PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9648724-0	1998	Phosphorylation of p130Cas by angiotensin II is dependent on c-Src, intracellular Ca2+, and protein kinase C. p130Cas is a signaling molecule that was initially found to be tyrosine-phosphorylated in v-Crk and v-Src transformed cells.	Tyrosine	173-181	angiotensinogen	Homo sapiens	30-44	
9648724-1	1998	We characterized the regulation of p130Cas tyrosine phosphorylation in vascular smooth muscle cells by angiotensin II (Ang II).	Tyrosine	43-51	angiotensinogen	Homo sapiens	103-117	
9648724-1	1998	We characterized the regulation of p130Cas tyrosine phosphorylation in vascular smooth muscle cells by angiotensin II (Ang II).	Tyrosine	43-51	angiotensinogen	Homo sapiens	119-125	
9648724-3	1998	The Ang II-induced tyrosine phosphorylation of p130Cas was also dependent on an active Src family tyrosine kinase, since it could be blocked by the Src kinase inhibitors geldanamycin and PP1.	Tyrosine	19-27	angiotensinogen	Homo sapiens	4-10	
9648724-7	1998	Inhibition of protein kinase C by either calphostin C or phorbol 12-myristate 13-acetate downregulation inhibited the Ang II-induced tyrosine phosphorylation of p130Cas.	Tyrosine	133-141	angiotensinogen	Homo sapiens	118-124	
9648724-8	1998	These results are the first to demonstrate that the tyrosine phosphorylation of p130Cas by Ang II is transduced by the Src, intracellular Ca2+, protein kinase C signaling pathway.	Tyrosine	52-60	angiotensinogen	Homo sapiens	91-97