PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27023330-6	2016	Like SIRT1, the nicotinamide inhibition of SIRT5 double mutant (Y102A/R105I) exhibited the mixed non-competitive behavior.	Niacinamide	16-28	sirtuin 5	Homo sapiens	43-48	
20060508-3	2010	SIRT3 and SIRT5 are NAD(+)-dependent deacetylases that remove acetyl groups from acetyllysine-modified proteins and yield 2"-O-acetyl-ADP-ribose and nicotinamide.	Niacinamide	149-161	sirtuin 5	Homo sapiens	10-15	
23028781-0	2012	Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition.	Niacinamide	64-76	sirtuin 5	Homo sapiens	0-5	
23028781-5	2012	Using this assay, we show that the deacetylation activity of human Sirt5 features an unusual insensitivity to nicotinamide inhibition.	Niacinamide	110-122	sirtuin 5	Homo sapiens	67-72	
23028781-7	2012	Structure comparison and mutagenesis identify an Arg neighboring to the Sirt5 nicotinamide binding pocket as a mediator of nicotinamide resistance, and statistical sequence analyses along with testing further Sirtuins reveal a network of coevolved residues likely defining a nicotinamide-insensitive Sirtuin deacetylase family.	Niacinamide	78-90	sirtuin 5	Homo sapiens	72-77	
23028781-7	2012	Structure comparison and mutagenesis identify an Arg neighboring to the Sirt5 nicotinamide binding pocket as a mediator of nicotinamide resistance, and statistical sequence analyses along with testing further Sirtuins reveal a network of coevolved residues likely defining a nicotinamide-insensitive Sirtuin deacetylase family.	Niacinamide	123-135	sirtuin 5	Homo sapiens	72-77	
23028781-7	2012	Structure comparison and mutagenesis identify an Arg neighboring to the Sirt5 nicotinamide binding pocket as a mediator of nicotinamide resistance, and statistical sequence analyses along with testing further Sirtuins reveal a network of coevolved residues likely defining a nicotinamide-insensitive Sirtuin deacetylase family.	Niacinamide	123-135	sirtuin 5	Homo sapiens	72-77	
23028781-8	2012	The same Arg was recently reported to render Sirt5 a preferential desuccinylase, and we find that this Sirt5 activity is highly sensitive to nicotinamide inhibition.	Niacinamide	141-153	sirtuin 5	Homo sapiens	45-50	
23028781-8	2012	The same Arg was recently reported to render Sirt5 a preferential desuccinylase, and we find that this Sirt5 activity is highly sensitive to nicotinamide inhibition.	Niacinamide	141-153	sirtuin 5	Homo sapiens	103-108	
23028781-9	2012	Analysis of Sirt5 structures and activity data suggest that an Arg/succinate interaction is the molecular basis of the differential nicotinamide sensitivities of the two Sirt5 activities.	Niacinamide	132-144	sirtuin 5	Homo sapiens	12-17	
23028781-9	2012	Analysis of Sirt5 structures and activity data suggest that an Arg/succinate interaction is the molecular basis of the differential nicotinamide sensitivities of the two Sirt5 activities.	Niacinamide	132-144	sirtuin 5	Homo sapiens	170-175