PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15207836-3	2004	Assays were performed in purified brain cell nuclei to determine Parp activity by incorporation of radiolabeled ADP-ribose moieties from nicotinamide adenine dinucleotide (NAD+) into nuclear proteins.	Ribose	116-122	poly (ADP-ribose) polymerase 1	Rattus norvegicus	65-69	
17766683-1	2007	Poly(ADP-ribose)polymerases (PARP-1 and -2) are activated by DNA strand breaks to synthesize protein-bound ADP-ribose polymers from NAD+.	Ribose	9-15	poly (ADP-ribose) polymerase 1	Rattus norvegicus	29-42	
15465278-3	2004	Upon activation PARP-1 uses NAD(+) as a substrate to catalyze the transfer of ADP-ribose subunits to a host of nuclear proteins.	Ribose	82-88	poly (ADP-ribose) polymerase 1	Rattus norvegicus	16-22	
14994994-1	2004	DNA damage-activated homodimer of PARP-1 binds to single-strand breaks and catalyzes the synthesis and transfer of negatively charged ADP-ribose polymers to nuclear protein acceptors, including itself.	Ribose	138-144	poly (ADP-ribose) polymerase 1	Rattus norvegicus	34-40	
12650200-6	2001	Moreover, PARP-1 can control its protein and DNA interactions by catalyzing its automodification with poly(ADP-ribose) molecules that can include up to 200 ADP-ribose residues and several branching points; by these polymers, PARP-1 may nocovalently interact with other proteins and alter their functions.	Ribose	111-117	poly (ADP-ribose) polymerase 1	Rattus norvegicus	10-16	
12650200-6	2001	Moreover, PARP-1 can control its protein and DNA interactions by catalyzing its automodification with poly(ADP-ribose) molecules that can include up to 200 ADP-ribose residues and several branching points; by these polymers, PARP-1 may nocovalently interact with other proteins and alter their functions.	Ribose	111-117	poly (ADP-ribose) polymerase 1	Rattus norvegicus	225-231