PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2436039-3	1987	The reduction of in vitro enzymatic activity correlated with a vanadate-induced increase in in vivo phosphorylation of pp60c-src at the major site of tyrosine phosphorylation in the carboxyl-terminal half of the molecule and at serine in the amino-terminal half of the molecule.	Vanadates	63-71	SRC proto-oncogene, non-receptor tyrosine kinase	Gallus gallus	119-128	
2436039-5	1987	4:1471-1477, 1985) suggest that vanadate may enhance a cellular regulatory mechanism that inhibits the activity of pp60c-src in normal cells.	Vanadates	32-40	SRC proto-oncogene, non-receptor tyrosine kinase	Gallus gallus	115-124	
2436039-9	1987	Assuming that pp60c-src is inhibited intracellularly by vanadate, either another tyrosine kinase is stimulated by vanadate (e.g., a growth factor receptor) or the 36-kilodalton phosphoprotein in normal cells is no longer rapidly dephosphorylated by a tyrosine phosphatase in the presence of vanadate.	Vanadates	56-64	SRC proto-oncogene, non-receptor tyrosine kinase	Gallus gallus	14-23