PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16388603-4	2006	In this study, Sir2-catalyzed reactions are shown to transfer an 18O label from the peptide acetyl group to the ribose 1"-position of OAADPr, providing direct evidence for the formation of a covalent alpha-1"-O-alkylamidate, whose existence is further supported by the observed methanolysis of the alpha-1"-O-alkylamidate intermediate to yield beta-1"-O-methyl-ADP-ribose in a Sir2 histidine-to-alanine mutant.	Ribose	112-118	sirtuin 1	Homo sapiens	15-19	
35566069-4	2022	It adopts a novel mechanism to promote SIRT1 activity by covalently bonding to the anomeric C1" carbon of the ribose ring in OAADPr.	Ribose	110-116	sirtuin 1	Homo sapiens	39-44	
35566069-6	2022	The longer distance between the anomeric C1" carbon of the ribose ring in OAADPr and Arg274 of SIRT1 (a conserved residue among sirtuins) than that between the anomeric C1" carbon in OAADPr and the Arg of SIRT2, SIRT3, SIRT5, and SIRT6, should be responsible for the high selectivity of CWR for SIRT1.	Ribose	59-65	sirtuin 1	Homo sapiens	95-100	
35566069-6	2022	The longer distance between the anomeric C1" carbon of the ribose ring in OAADPr and Arg274 of SIRT1 (a conserved residue among sirtuins) than that between the anomeric C1" carbon in OAADPr and the Arg of SIRT2, SIRT3, SIRT5, and SIRT6, should be responsible for the high selectivity of CWR for SIRT1.	Ribose	59-65	sirtuin 1	Homo sapiens	295-300	
16388603-4	2006	In this study, Sir2-catalyzed reactions are shown to transfer an 18O label from the peptide acetyl group to the ribose 1"-position of OAADPr, providing direct evidence for the formation of a covalent alpha-1"-O-alkylamidate, whose existence is further supported by the observed methanolysis of the alpha-1"-O-alkylamidate intermediate to yield beta-1"-O-methyl-ADP-ribose in a Sir2 histidine-to-alanine mutant.	Ribose	112-118	sirtuin 1	Homo sapiens	377-381	
33873776-5	2004	A second group of proteins unrelated to those above, the sirtuins (Sir2) and poly ADP-ribose polymerases (PARPs), cleave NAD and transfer the ADP-ribose group to acetyl groups and proteins, respectively.	Ribose	86-92	sirtuin 1	Homo sapiens	67-71