PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33015038-4	2020	Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity.	NAD	45-78	sirtuin 3	Homo sapiens	0-9	
33015038-4	2020	Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity.	NAD	45-78	sirtuin 3	Homo sapiens	11-16	
33015038-4	2020	Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity.	NAD	80-83	sirtuin 3	Homo sapiens	0-9	
33015038-4	2020	Sirtuin 3 (SIRT3) is the major mitochondrial nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, which deacetylates two critical lysine residues (lysine 68 and lysine 122) on SOD2 and promotes its antioxidative activity.	NAD	80-83	sirtuin 3	Homo sapiens	11-16	
33015038-7	2020	Mechanistically, caffeine bound to SIRT3 with high affinity (K D = 6.858 x 10-7 M); the binding affinity between SIRT3 and its substrate acetylated p53 was also 9.03 (without NAD+) or 6.87 (with NAD+) times higher in the presence of caffeine.	NAD	195-199	sirtuin 3	Homo sapiens	113-118