PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25561730-5	2015	The molecular modeling study showed that Ile(196) at transmembrane helix 2, Met(233) at ECL1, and Asn(302) at ECL2 of GLP1R have contacts with His(1) and Thr(7) of GLP-1.	Isoleucine	41-44	glucagon like peptide 1 receptor	Homo sapiens	118-123	
22105074-4	2012	Here, using chimeric and point-mutated GLP1R/GIPR, we determined that evolutionarily conserved amino acid residues such as Ile(196) at transmembrane helix 2, Leu(232) and Met(233) at extracellular loop 1, and Asn(302) at extracellular loop 2 of GLP1R are responsible for interaction with ligand and receptor activation.	Isoleucine	123-126	glucagon like peptide 1 receptor	Homo sapiens	39-44	
20799012-5	2010	A mutated GIP peptide in which Tyr(1), Ile(7), Asp(15), and His(18) were replaced by His, Thr, Glu, and Ala, respectively, was able to activate both GLP1R and GIPR with moderate potency.	Isoleucine	39-42	glucagon like peptide 1 receptor	Homo sapiens	149-154	
20799012-8	2010	These results suggest that Tyr/His(1) and Ile/Thr(7) of GIP/GLP-1 peptides confer differential ligand selectivity toward GIPR and GLP1R.	Isoleucine	42-45	glucagon like peptide 1 receptor	Homo sapiens	130-135