PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8626373-2	1996	Because paxillin is a tyrosine-phosphorylated protein that may play a role in regulating cell morphology, we examined its expression in neuronal cells and how its tyrosine phosphorylation is related to neurite outgrowth.	Tyrosine	22-30	paxillin	Homo sapiens	8-16	
8626373-2	1996	Because paxillin is a tyrosine-phosphorylated protein that may play a role in regulating cell morphology, we examined its expression in neuronal cells and how its tyrosine phosphorylation is related to neurite outgrowth.	Tyrosine	163-171	paxillin	Homo sapiens	8-16	
8626373-5	1996	Furthermore, paxillin was tyrosine-phosphorylated in SH-SY5Y cells upon adhesion to laminin.	Tyrosine	26-34	paxillin	Homo sapiens	13-21	
8626373-8	1996	In contrast, cytochalasin D eliminated neurite outgrowth, cell spreading, and the tyrosine phosphorylation of paxillin and focal adhesion kinase.	Cytochalasin D	13-27	paxillin	Homo sapiens	110-118	
8626373-8	1996	In contrast, cytochalasin D eliminated neurite outgrowth, cell spreading, and the tyrosine phosphorylation of paxillin and focal adhesion kinase.	Tyrosine	82-90	paxillin	Homo sapiens	110-118	
8626373-9	1996	These results show that paxillin is tyrosine-phosphorylated upon integrin ligand binding in neuronal cells.	Tyrosine	36-44	paxillin	Homo sapiens	24-32