PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7518560-2	1994	Results of co-immunoprecipitation experiments suggest that phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR.	phosphotyrosines y-1068	59-82	growth factor receptor bound protein 2	Homo sapiens	117-121	
7518560-2	1994	Results of co-immunoprecipitation experiments suggest that phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR.	phosphotyrosines y-1068	59-82	epidermal growth factor receptor	Homo sapiens	129-133	
7518560-2	1994	Results of co-immunoprecipitation experiments suggest that phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR.	Y-1173	87-93	growth factor receptor bound protein 2	Homo sapiens	117-121	
7518560-2	1994	Results of co-immunoprecipitation experiments suggest that phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR.	Y-1173	87-93	epidermal growth factor receptor	Homo sapiens	129-133	
7518560-3	1994	Competition experiments with synthetic phosphopeptides corresponding to known autophosphorylation sites on the EGFR demonstrated that phosphopeptides containing Y-1068, and to a lesser extent Y-1086, were able to inhibit the binding of Grb2 to the EGFR, while a Y-1173 peptide did not.	y-1068	161-167	epidermal growth factor receptor	Homo sapiens	111-115	
7518560-3	1994	Competition experiments with synthetic phosphopeptides corresponding to known autophosphorylation sites on the EGFR demonstrated that phosphopeptides containing Y-1068, and to a lesser extent Y-1086, were able to inhibit the binding of Grb2 to the EGFR, while a Y-1173 peptide did not.	y-1068	161-167	growth factor receptor bound protein 2	Homo sapiens	236-240	
7518560-3	1994	Competition experiments with synthetic phosphopeptides corresponding to known autophosphorylation sites on the EGFR demonstrated that phosphopeptides containing Y-1068, and to a lesser extent Y-1086, were able to inhibit the binding of Grb2 to the EGFR, while a Y-1173 peptide did not.	y-1068	161-167	epidermal growth factor receptor	Homo sapiens	248-252	
7518560-4	1994	These findings were confirmed by using a dephosphorylation protection assay and by measuring the dissociation constants of Grb2"s SH2 domain to tyrosine-phosphorylated peptides, using real-time biospecific interaction analysis (BIAcore).	Tyrosine	144-152	growth factor receptor bound protein 2	Homo sapiens	123-127	
7518560-6	1994	Since Grb2 also binds Shc after EGF stimulation, we investigated whether Y-1173 is a binding site for the SH2 domain of Shc on the EGFR.	Y-1173	73-79	SHC adaptor protein 1	Homo sapiens	120-123	
7518560-6	1994	Since Grb2 also binds Shc after EGF stimulation, we investigated whether Y-1173 is a binding site for the SH2 domain of Shc on the EGFR.	Y-1173	73-79	epidermal growth factor receptor	Homo sapiens	131-135	
7518560-9	1994	These analyses reveal a hierarchy of interactions between Grb2 and Shc with the EGFR and indicate that Grb2 can bind the tyrosine-phosphorylated EGFR directly, as well as indirectly via Shc.	Tyrosine	121-129	growth factor receptor bound protein 2	Homo sapiens	103-107	
7518560-9	1994	These analyses reveal a hierarchy of interactions between Grb2 and Shc with the EGFR and indicate that Grb2 can bind the tyrosine-phosphorylated EGFR directly, as well as indirectly via Shc.	Tyrosine	121-129	epidermal growth factor receptor	Homo sapiens	145-149	
7518560-9	1994	These analyses reveal a hierarchy of interactions between Grb2 and Shc with the EGFR and indicate that Grb2 can bind the tyrosine-phosphorylated EGFR directly, as well as indirectly via Shc.	Tyrosine	121-129	SHC adaptor protein 1	Homo sapiens	186-189