ser are mediated by the group III metabotropic glutamate receptor 4 (mGluR4).	Phosphoserine	43-48	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	114-120	
19621591-5	2009	The rank order of the agonist potency for the stable human mGluR4 cell line was L-(+)-2-Amino-4-phosphonobutyric acid (L-AP4) > L-Serine-O-phosphate (L-SOP) > L-Glu, and of the antagonist potency was (RS)-alpha-Methylserine-O-phosphate (MSOP) > (RS)-alpha-Methyl-4-phosphonophenylglycine (MPPG).	Phosphoserine	131-151	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	59-65	
19621591-5	2009	The rank order of the agonist potency for the stable human mGluR4 cell line was L-(+)-2-Amino-4-phosphonobutyric acid (L-AP4) > L-Serine-O-phosphate (L-SOP) > L-Glu, and of the antagonist potency was (RS)-alpha-Methylserine-O-phosphate (MSOP) > (RS)-alpha-Methyl-4-phosphonophenylglycine (MPPG).	Phosphoserine	153-158	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	59-65	
25519912-3	2015	In contrast, mGluR4 has in common with other group III mGluR that it is activated with higher potency and efficacy by L-SOP.	Phosphoserine	118-123	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	13-19	
25519912-5	2015	Enhanced versions of the evolutionary trace (ET) algorithm were used to identify residues that when swapped between mGluR1 and mGluR4 increased the potency of L-SOP inhibition relative to the potency of L-glutamate activation in mGluR1 mutants and others that diminished the potency/efficacy of L-SOP for mGluR4 mutants.	Phosphoserine	159-164	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	127-133	
25519912-5	2015	Enhanced versions of the evolutionary trace (ET) algorithm were used to identify residues that when swapped between mGluR1 and mGluR4 increased the potency of L-SOP inhibition relative to the potency of L-glutamate activation in mGluR1 mutants and others that diminished the potency/efficacy of L-SOP for mGluR4 mutants.	Phosphoserine	159-164	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	305-311	
25519912-5	2015	Enhanced versions of the evolutionary trace (ET) algorithm were used to identify residues that when swapped between mGluR1 and mGluR4 increased the potency of L-SOP inhibition relative to the potency of L-glutamate activation in mGluR1 mutants and others that diminished the potency/efficacy of L-SOP for mGluR4 mutants.	Phosphoserine	295-300	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	127-133	
25193666-8	2014	Molecular docking studies suggested that residue 74 corresponding to lysine in mGluR4 and asparagine in mGluR7 might play a key role, and, indeed, mutagenesis experiments demonstrated that mutating this residue to lysine in mGluR7 enhances the potency of L-SOP.	Phosphoserine	255-260	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	79-85	
17884634-5	2007	siRNA-mediated knockdown of mGluR4 abolished the effects of P-Ser and increased neurosphere proliferation, at least in part through upregulation of mTOR pathway activity.	Phosphoserine	60-65	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	28-34	
10559233-6	1999	Based on these experimental findings, together with information obtained from the model in which the glutamate analog L-serine O-phosphate (L-SOP) was "docked" into the binding pocket, we suggest that the hydroxyl groups on the side chains of Ser(159) and Thr(182) of mGluR4 form hydrogen bonds with the alpha-carboxyl and alpha-amino groups on L-SOP, respectively, whereas Arg(78) forms an electrostatic interaction with the acidic side chains of L-SOP or glutamate.	Phosphoserine	118-138	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	268-274	
10559233-6	1999	Based on these experimental findings, together with information obtained from the model in which the glutamate analog L-serine O-phosphate (L-SOP) was "docked" into the binding pocket, we suggest that the hydroxyl groups on the side chains of Ser(159) and Thr(182) of mGluR4 form hydrogen bonds with the alpha-carboxyl and alpha-amino groups on L-SOP, respectively, whereas Arg(78) forms an electrostatic interaction with the acidic side chains of L-SOP or glutamate.	Phosphoserine	140-145	glutamate receptor, ionotropic, AMPA4 (alpha 4)	Mus musculus	268-274