PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30401677-6	2019	Cell-based studies indicated that PARP1 interacted directly with STAT3 and caused STAT3 poly(ADP-ribosyl)ation.	ribosyl)	97-105	poly(ADP-ribose) polymerase 1	Homo sapiens	34-39	
17891139-3	2007	Here, we identify the major poly(ADP-ribosyl)ated sites of p53 by PARP-1 and find that PARP-1-mediated poly(ADP-ribosyl)ation blocks the interaction between p53 and the nuclear export receptor Crm1, resulting in nuclear accumulation of p53.	ribosyl)	37-45	poly(ADP-ribose) polymerase 1	Homo sapiens	66-72	
17891139-3	2007	Here, we identify the major poly(ADP-ribosyl)ated sites of p53 by PARP-1 and find that PARP-1-mediated poly(ADP-ribosyl)ation blocks the interaction between p53 and the nuclear export receptor Crm1, resulting in nuclear accumulation of p53.	ribosyl)	37-45	poly(ADP-ribose) polymerase 1	Homo sapiens	87-93