PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29907568-2	2018	ARH3 degrades poly(ADP-ribose) to protect cells from poly(ADP-ribose)-dependent cell death, reverses serine mono(ADP-ribosyl)ation, and hydrolyzes O-acetyl-ADP-ribose, a product of Sirtuin-catalyzed histone deacetylation.	Ribose	23-29	ADP-ribosylserine hydrolase	Homo sapiens	0-4	
34321462-5	2021	Structural analysis of ARH3 in complex with dimeric ADP-ribose as well as an ADP-ribosylated peptide reveal the molecular basis for the hydrolysis of linear and terminal ADP-ribose linkages.	Ribose	174-180	ADP-ribosylserine hydrolase	Homo sapiens	23-27	
30472116-7	2018	Despite this apparent similarity, we elucidate the structural basis for the selective inhibition of ARH3 by the ADP-ribose analogues ADP-HPD and arginine-ADP-ribose.	Ribose	116-122	ADP-ribosylserine hydrolase	Homo sapiens	100-104	
16278211-5	2006	We report here the identification of an ARH1-like protein, termed poly(ADP-ribose) hydrolase or ARH3, which exhibited PARG activity, generating ADP-ribose from poly-(ADP-ribose), but did not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds.	Ribose	75-81	ADP-ribosylserine hydrolase	Homo sapiens	96-100