PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
30789810-0	2020	QSAR studies on the human sirtuin 2 inhibition by non-covalent 7,5,2-anilinobenzamide derivatives.	7,5,2-anilinobenzamide	63-85	sirtuin 2	Homo sapiens	26-35
33789098-4	2021	SIRT2 complexes with BRCA1-BARD1 and deacetylates conserved lysines in the BARD1 RING domain, interfacing BRCA1, which promotes BRCA1-BARD1 heterodimerization and consequently BRCA1-BARD1 stability, nuclear retention, and localization to DNA damage sites, thus contributing to efficient HR.	Lysine	60-67	sirtuin 2	Homo sapiens	0-5
30789810-2	2020	Anilinobenzamide derivatives have been discussed as selective sirtuin 2 inhibitors and can be developed further.	2-(phenylamino)benzamide	0-16	sirtuin 2	Homo sapiens	62-71
34601098-1	2021	SIRT2, a Class III HDACs, aggravates cell damage and activates caspase-3 under oxygen-glucose deprivation/reoxygenation and glucose (OGD/R) conditions.	Oxygen	79-85	sirtuin 2	Homo sapiens	0-5
34856334-5	2022	Silent information regulator 2 or SIR2 or more commonly known as sirtuins are NAD+ dependent histone deacetylase.	NAD	78-81	sirtuin 2	Homo sapiens	0-30
34856334-5	2022	Silent information regulator 2 or SIR2 or more commonly known as sirtuins are NAD+ dependent histone deacetylase.	NAD	78-81	sirtuin 2	Homo sapiens	34-38
34961760-0	2021	Histone lysine methacrylation is a dynamic post-translational modification regulated by HAT1 and SIRT2.	Lysine	8-14	sirtuin 2	Homo sapiens	97-102
34965411-5	2021	In parallel, downregulation of SIRT2 hyperacetylates the serine/threonine protein kinase AKT1 at Lys20 in a non-canonical way, activating DRP1 and metabolic reprogramming.	Serine	57-63	sirtuin 2	Homo sapiens	31-36
34695733-6	2021	It could be demonstrated that the stalled intermediate formed by the reaction of Sirt2-bound thiomyristoylated peptide and NAD+ has IC50 values below 200 pM.	thiomyristoylated	93-110	sirtuin 2	Homo sapiens	81-86
34695733-6	2021	It could be demonstrated that the stalled intermediate formed by the reaction of Sirt2-bound thiomyristoylated peptide and NAD+ has IC50 values below 200 pM.	Peptides	111-118	sirtuin 2	Homo sapiens	81-86
34695733-6	2021	It could be demonstrated that the stalled intermediate formed by the reaction of Sirt2-bound thiomyristoylated peptide and NAD+ has IC50 values below 200 pM.	NAD	123-127	sirtuin 2	Homo sapiens	81-86
34601098-1	2021	SIRT2, a Class III HDACs, aggravates cell damage and activates caspase-3 under oxygen-glucose deprivation/reoxygenation and glucose (OGD/R) conditions.	Glucose	124-131	sirtuin 2	Homo sapiens	0-5
34601098-4	2021	The lysine 312 residue (K312) was selected as the target site in ANXA1 because it is associated with SIRT2, and its mimic (K312Q) and silent (K312R) mutants were then established through site mutagenesis.	Lysine	4-10	sirtuin 2	Homo sapiens	101-106
34474091-0	2021	Pterostilbene attenuates RIPK3-dependent hepatocyte necroptosis in alcoholic liver disease via SIRT2-mediated NFATc4 deacetylation.	pterostilbene	0-13	sirtuin 2	Homo sapiens	95-100
34925016-3	2021	Sirtuin2 (Sirt2), a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, has been proved to be involved in the fibrosis and inflammation in the liver, kidney and heart.	NAD	20-53	sirtuin 2	Homo sapiens	0-8
34925016-3	2021	Sirtuin2 (Sirt2), a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, has been proved to be involved in the fibrosis and inflammation in the liver, kidney and heart.	NAD	20-53	sirtuin 2	Homo sapiens	10-15
34925016-3	2021	Sirtuin2 (Sirt2), a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, has been proved to be involved in the fibrosis and inflammation in the liver, kidney and heart.	NAD	55-58	sirtuin 2	Homo sapiens	0-8
34925016-3	2021	Sirtuin2 (Sirt2), a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, has been proved to be involved in the fibrosis and inflammation in the liver, kidney and heart.	NAD	55-58	sirtuin 2	Homo sapiens	10-15
34429771-5	2021	Sirtuin 2 (SIRT2), a primarily cytosolic nicotinamide adenine dinucleotide-dependent class III protein deacetylase, has been shown to catalyze the removal of acetyl groups from a wide range of proteins, including tubulin, ribonucleotide reductase regulatory subunit M2 and glucose-6-phosphate dehydrogenase.	NAD	41-74	sirtuin 2	Homo sapiens	0-9
34429771-5	2021	Sirtuin 2 (SIRT2), a primarily cytosolic nicotinamide adenine dinucleotide-dependent class III protein deacetylase, has been shown to catalyze the removal of acetyl groups from a wide range of proteins, including tubulin, ribonucleotide reductase regulatory subunit M2 and glucose-6-phosphate dehydrogenase.	NAD	41-74	sirtuin 2	Homo sapiens	11-16
34429771-6	2021	In addition, SIRT2 is also known to possess lysine fatty deacylation activity.	Lysine	44-50	sirtuin 2	Homo sapiens	13-18
34476599-7	2022	As for chemosensitivity, upregulation of SIRT2 increased relative cell viability in cisplatin-treated and paclitaxel-treated Ishikawa cells.	Cisplatin	84-93	sirtuin 2	Homo sapiens	41-46
34476599-7	2022	As for chemosensitivity, upregulation of SIRT2 increased relative cell viability in cisplatin-treated and paclitaxel-treated Ishikawa cells.	Paclitaxel	106-116	sirtuin 2	Homo sapiens	41-46
34618427-5	2021	Moreover, the site specifically incorporated lysine benzoylation within native full-length histone proteins revealed distinct dynamics of debenzoylation in the presence of debenzoylase sirtuin 2 (SIRT2).	Lysine	45-51	sirtuin 2	Homo sapiens	185-194
34618427-5	2021	Moreover, the site specifically incorporated lysine benzoylation within native full-length histone proteins revealed distinct dynamics of debenzoylation in the presence of debenzoylase sirtuin 2 (SIRT2).	Lysine	45-51	sirtuin 2	Homo sapiens	196-201
34382754-2	2021	Here, we developed a high-throughput screen to identify novel SIRT2 inhibitors using a fluorescent SIRT2 probe, 1-aminoanthracene (AMA).	1-aminoanthracene	112-129	sirtuin 2	Homo sapiens	62-67
34382754-2	2021	Here, we developed a high-throughput screen to identify novel SIRT2 inhibitors using a fluorescent SIRT2 probe, 1-aminoanthracene (AMA).	1-aminoanthracene	112-129	sirtuin 2	Homo sapiens	99-104
34382754-2	2021	Here, we developed a high-throughput screen to identify novel SIRT2 inhibitors using a fluorescent SIRT2 probe, 1-aminoanthracene (AMA).	1-aminoanthracene	131-134	sirtuin 2	Homo sapiens	62-67
34382754-2	2021	Here, we developed a high-throughput screen to identify novel SIRT2 inhibitors using a fluorescent SIRT2 probe, 1-aminoanthracene (AMA).	1-aminoanthracene	131-134	sirtuin 2	Homo sapiens	99-104
34382754-4	2021	We used this property of AMA to screen a library of known bioactive compounds for SIRT2 binding and discovered two known pharmaceutical compounds that bind SIRT2 with K d values in the low muM range, ascorbyl palmitate and pictilisib.	6-O-palmitoylascorbic acid	200-218	sirtuin 2	Homo sapiens	156-161
34382754-4	2021	We used this property of AMA to screen a library of known bioactive compounds for SIRT2 binding and discovered two known pharmaceutical compounds that bind SIRT2 with K d values in the low muM range, ascorbyl palmitate and pictilisib.	2-(1H-indazol-4-yl)-6-(4-methanesulfonylpiperazin-1-ylmethyl)-4-morpholin-4-ylthieno(3,2-d)pyrimidine	223-233	sirtuin 2	Homo sapiens	156-161
34382754-6	2021	While pictilisib has selectivity for SIRT2, ascorbyl palmitate also inhibits the enzymatic activities of SIRT1 and SIRT6.	2-(1H-indazol-4-yl)-6-(4-methanesulfonylpiperazin-1-ylmethyl)-4-morpholin-4-ylthieno(3,2-d)pyrimidine	6-16	sirtuin 2	Homo sapiens	37-42
34382754-7	2021	Finally, we show that ascorbyl palmitate inhibits SIRT2 deacetylase and defatty-acylase activities in cells, and SIRT2 inhibition by ascorbyl palmitate contributes to the cytotoxicity of the compound.	6-O-palmitoylascorbic acid	22-40	sirtuin 2	Homo sapiens	50-55
34382754-7	2021	Finally, we show that ascorbyl palmitate inhibits SIRT2 deacetylase and defatty-acylase activities in cells, and SIRT2 inhibition by ascorbyl palmitate contributes to the cytotoxicity of the compound.	6-O-palmitoylascorbic acid	133-151	sirtuin 2	Homo sapiens	113-118
34697541-7	2021	Moreover, SIRT2 was further proved to be a downstream target of miR-138.	mir-138	64-71	sirtuin 2	Homo sapiens	10-15
34642296-9	2021	High amounts of H2O2, however, rapidly carbonylated selectively SIRT2, SIRT6, and SIRT7, which were found to accumulate carbonylation-prone amino acids.	Hydrogen Peroxide	16-20	sirtuin 2	Homo sapiens	64-69
34712915-0	2021	Rapamycin recruits SIRT2 for FKBP12 deacetylation during mTOR activity modulation in innate immunity.	Sirolimus	0-9	sirtuin 2	Homo sapiens	19-24
34712915-7	2021	Rapamycin recruits SIRT2 with a high affinity for FKBP12 association and deacetylation.	Sirolimus	0-9	sirtuin 2	Homo sapiens	19-24
34712915-10	2021	In contrast, rapamycin strengthening FKBP12-mTOR association blocks mTOR antiviral activity by recruiting SIRT2 to deacetylate FKBP12.	Sirolimus	13-22	sirtuin 2	Homo sapiens	106-111
34474091-12	2021	In conclusion, PTS attenuated RIPK3-dependent hepatocyte necroptosis after ethanol exposure via SIRT2-mediated NFATc4 deacetylation.	Ethanol	75-82	sirtuin 2	Homo sapiens	96-101
34458803-1	2021	Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues.	Lysine	139-145	sirtuin 2	Homo sapiens	0-9
34108853-1	2021	As a type of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases, sirtuin 2 (SIRT2) is predominantly found in the cytoplasm of cells in the central nervous system (CNS), suggesting its potential role in neurological disorders.	NAD	13-46	sirtuin 2	Homo sapiens	78-87
34108853-1	2021	As a type of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases, sirtuin 2 (SIRT2) is predominantly found in the cytoplasm of cells in the central nervous system (CNS), suggesting its potential role in neurological disorders.	NAD	13-46	sirtuin 2	Homo sapiens	89-94
34108853-1	2021	As a type of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases, sirtuin 2 (SIRT2) is predominantly found in the cytoplasm of cells in the central nervous system (CNS), suggesting its potential role in neurological disorders.	NAD	48-51	sirtuin 2	Homo sapiens	78-87
34108853-1	2021	As a type of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases, sirtuin 2 (SIRT2) is predominantly found in the cytoplasm of cells in the central nervous system (CNS), suggesting its potential role in neurological disorders.	NAD	48-51	sirtuin 2	Homo sapiens	89-94
34068624-0	2021	Targeting SIRT2 Sensitizes Melanoma Cells to Cisplatin via an EGFR-Dependent Mechanism.	Cisplatin	45-54	sirtuin 2	Homo sapiens	10-15
34068624-4	2021	Increasing evidence suggests that sirtuin 2 (SIRT2) plays a key role in the response of melanoma cells to chemotherapeutics; thus, in the present study, we evaluated the impact of shRNA-mediated and pharmacological inhibition of SIRT2 on the sensitivity of melanoma cells to cisplatin, which is used in several regimens to treat melanoma patients.	Cisplatin	275-284	sirtuin 2	Homo sapiens	34-43
34068624-4	2021	Increasing evidence suggests that sirtuin 2 (SIRT2) plays a key role in the response of melanoma cells to chemotherapeutics; thus, in the present study, we evaluated the impact of shRNA-mediated and pharmacological inhibition of SIRT2 on the sensitivity of melanoma cells to cisplatin, which is used in several regimens to treat melanoma patients.	Cisplatin	275-284	sirtuin 2	Homo sapiens	45-50
34068624-5	2021	We found that cells with SIRT2 inhibition revealed increased sensitivity to cisplatin and exhibited increased accumulation of gamma-H2AX and reduced EGFR-AKT-RAF-ERK1/2 (epidermal growth factor receptor-protein B kinase-RAF kinase-extracellular signal-regulated kinase 1/2) pathway signaling compared to control cells.	Cisplatin	76-85	sirtuin 2	Homo sapiens	25-30
34068624-6	2021	Thus, our results show that sirtuin 2 inhibition increased the in vitro efficacy of cisplatin against melanoma cells.	Cisplatin	84-93	sirtuin 2	Homo sapiens	28-37
34458803-1	2021	Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues.	Lysine	139-145	sirtuin 2	Homo sapiens	11-16
35467856-10	2022	Two compounds, NDJ18 and NDJ85, were identified as potent and selective SIRT2 inhibitors, which validated the in silico protocol and opened up the possibility for generalization and broadening of its application.	ndj18	15-20	sirtuin 2	Homo sapiens	72-77
35467856-10	2022	Two compounds, NDJ18 and NDJ85, were identified as potent and selective SIRT2 inhibitors, which validated the in silico protocol and opened up the possibility for generalization and broadening of its application.	ndj85	25-30	sirtuin 2	Homo sapiens	72-77
35177983-0	2021	Decylubiquinone Inhibits Colorectal Cancer Growth Through Upregulating Sirtuin2.	2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone	0-15	sirtuin 2	Homo sapiens	71-79
35264593-0	2022	Quantitative proteomic analysis of the lysine acetylome reveals diverse SIRT2 substrates.	lysine acetylome	39-55	sirtuin 2	Homo sapiens	72-77
35264593-2	2022	While a number of substrates involved in these processes have been identified, the global landscape of the SIRT2 acetylome remains unclear.	acetylome	113-122	sirtuin 2	Homo sapiens	107-112
35264593-3	2022	Using a label-free quantitative proteomic approach following enrichment for acetylated peptides from SIRT2-depleted and SIRT2-overexpressing HCT116 human colorectal cancer cells, we identified a total of 2,846 unique acetylation sites from 1414 proteins.	Peptides	87-95	sirtuin 2	Homo sapiens	101-106
35264593-6	2022	Gene Ontology, KEGG, and MetaCore pathway analyses identified SIRT2 substrates involved in diverse pathways, including carbon metabolism, glycolysis, spliceosome, RNA transport, RNA binding, transcription, DNA damage response, the cell cycle, and colorectal cancer.	Carbon	119-125	sirtuin 2	Homo sapiens	62-67
35358824-0	2022	Hit evaluation results in 5-benzyl-1,3,4-thiadiazole-2-carboxamide based SIRT2-selective inhibitor with improved affinity and selectivity.	5-benzyl-1,3,4-thiadiazole-2-carboxamide	26-66	sirtuin 2	Homo sapiens	73-78
35358824-2	2022	The enzymatic activity of SIRT2 is dependent on nicotinamide adenine dinucleotide (NAD+) and SIRT2 regulates post-translational modifications that are responsible for deacetylation of lysine residues in histone and non-histone substrates.	NAD	48-81	sirtuin 2	Homo sapiens	26-31
35358824-2	2022	The enzymatic activity of SIRT2 is dependent on nicotinamide adenine dinucleotide (NAD+) and SIRT2 regulates post-translational modifications that are responsible for deacetylation of lysine residues in histone and non-histone substrates.	NAD	83-87	sirtuin 2	Homo sapiens	26-31
35358824-2	2022	The enzymatic activity of SIRT2 is dependent on nicotinamide adenine dinucleotide (NAD+) and SIRT2 regulates post-translational modifications that are responsible for deacetylation of lysine residues in histone and non-histone substrates.	Lysine	184-190	sirtuin 2	Homo sapiens	26-31
35358824-2	2022	The enzymatic activity of SIRT2 is dependent on nicotinamide adenine dinucleotide (NAD+) and SIRT2 regulates post-translational modifications that are responsible for deacetylation of lysine residues in histone and non-histone substrates.	Lysine	184-190	sirtuin 2	Homo sapiens	93-98
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 2	Homo sapiens	205-210
35406775-0	2022	Assessment of Pharmacological Interactions between SIRT2 Inhibitor AGK2 and Paclitaxel in Different Molecular Subtypes of Breast Cancer Cells.	Paclitaxel	76-86	sirtuin 2	Homo sapiens	51-56
35150663-10	2022	Of those, the selective SIRT2 inhibitor Mz25 showed a strong cestocidal activity in Mesocestoides vogae (syn.	mz25	40-44	sirtuin 2	Homo sapiens	24-29
35150663-15	2022	Interestingly, some non-conservative mutations were found on the selectivity pocket (an Mz25-induced structural rearrangement on the active site), which represent a promising lead for developing selective cestode SIRT2 inhibitors derived from Mz25.	mz25	88-92	sirtuin 2	Homo sapiens	213-218
35150663-15	2022	Interestingly, some non-conservative mutations were found on the selectivity pocket (an Mz25-induced structural rearrangement on the active site), which represent a promising lead for developing selective cestode SIRT2 inhibitors derived from Mz25.	mz25	243-247	sirtuin 2	Homo sapiens	213-218
35353606-8	2022	RSV can activate the human silent information regulator 2/sirtuin 1 (Sirt-1) and can inhibit the cyclooxygenase-2 (COX-2), 5-lipoxygenase, and nuclear factor-kappaB, resulting in the reduction of the proinflammation pathways.	Resveratrol	0-3	sirtuin 2	Homo sapiens	27-67
35441145-0	2022	Development of a NanoBRET assay to validate inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration.	Lysine	73-79	sirtuin 2	Homo sapiens	58-63
35441145-1	2022	Sirtuin2 (Sirt2) with its NAD+-dependent deacetylase and defatty-acylase activities plays a central role in the regulation of specific cellular functions.	NAD	26-29	sirtuin 2	Homo sapiens	0-8
35441145-1	2022	Sirtuin2 (Sirt2) with its NAD+-dependent deacetylase and defatty-acylase activities plays a central role in the regulation of specific cellular functions.	NAD	26-29	sirtuin 2	Homo sapiens	10-15
35425455-5	2022	The MD simulation unveiled that electrostatic complementarity at the substrate-binding-site through a novel motif "SLxVxP(V/F)A" could be a cause of increased Sirt1 inhibition by 13h and 13l over Sirt2 in cell-based assay, as compared to the control Ex527 and 7d.	13h	179-182	sirtuin 2	Homo sapiens	196-201
34979841-0	2021	SIRT2 tyrosine nitration by peroxynitrite in response to renal ischaemia/reperfusion injury.	Tyrosine	6-14	sirtuin 2	Homo sapiens	0-5
34979841-0	2021	SIRT2 tyrosine nitration by peroxynitrite in response to renal ischaemia/reperfusion injury.	Peroxynitrous Acid	28-41	sirtuin 2	Homo sapiens	0-5
34979841-2	2021	The current study is to elucidate a mechanism of SIRT2 tyrosine nitration to accelerate the cell apoptosis induced by peroxynitrite (ONOO ), the most reactive and deleterious RNS type in renal ischaemia/reperfusion (I/R) injury.	Tyrosine	55-63	sirtuin 2	Homo sapiens	49-54
34979841-2	2021	The current study is to elucidate a mechanism of SIRT2 tyrosine nitration to accelerate the cell apoptosis induced by peroxynitrite (ONOO ), the most reactive and deleterious RNS type in renal ischaemia/reperfusion (I/R) injury.	Peroxynitrous Acid	118-131	sirtuin 2	Homo sapiens	49-54
34979841-2	2021	The current study is to elucidate a mechanism of SIRT2 tyrosine nitration to accelerate the cell apoptosis induced by peroxynitrite (ONOO ), the most reactive and deleterious RNS type in renal ischaemia/reperfusion (I/R) injury.	onoo	133-137	sirtuin 2	Homo sapiens	49-54
34979841-4	2021	Notably, peroxynitrite-evoked nitration of SIRT2 destroyed its enzymatic activity and the capability to deacetylate FOXO3a, and enhanced expression of Bim and caspase3, facilitating renal cell apoptosis in renal ischaemia/reperfusion and SIN-1(peroxynitrite donor) treatment in vitro, and these effects were reversed by FeTMPyP, a peroxynitrite decomposition scavenger.	Peroxynitrous Acid	9-22	sirtuin 2	Homo sapiens	43-48
34979841-4	2021	Notably, peroxynitrite-evoked nitration of SIRT2 destroyed its enzymatic activity and the capability to deacetylate FOXO3a, and enhanced expression of Bim and caspase3, facilitating renal cell apoptosis in renal ischaemia/reperfusion and SIN-1(peroxynitrite donor) treatment in vitro, and these effects were reversed by FeTMPyP, a peroxynitrite decomposition scavenger.	Peroxynitrous Acid	244-257	sirtuin 2	Homo sapiens	43-48
34979841-4	2021	Notably, peroxynitrite-evoked nitration of SIRT2 destroyed its enzymatic activity and the capability to deacetylate FOXO3a, and enhanced expression of Bim and caspase3, facilitating renal cell apoptosis in renal ischaemia/reperfusion and SIN-1(peroxynitrite donor) treatment in vitro, and these effects were reversed by FeTMPyP, a peroxynitrite decomposition scavenger.	FeTMPyP	320-327	sirtuin 2	Homo sapiens	43-48
34979841-4	2021	Notably, peroxynitrite-evoked nitration of SIRT2 destroyed its enzymatic activity and the capability to deacetylate FOXO3a, and enhanced expression of Bim and caspase3, facilitating renal cell apoptosis in renal ischaemia/reperfusion and SIN-1(peroxynitrite donor) treatment in vitro, and these effects were reversed by FeTMPyP, a peroxynitrite decomposition scavenger.	Peroxynitrous Acid	331-344	sirtuin 2	Homo sapiens	43-48
34979841-5	2021	Importantly, we identified that the tyrosine 86 is responsible for SIRT2 nitration and inactivation using site-mutation assay and Mass Spectrography analysis.	Tyrosine	36-44	sirtuin 2	Homo sapiens	67-72
34979841-6	2021	Altogether, these findings point to a novel protective mechanism that an inhibition of SIRT2 tyrosine nitration can be a promising strategy to prevent ischaemic renal diseases involving AKI.	Tyrosine	93-101	sirtuin 2	Homo sapiens	87-92
34028177-6	2021	SIRT2 can reduce the level of reactive oxygen species (ROS), which may help to reduce the severity of diabetic cardiomyopathy.	Reactive Oxygen Species	30-53	sirtuin 2	Homo sapiens	0-5
34028177-6	2021	SIRT2 can reduce the level of reactive oxygen species (ROS), which may help to reduce the severity of diabetic cardiomyopathy.	Reactive Oxygen Species	55-58	sirtuin 2	Homo sapiens	0-5
33627431-3	2021	Our analyses of human cancerous tissue revealed that the NAD-dependent deacetylase SIRT2 is up-regulated in early-stage carcinomas of various organs.	NAD	57-60	sirtuin 2	Homo sapiens	83-88
33606530-5	2021	Furthermore, essential dynamics and residue network analysis revealed that the side-chain reorientation in residue F190 due to nonconserved residue Y191 played a major role in the formation of an extended selectivity pocket in Sirt2.	y191	148-152	sirtuin 2	Homo sapiens	227-232
33986372-5	2021	The molecular dynamics simulations and post-simulation analysis of Sirt2-drug complexes revealed substantial stability for Fluphenazine and Nintedanib with Sirt2.	Fluphenazine	123-135	sirtuin 2	Homo sapiens	67-72
33986372-5	2021	The molecular dynamics simulations and post-simulation analysis of Sirt2-drug complexes revealed substantial stability for Fluphenazine and Nintedanib with Sirt2.	nintedanib	140-150	sirtuin 2	Homo sapiens	67-72
33986372-5	2021	The molecular dynamics simulations and post-simulation analysis of Sirt2-drug complexes revealed substantial stability for Fluphenazine and Nintedanib with Sirt2.	nintedanib	140-150	sirtuin 2	Homo sapiens	156-161
33738067-4	2021	The most potent inhibitor 12n displayed an IC50 of 460 nM and a selectivity for SIRT1 over SIRT2, SIRT3, and SIRT5 of 113.5-, 254.3-, and 10.83-fold, respectively.	12-nitroxide stearate	26-29	sirtuin 2	Homo sapiens	91-96
33614337-9	2021	Sirtuin 2 (SIRT2) regulates LDL cholesterol by inhibiting pcsk9, increasing LDL receptors on the cell surface of hepatocytes.	Cholesterol	32-43	sirtuin 2	Homo sapiens	0-9
33566315-0	2022	Sirtuin2 correlates with lymph node metastasis, increased FIGO stage, worse overall survival, and reduced chemosensitivity to cisplatin and paclitaxel in endometrial cancer.	Cisplatin	126-135	sirtuin 2	Homo sapiens	0-8
33566315-0	2022	Sirtuin2 correlates with lymph node metastasis, increased FIGO stage, worse overall survival, and reduced chemosensitivity to cisplatin and paclitaxel in endometrial cancer.	Paclitaxel	140-150	sirtuin 2	Homo sapiens	0-8
33566315-5	2022	Besides, SIRT2 was modulated by plasmid transfection in EC cells, then their chemosensitivity to cisplatin and paclitaxel was evaluated.	Cisplatin	97-106	sirtuin 2	Homo sapiens	9-14
33566315-5	2022	Besides, SIRT2 was modulated by plasmid transfection in EC cells, then their chemosensitivity to cisplatin and paclitaxel was evaluated.	Paclitaxel	111-121	sirtuin 2	Homo sapiens	9-14
33566315-10	2022	SIRT2 overexpression decreased chemosensitivity to cisplatin and paclitaxel in Ishikawa cells, while SIRT2 knockdown increased chemosensitivity to cisplatin and paclitaxel in KLE cells (all P < 0.05).	Cisplatin	51-60	sirtuin 2	Homo sapiens	0-5
33566315-10	2022	SIRT2 overexpression decreased chemosensitivity to cisplatin and paclitaxel in Ishikawa cells, while SIRT2 knockdown increased chemosensitivity to cisplatin and paclitaxel in KLE cells (all P < 0.05).	Paclitaxel	65-75	sirtuin 2	Homo sapiens	0-5
33566315-10	2022	SIRT2 overexpression decreased chemosensitivity to cisplatin and paclitaxel in Ishikawa cells, while SIRT2 knockdown increased chemosensitivity to cisplatin and paclitaxel in KLE cells (all P < 0.05).	Cisplatin	147-156	sirtuin 2	Homo sapiens	101-106
33566315-11	2022	CONCLUSION: SIRT2 correlates with lymph node metastasis, increased FIGO stage, worse OS, and reduced chemosensitivity to cisplatin and paclitaxel in EC.	Cisplatin	121-130	sirtuin 2	Homo sapiens	12-17
33566315-11	2022	CONCLUSION: SIRT2 correlates with lymph node metastasis, increased FIGO stage, worse OS, and reduced chemosensitivity to cisplatin and paclitaxel in EC.	Paclitaxel	135-145	sirtuin 2	Homo sapiens	12-17
33546767-7	2021	We found that inhibition of NAMPT or SIRT2 in iPS cells induces p53 protein by promoting its lysine acetylation.	Lysine	93-99	sirtuin 2	Homo sapiens	37-42
33316537-4	2021	In this study, we found that SUMOylation can occur in the Sirt2 protein at both lysine 183 and lysine 340 sites.	Lysine	80-86	sirtuin 2	Homo sapiens	58-63
33316537-4	2021	In this study, we found that SUMOylation can occur in the Sirt2 protein at both lysine 183 and lysine 340 sites.	Lysine	95-101	sirtuin 2	Homo sapiens	58-63
33360352-2	2021	NQO1 catalyzes the oxidation of NADH to NAD+ and may supplement levels of NAD+ near microtubules to aid SIRT2 deacetylase activity.	NAD	74-78	sirtuin 2	Homo sapiens	104-109
33438557-6	2021	RESULTS: Experimental in vitro testing of highest-ranked hits identified asperphenamate and salvianolic acid B as active SIRT2 inhibitors with IC50 values in low micromolar range.	asperphenamate	73-87	sirtuin 2	Homo sapiens	121-126
33438557-6	2021	RESULTS: Experimental in vitro testing of highest-ranked hits identified asperphenamate and salvianolic acid B as active SIRT2 inhibitors with IC50 values in low micromolar range.	salvianolic acid B	92-110	sirtuin 2	Homo sapiens	121-126
33569452-14	2021	Conclusions: SIRT2 expression may be a useful marker for identifying sepsis survivors who are at risk of progressing to CCI.	CCI	120-123	sirtuin 2	Homo sapiens	13-18
33614337-9	2021	Sirtuin 2 (SIRT2) regulates LDL cholesterol by inhibiting pcsk9, increasing LDL receptors on the cell surface of hepatocytes.	Cholesterol	32-43	sirtuin 2	Homo sapiens	11-16
32672888-1	2020	We have discovered the sirtuin rearranging ligands (SirReals) as a novel class of highly potent and selective inhibitors of the NAD+-dependent lysine deacetylase sirtuin 2 (Sirt2).	NAD	128-131	sirtuin 2	Homo sapiens	162-171
32672888-1	2020	We have discovered the sirtuin rearranging ligands (SirReals) as a novel class of highly potent and selective inhibitors of the NAD+-dependent lysine deacetylase sirtuin 2 (Sirt2).	NAD	128-131	sirtuin 2	Homo sapiens	173-178
32965071-6	2020	Reagents targeting the NAD+ -dependent deacetylase activity of SIRT2 would be beneficial for inhibiting tumor lymphangiogenesis and treating other hypoxia-related diseases.	NAD	23-26	sirtuin 2	Homo sapiens	63-68
33207824-0	2020	ROS-Induced SIRT2 Upregulation Contributes to Cisplatin Sensitivity in Ovarian Cancer.	Reactive Oxygen Species	0-3	sirtuin 2	Homo sapiens	12-17
33207824-0	2020	ROS-Induced SIRT2 Upregulation Contributes to Cisplatin Sensitivity in Ovarian Cancer.	Cisplatin	46-55	sirtuin 2	Homo sapiens	12-17
33207824-4	2020	In this study, we aimed to identify the role of SIRT2 in oxidative stress and cisplatin response in cancer.	Cisplatin	78-87	sirtuin 2	Homo sapiens	48-53
33207824-6	2020	We found different expression patterns of SIRT2 in cisplatin-sensitive (A2780/S) and cisplatin-resistant (A2780/CP) cancer cells with cisplatin treatment, where SIRT2 expression was augmented only in A2780/S cells.	Cisplatin	51-60	sirtuin 2	Homo sapiens	42-47
33207824-6	2020	We found different expression patterns of SIRT2 in cisplatin-sensitive (A2780/S) and cisplatin-resistant (A2780/CP) cancer cells with cisplatin treatment, where SIRT2 expression was augmented only in A2780/S cells.	Cisplatin	51-60	sirtuin 2	Homo sapiens	161-166
33207824-6	2020	We found different expression patterns of SIRT2 in cisplatin-sensitive (A2780/S) and cisplatin-resistant (A2780/CP) cancer cells with cisplatin treatment, where SIRT2 expression was augmented only in A2780/S cells.	Cisplatin	85-94	sirtuin 2	Homo sapiens	42-47
33207824-6	2020	We found different expression patterns of SIRT2 in cisplatin-sensitive (A2780/S) and cisplatin-resistant (A2780/CP) cancer cells with cisplatin treatment, where SIRT2 expression was augmented only in A2780/S cells.	Cisplatin	85-94	sirtuin 2	Homo sapiens	161-166
33207824-6	2020	We found different expression patterns of SIRT2 in cisplatin-sensitive (A2780/S) and cisplatin-resistant (A2780/CP) cancer cells with cisplatin treatment, where SIRT2 expression was augmented only in A2780/S cells.	Cisplatin	85-94	sirtuin 2	Homo sapiens	42-47
33207824-6	2020	We found different expression patterns of SIRT2 in cisplatin-sensitive (A2780/S) and cisplatin-resistant (A2780/CP) cancer cells with cisplatin treatment, where SIRT2 expression was augmented only in A2780/S cells.	Cisplatin	85-94	sirtuin 2	Homo sapiens	161-166
33207824-7	2020	Furthermore, cisplatin-induced ROS generation was responsible for the upregulation of SIRT2 in A2780/S cells, whereas overexpression of SIRT2 significantly enhanced the sensitivity of cisplatin-resistant counterpart cells to cisplatin.	Cisplatin	13-22	sirtuin 2	Homo sapiens	86-91
33207824-7	2020	Furthermore, cisplatin-induced ROS generation was responsible for the upregulation of SIRT2 in A2780/S cells, whereas overexpression of SIRT2 significantly enhanced the sensitivity of cisplatin-resistant counterpart cells to cisplatin.	Cisplatin	184-193	sirtuin 2	Homo sapiens	136-141
33207824-7	2020	Furthermore, cisplatin-induced ROS generation was responsible for the upregulation of SIRT2 in A2780/S cells, whereas overexpression of SIRT2 significantly enhanced the sensitivity of cisplatin-resistant counterpart cells to cisplatin.	Cisplatin	184-193	sirtuin 2	Homo sapiens	136-141
33207824-8	2020	Our study proposes that targeting SIRT2 may provide new strategies to potentiate platinum-based chemotherapy in ovarian cancer patients.	Platinum	81-89	sirtuin 2	Homo sapiens	34-39
33129330-13	2020	Silencing LncRNA-NEAT1 in MSCs, miR-221-3p overexpression or Sirt2 silencing in cardiomyocytes decreased the exosomeMIF-induced anti-senescent effect against Dox.	Doxorubicin	158-161	sirtuin 2	Homo sapiens	61-66
33129330-14	2020	CONCLUSIONS: The results indicated exosomeMIF serving as a promising anti-senescent effector against Dox-induced cardiotoxicity through LncRNA-NEAT1 transfer, thus inhibiting miR-221-3p and leading to Sirt2 activation.	Doxorubicin	101-104	sirtuin 2	Homo sapiens	201-206
33061819-0	2020	The NAD-dependent deacetylase SIRT2 regulates T cell differentiation involved in tumor immune response.	NAD	4-7	sirtuin 2	Homo sapiens	30-35
32941003-0	2020	Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene.	1-aminoanthracene	64-81	sirtuin 2	Homo sapiens	34-39
32941003-1	2020	Sirtuin isoform 2 (SIRT2) is an enzyme that catalyzes the removal of acyl groups from lysine residues.	Lysine	86-92	sirtuin 2	Homo sapiens	0-17
32941003-1	2020	Sirtuin isoform 2 (SIRT2) is an enzyme that catalyzes the removal of acyl groups from lysine residues.	Lysine	86-92	sirtuin 2	Homo sapiens	19-24
32941003-3	2020	Here, we report that the fluorescent probe 1-aminoanthracene (AMA) binds within SIRT2"s hydrophobic tunnel in a substrate-dependent manner.	1-aminoanthracene	43-60	sirtuin 2	Homo sapiens	80-85
32941003-3	2020	Here, we report that the fluorescent probe 1-aminoanthracene (AMA) binds within SIRT2"s hydrophobic tunnel in a substrate-dependent manner.	1-aminoanthracene	62-65	sirtuin 2	Homo sapiens	80-85
33061819-1	2020	Sirtuin 2 (SIRT2), an NAD+-dependent deacetylase, regulates multiple biologic and pathologic processes including mitosis, genomic integrity, cell homeostasis and tumorigenesis.	NAD	22-25	sirtuin 2	Homo sapiens	0-9
33061819-1	2020	Sirtuin 2 (SIRT2), an NAD+-dependent deacetylase, regulates multiple biologic and pathologic processes including mitosis, genomic integrity, cell homeostasis and tumorigenesis.	NAD	22-25	sirtuin 2	Homo sapiens	11-16
32755678-0	2020	Structure activity study of S-trityl-cysteamine dimethylaminopyridine derivatives as SIRT2 inhibitors: Improvement of SIRT2 binding and inhibition.	s-trityl-cysteamine dimethylaminopyridine	28-69	sirtuin 2	Homo sapiens	85-90
32755678-0	2020	Structure activity study of S-trityl-cysteamine dimethylaminopyridine derivatives as SIRT2 inhibitors: Improvement of SIRT2 binding and inhibition.	s-trityl-cysteamine dimethylaminopyridine	28-69	sirtuin 2	Homo sapiens	118-123
32755678-4	2020	Previously, we reported S-Trityl-L-Cysteine (STLC)-ornamented dimethylaminopyridine chemical entity named STC4 with a significant SIRT2 inhibitory capacity; this was separate from the conventional application of STLC scaffold as a kinesin-5 inhibitor.	3-tritylthio-L-alanine	24-43	sirtuin 2	Homo sapiens	130-135
32755678-4	2020	Previously, we reported S-Trityl-L-Cysteine (STLC)-ornamented dimethylaminopyridine chemical entity named STC4 with a significant SIRT2 inhibitory capacity; this was separate from the conventional application of STLC scaffold as a kinesin-5 inhibitor.	3-tritylthio-L-alanine	45-49	sirtuin 2	Homo sapiens	130-135
32755678-4	2020	Previously, we reported S-Trityl-L-Cysteine (STLC)-ornamented dimethylaminopyridine chemical entity named STC4 with a significant SIRT2 inhibitory capacity; this was separate from the conventional application of STLC scaffold as a kinesin-5 inhibitor.	2-Dimethylaminopyridine	62-83	sirtuin 2	Homo sapiens	130-135
32755678-5	2020	An interactive molecular docking study of SIRT2 and STC4 showed interaction between Asn168 of SIRT2 and the methyl ester of STC4, that appears to hinder STC4 to reach the selective pocket of the protein unlike strong SIRT2 inhibitor SirReal2.	methyl ester	108-120	sirtuin 2	Homo sapiens	42-47
32755678-5	2020	An interactive molecular docking study of SIRT2 and STC4 showed interaction between Asn168 of SIRT2 and the methyl ester of STC4, that appears to hinder STC4 to reach the selective pocket of the protein unlike strong SIRT2 inhibitor SirReal2.	methyl ester	108-120	sirtuin 2	Homo sapiens	94-99
32755678-5	2020	An interactive molecular docking study of SIRT2 and STC4 showed interaction between Asn168 of SIRT2 and the methyl ester of STC4, that appears to hinder STC4 to reach the selective pocket of the protein unlike strong SIRT2 inhibitor SirReal2.	methyl ester	108-120	sirtuin 2	Homo sapiens	94-99
32755678-9	2020	A molecular docking study was executed to shed light on the supposed binding mode of the lead compound, STCY1, into the selective pocket of SIRT2 by interaction of the nitrogen of pyridine ring of the compound and Ala135 of the protein.	Nitrogen	168-176	sirtuin 2	Homo sapiens	140-145
32755678-9	2020	A molecular docking study was executed to shed light on the supposed binding mode of the lead compound, STCY1, into the selective pocket of SIRT2 by interaction of the nitrogen of pyridine ring of the compound and Ala135 of the protein.	pyridine	180-188	sirtuin 2	Homo sapiens	140-145
32697380-6	2020	The ectopic expression of SIRT2 reverses the effect of miR-212-5p overexpression on CRC cell colony formation, invasion, migration and proliferation.	mir-212-5p	55-65	sirtuin 2	Homo sapiens	26-31
33214845-1	2020	As a member of the sirtuin family of enzymes, SIRT2 promotes tumor growth and regulates various biological pathways through lysine deacetylation and defatty-acylation.	Lysine	124-130	sirtuin 2	Homo sapiens	46-51
33214845-4	2020	Here, we have applied the Proteolysis Targeting Chimera (PROTAC) strategy and synthesized a new SIRT2 inhibitor (TM-P4-Thal) to degrade SIRT2 selectively, which led to simultaneous inhibition of its deacetylase and defatty-acylase activities in living cells.	tm-p4-thal	113-123	sirtuin 2	Homo sapiens	96-101
33214845-4	2020	Here, we have applied the Proteolysis Targeting Chimera (PROTAC) strategy and synthesized a new SIRT2 inhibitor (TM-P4-Thal) to degrade SIRT2 selectively, which led to simultaneous inhibition of its deacetylase and defatty-acylase activities in living cells.	tm-p4-thal	113-123	sirtuin 2	Homo sapiens	136-141
32711231-4	2020	The most potent SIRT1 inhibitor 3h, bearing an isopropyl substituent, was as potent as EX-527, and more selective for SIRT1 over SIRT2.	Tritium	32-34	sirtuin 2	Homo sapiens	129-134
33117567-6	2020	Theoretical prediction of potential biological activities was performed, which suggested that the title anil compound can exhibit histone de-acetyl-ase SIRT2, histone de-acetyl-ase class III and histone de-acetyl-ase SIRT1 activities, and will act as inhibitor to aspulvinone di-methyl-allyl-transferase, de-hydro-l-gulonate deca-rboxylase and gluta-thione thiol-esterase.	anil	104-108	sirtuin 2	Homo sapiens	152-157
32768387-5	2020	Mechanistically, Sirt2 suppresses T cell metabolism by targeting key enzymes involved in glycolysis, tricarboxylic acid-cycle, fatty acid oxidation, and glutaminolysis.	Tricarboxylic Acids	101-119	sirtuin 2	Homo sapiens	17-22
32768387-5	2020	Mechanistically, Sirt2 suppresses T cell metabolism by targeting key enzymes involved in glycolysis, tricarboxylic acid-cycle, fatty acid oxidation, and glutaminolysis.	Fatty Acids	127-137	sirtuin 2	Homo sapiens	17-22
32831651-10	2020	Impact of modulation of p33ING1b alone or in combination with SIR2 on chemosensitivity of YD-9 and YD-8 cells to cisplatin was determined in time and dose-dependent cell proliferation assays.	Cisplatin	113-122	sirtuin 2	Homo sapiens	62-66
32831651-16	2020	Expression of p33ING1b was found to be inversely correlated to the NAD-dependent deacetylase silent information regulator 2 (SIR2).	NAD	67-70	sirtuin 2	Homo sapiens	93-123
32831651-16	2020	Expression of p33ING1b was found to be inversely correlated to the NAD-dependent deacetylase silent information regulator 2 (SIR2).	NAD	67-70	sirtuin 2	Homo sapiens	125-129
32831651-19	2020	Concomitant overexpression of p33ING1b and knockdown of SIR2 had a synergistic effect on chemosensitivity of OSCC cell lines to cisplatin, compared to either overexpression of p33ING1b or knockdown of SIR2 alone.	Cisplatin	128-137	sirtuin 2	Homo sapiens	56-60
32631535-0	2020	Exploring the newer oxadiazoles as real inhibitors of human SIRT2 in hepatocellular cancer cells.	Oxadiazoles	20-31	sirtuin 2	Homo sapiens	60-65
32631535-3	2020	Among the tested OTDs, compound 2-(4-methoxyphenyl)-5-(1-methyl-1H-indazol-3-yl)-1,3,4-oxadiazole was found to inhibit the catalytical activity of SIRT2 and brings about apoptosis as shown by western blot analysis and flow cytometry data.	2-(4-methoxyphenyl)-5-(1-methyl-1h-indazol-3-yl)-1,3,4-oxadiazole	32-97	sirtuin 2	Homo sapiens	147-152
32783943-7	2020	Tip60 and SIRT2 regulate the reversible acetylation modification of PHGDH in response to glucose alteration.	Glucose	89-96	sirtuin 2	Homo sapiens	10-15
32314517-5	2020	Besides, derivatization with long-chain fatty acids yielded potent sirtuin 2 inhibitors, featuring another intriguing aspect of azo-based photoswitches.	long-chain fatty acids	29-51	sirtuin 2	Homo sapiens	67-76
32314517-5	2020	Besides, derivatization with long-chain fatty acids yielded potent sirtuin 2 inhibitors, featuring another intriguing aspect of azo-based photoswitches.	azo-based	128-137	sirtuin 2	Homo sapiens	67-76
32170178-4	2020	To demonstrate this, phage-displayed peptide libraries are developed that contain a genetically encoded butyryl lysine and are subsequently used to select for ligands that bind SIRT2.	butyryl lysine	104-118	sirtuin 2	Homo sapiens	177-182
32371394-3	2020	Here, using IC50 and k inact/K I analyses, we quantified the ability of nitrosothiols (S-nitrosoglutathione and S-nitroso-N-acetyl-D,L-penicillamine), nitric oxide, oxidized glutathione, and hydrogen peroxide to posttranslationally modify and inhibit the deacylase activity of Sirt1, Sirt2, Sirt3, Sirt5, and Sirt6.	S-Nitrosothiols	72-85	sirtuin 2	Homo sapiens	284-289
32371394-5	2020	We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation.	Cysteine	141-149	sirtuin 2	Homo sapiens	104-109
32371394-5	2020	We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation.	Cysteine	141-149	sirtuin 2	Homo sapiens	288-293
32371394-5	2020	We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation.	Nitric Oxide	201-213	sirtuin 2	Homo sapiens	104-109
32371394-5	2020	We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation.	Nitric Oxide	201-213	sirtuin 2	Homo sapiens	288-293
32371394-5	2020	We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation.	S-Nitrosothiols	218-231	sirtuin 2	Homo sapiens	104-109
32549218-0	2020	Design, Synthesis, and Biological Evaluation of 8-Mercapto-3,7-Dihydro-1H-Purine-2,6-Diones as Potent Inhibitors of SIRT1, SIRT2, SIRT3, and SIRT5.	8-mercapto-3,7-dihydro-1h-purine-2,6-diones	48-91	sirtuin 2	Homo sapiens	123-128
32112098-3	2020	MORC2 is acetylated by the acetyltransferase NAT10 at lysine 767 (K767Ac) and this process is counteracted by the deacetylase SIRT2 under unperturbed conditions.	Lysine	54-60	sirtuin 2	Homo sapiens	126-131
32493816-1	2020	Sirtuin 2 (Sirt2), an NAD+-dependent protein deacetylase, deacetylates tubulin, AKT, and other proteins.	NAD	22-25	sirtuin 2	Homo sapiens	0-9
32493816-1	2020	Sirtuin 2 (Sirt2), an NAD+-dependent protein deacetylase, deacetylates tubulin, AKT, and other proteins.	NAD	22-25	sirtuin 2	Homo sapiens	11-16
32711564-5	2020	We also demonstrated that ectopic expression of SIRT2, a cytoplasmic NAD+ - dependent deacetylase, suppresses the defects of HDAC6 knockdown neurons.	NAD	69-72	sirtuin 2	Homo sapiens	48-53
32247664-6	2020	In addition, KCl depolarization inhibits the activity of SIRT2, an alpha-tubulin deacetylase.	Potassium Chloride	13-16	sirtuin 2	Homo sapiens	57-62
32247664-7	2020	The inhibitory effect of KCl on SIRT2 activity requires CDK5 activity.	Potassium Chloride	25-28	sirtuin 2	Homo sapiens	32-37
31692222-1	2020	We have discovered the sirtuin rearranging ligands (SirReals) as highly potent and selective inhibitors of the NAD+-dependent lysine deacetylase Sirt2.	NAD	111-114	sirtuin 2	Homo sapiens	145-150
31692222-1	2020	We have discovered the sirtuin rearranging ligands (SirReals) as highly potent and selective inhibitors of the NAD+-dependent lysine deacetylase Sirt2.	tyrosyl-lysine	126-132	sirtuin 2	Homo sapiens	145-150
32141187-4	2020	We find that IDH1 K224 deacetylation promotes its enzymatic activity and the production of alpha-KG, and we identify sirtuin-2 (SIRT2) as a major deacetylase for IDH1.	alpha-kg	91-99	sirtuin 2	Homo sapiens	128-133
31932479-1	2020	The NAD-dependent histone deacetylase sirtuin 2 (SIRT2) plays critical roles in mitosis and cell cycle progression and recently was shown to suppress tumor growth and to be down-regulated in several types of cancers.	NAD	4-7	sirtuin 2	Homo sapiens	38-47
31932479-1	2020	The NAD-dependent histone deacetylase sirtuin 2 (SIRT2) plays critical roles in mitosis and cell cycle progression and recently was shown to suppress tumor growth and to be down-regulated in several types of cancers.	NAD	4-7	sirtuin 2	Homo sapiens	49-54
32122297-0	2020	Sirt2-associated transcriptome modifications in cisplatin-induced neuronal injury.	Cisplatin	48-57	sirtuin 2	Homo sapiens	0-5
32122297-3	2020	As demonstrated previously by our laboratory and others, the overexpression of Sirt2 can improve cisplatin-induced neuropathy, although the mechanism is still unclear.	Cisplatin	97-106	sirtuin 2	Homo sapiens	79-84
32122297-4	2020	RESULTS: In this study, the underlying mechanism by which Sirt2 protects neurons from cisplatin-induced injury was explored using the RNAseq technique in cultured rodent neurons.	Cisplatin	86-95	sirtuin 2	Homo sapiens	58-63
32122297-8	2020	Furthermore, cisplatin-induced changes to the transcriptome are strongly associated with Sirt2 status.	Cisplatin	13-22	sirtuin 2	Homo sapiens	89-94
32122297-9	2020	Cisplatin induced distinctive transcriptome changes for 227 genes in Sirt2-expressing cells and for 783 genes in Sirt2-deficient cells, while changes in only 138 of these genes were independent of Sirt2 status.	Cisplatin	0-9	sirtuin 2	Homo sapiens	69-74
32122297-9	2020	Cisplatin induced distinctive transcriptome changes for 227 genes in Sirt2-expressing cells and for 783 genes in Sirt2-deficient cells, while changes in only 138 of these genes were independent of Sirt2 status.	Cisplatin	0-9	sirtuin 2	Homo sapiens	113-118
32122297-9	2020	Cisplatin induced distinctive transcriptome changes for 227 genes in Sirt2-expressing cells and for 783 genes in Sirt2-deficient cells, while changes in only 138 of these genes were independent of Sirt2 status.	Cisplatin	0-9	sirtuin 2	Homo sapiens	113-118
32122297-10	2020	Interestingly, changes in the p53 pathway, ECM-receptor interactions, and cytokine-cytokine receptor interactions were induced by cisplatin only in Sirt2-deficient cells.	Cisplatin	130-139	sirtuin 2	Homo sapiens	148-153
32122297-12	2020	Furthermore, Sirt2-associated transcriptome regulation may be an important mechanism underlying the role of Sirt2 in organ protection, such as in cisplatin-induced neuronal injury.	Cisplatin	146-155	sirtuin 2	Homo sapiens	13-18
32122297-12	2020	Furthermore, Sirt2-associated transcriptome regulation may be an important mechanism underlying the role of Sirt2 in organ protection, such as in cisplatin-induced neuronal injury.	Cisplatin	146-155	sirtuin 2	Homo sapiens	108-113
31848116-3	2020	Previously, we have shown that substituted 2-alkyl-chroman-4-one/chromone derivatives can serve as selective inhibitors of SIRT2 possessing an antiproliferative effect in two human cancer cell lines.	2-alkyl-chroman-4-one	43-64	sirtuin 2	Homo sapiens	123-128
32271403-12	2020	High glucose suppressed the expression of SIRT2 but accelerated the acetylation of H3K9, H3K14, and H3K56.	Glucose	5-12	sirtuin 2	Homo sapiens	42-47
32271403-16	2020	However, supplied rh-SIRT2 reversed these negative effects of high glucose in CHs.	Glucose	67-74	sirtuin 2	Homo sapiens	21-26
32271403-17	2020	CONCLUSIONS: SIRT2 expression is reduced along with the diabetic OA process with increased acetylation of H3, oxidative stress, and inflammatory response.	HS 3	106-108	sirtuin 2	Homo sapiens	13-18
32103017-4	2020	We demonstrate that the NAD+-dependent deacylase SIRT2 removes the myristoyl group, and our evidence suggests that NMT prefers the GTP-bound while SIRT2 prefers the GDP-bound ARF6.	NAD	24-28	sirtuin 2	Homo sapiens	49-54
32103017-4	2020	We demonstrate that the NAD+-dependent deacylase SIRT2 removes the myristoyl group, and our evidence suggests that NMT prefers the GTP-bound while SIRT2 prefers the GDP-bound ARF6.	NAD	24-28	sirtuin 2	Homo sapiens	147-152
32103017-4	2020	We demonstrate that the NAD+-dependent deacylase SIRT2 removes the myristoyl group, and our evidence suggests that NMT prefers the GTP-bound while SIRT2 prefers the GDP-bound ARF6.	Guanosine Triphosphate	131-134	sirtuin 2	Homo sapiens	49-54
32103017-4	2020	We demonstrate that the NAD+-dependent deacylase SIRT2 removes the myristoyl group, and our evidence suggests that NMT prefers the GTP-bound while SIRT2 prefers the GDP-bound ARF6.	Guanosine Diphosphate	165-168	sirtuin 2	Homo sapiens	49-54
32103017-4	2020	We demonstrate that the NAD+-dependent deacylase SIRT2 removes the myristoyl group, and our evidence suggests that NMT prefers the GTP-bound while SIRT2 prefers the GDP-bound ARF6.	Guanosine Diphosphate	165-168	sirtuin 2	Homo sapiens	147-152
32049001-3	2020	Treatment with the NAD+ metabolic precursor nicotinamide mononucleotide (NMN) rejuvenates oocyte quality in aged animals, leading to restoration in fertility, and this can be recapitulated by transgenic overexpression of the NAD+-dependent deacylase SIRT2, though deletion of this enzyme does not impair oocyte quality.	NAD	19-22	sirtuin 2	Homo sapiens	250-255
32049001-3	2020	Treatment with the NAD+ metabolic precursor nicotinamide mononucleotide (NMN) rejuvenates oocyte quality in aged animals, leading to restoration in fertility, and this can be recapitulated by transgenic overexpression of the NAD+-dependent deacylase SIRT2, though deletion of this enzyme does not impair oocyte quality.	Nicotinamide Mononucleotide	44-71	sirtuin 2	Homo sapiens	250-255
32049001-3	2020	Treatment with the NAD+ metabolic precursor nicotinamide mononucleotide (NMN) rejuvenates oocyte quality in aged animals, leading to restoration in fertility, and this can be recapitulated by transgenic overexpression of the NAD+-dependent deacylase SIRT2, though deletion of this enzyme does not impair oocyte quality.	Nicotinamide Mononucleotide	73-76	sirtuin 2	Homo sapiens	250-255
32049001-3	2020	Treatment with the NAD+ metabolic precursor nicotinamide mononucleotide (NMN) rejuvenates oocyte quality in aged animals, leading to restoration in fertility, and this can be recapitulated by transgenic overexpression of the NAD+-dependent deacylase SIRT2, though deletion of this enzyme does not impair oocyte quality.	NAD	225-228	sirtuin 2	Homo sapiens	250-255
31812033-0	2020	Synthesis of certain benzothieno[3,2-d]pyrimidine derivatives as a selective SIRT2 inhibitors.	benzothieno[3,2-d]pyrimidine	21-49	sirtuin 2	Homo sapiens	77-82
31848116-3	2020	Previously, we have shown that substituted 2-alkyl-chroman-4-one/chromone derivatives can serve as selective inhibitors of SIRT2 possessing an antiproliferative effect in two human cancer cell lines.	Chromones	65-73	sirtuin 2	Homo sapiens	123-128
31848116-6	2020	Among the evaluated scaffolds, the benzothiadiazine-1,1-dioxide-based compounds showed the highest SIRT2 inhibitory activity.	benzothiadiazine-1,1-dioxide	35-63	sirtuin 2	Homo sapiens	99-104
31644285-0	2019	Chemical Probes Reveal Sirt2"s New Function as a Robust "Eraser" of Lysine Lipoylation.	Lysine	68-74	sirtuin 2	Homo sapiens	23-28
31844103-4	2019	To understand Sirt6 modulation by quercetin-based compounds, we analysed their binding and activity effects on Sirt6 and other Sirtuin isoforms and solved crystal structures of compound complexes with Sirt6 and Sirt2.	Quercetin	34-43	sirtuin 2	Homo sapiens	211-216
31726826-4	2019	The reductive cleavage of an SiR2 moiety (R = 2,4,6-iPr3C6H2) from Si6R6 selectively yields a dianionic Si5R42- cluster as its lithium salt.	Silicon	67-69	sirtuin 2	Homo sapiens	29-33
31726826-4	2019	The reductive cleavage of an SiR2 moiety (R = 2,4,6-iPr3C6H2) from Si6R6 selectively yields a dianionic Si5R42- cluster as its lithium salt.	Lithium	127-134	sirtuin 2	Homo sapiens	29-33
31954883-7	2020	For studies using organoids, intestinal crypts were isolated RESULTS: Increased SIRT2 expression was localized to the more differentiated region of the intestine.	organoids	18-27	sirtuin 2	Homo sapiens	80-85
31644285-6	2019	To explore the potential activity of Sirt2 toward lysine lipoylation, we designed a single-step fluorogenic probe, KTlip, which reports delipoylation activity in a continuous manner.	Lysine	50-56	sirtuin 2	Homo sapiens	37-42
31644285-11	2019	Using our chemical probes, we have successfully established the relationship between Sirt2 and lysine lipoylation in living cells for the first time.	Lysine	95-101	sirtuin 2	Homo sapiens	85-90
31727006-9	2019	Consistently, clonogenic assays demonstrated that the SIRT2 inhibitors AK1 and AGK2 as well as SIRT2-knockdown increase Lapatinib cytotoxicity further in both the sensitive and resistant NPC cells.	lapatinib	120-129	sirtuin 2	Homo sapiens	54-59
31727006-9	2019	Consistently, clonogenic assays demonstrated that the SIRT2 inhibitors AK1 and AGK2 as well as SIRT2-knockdown increase Lapatinib cytotoxicity further in both the sensitive and resistant NPC cells.	lapatinib	120-129	sirtuin 2	Homo sapiens	95-100
31727006-11	2019	Importantly, SIRT2 inhibition and depletion further enhanced Lapatinib-mediated FOXO3-acetylation in NPC cells.	lapatinib	61-70	sirtuin 2	Homo sapiens	13-18
31727006-12	2019	CONCLUSION: Collectively, our results suggest the involvement of SIRT2-mediated FOXO3 deacetylation in Lapatinib response and sensitivity, and that SIRT2 can specifically antagonise the cytotoxicity of Lapatinib through mediating FOXO3 deacetylation in both sensitive and resistant NPC cells.	lapatinib	103-112	sirtuin 2	Homo sapiens	65-70
31727006-12	2019	CONCLUSION: Collectively, our results suggest the involvement of SIRT2-mediated FOXO3 deacetylation in Lapatinib response and sensitivity, and that SIRT2 can specifically antagonise the cytotoxicity of Lapatinib through mediating FOXO3 deacetylation in both sensitive and resistant NPC cells.	lapatinib	202-211	sirtuin 2	Homo sapiens	148-153
31727006-13	2019	The present findings also propose that SIRT2 can be an important biomarker for metastatic and Lapatinib resistant NPC and that targeting the SIRT2-FOXO3 axis may provide novel strategies for treating NPC and for overcoming chemoresistance.	lapatinib	94-103	sirtuin 2	Homo sapiens	39-44
31726691-5	2019	Our investigations indicated that chemical substitutions applied to MC2494 scaffold did not confer higher efficacy in terms of biological activity and SIRT1 inhibition, but carbethoxy-containing derivatives showed higher SIRT2 specificity.	3-carbethoxy-2-piperidone	173-183	sirtuin 2	Homo sapiens	221-226
31604796-1	2019	Sirtuin 2 (SIRT2) is an NAD-dependent sirtuin deacetylase that regulates microtubule and chromatin dynamics, gene expression and cell cycle progression, as well as nuclear envelope reassembly.	NAD	24-27	sirtuin 2	Homo sapiens	0-9
31727006-0	2019	Lapatinib sensitivity in nasopharyngeal carcinoma is modulated by SIRT2-mediated FOXO3 deacetylation.	lapatinib	0-9	sirtuin 2	Homo sapiens	66-71
31727006-6	2019	Western blot analysis of the Lapatinib-sensitive 6-10B and resistant 5-8F NPC cells showed that the expression of phosphorylated/inactive FOXO3 (P-FOXO3;T32), its target FOXM1 and its regulator SIRT2 correlate negatively with Lapatinib response and sensitivity, suggesting that SIRT2 mediates FOXO3 deacetylation to promote Lapatinib resistance.	lapatinib	29-38	sirtuin 2	Homo sapiens	194-199
31727006-6	2019	Western blot analysis of the Lapatinib-sensitive 6-10B and resistant 5-8F NPC cells showed that the expression of phosphorylated/inactive FOXO3 (P-FOXO3;T32), its target FOXM1 and its regulator SIRT2 correlate negatively with Lapatinib response and sensitivity, suggesting that SIRT2 mediates FOXO3 deacetylation to promote Lapatinib resistance.	lapatinib	29-38	sirtuin 2	Homo sapiens	278-283
31867164-7	2019	Thus, SIRT2 was used to modify substrates by truncating the amino acids or lysine side chain of nonapeptide.	tyrosyl-lysine	75-81	sirtuin 2	Homo sapiens	6-11
31561106-0	2019	Design, synthesis, in-vitro evaluation and molecular docking studies of novel indole derivatives as inhibitors of SIRT1 and SIRT2.	indole	78-84	sirtuin 2	Homo sapiens	124-129
31561106-3	2019	Compounds containing indole moiety are potential lead molecules inhibiting SIRT1 and SIRT2 activity.	indole	21-27	sirtuin 2	Homo sapiens	85-90
31561106-4	2019	In the current study, we have successfully synthesized 22 indole derivatives in association with an additional triazole moiety that provide better anchoring of the ligands in the binding cavity of SIRT1 and SIRT2.	indole	58-64	sirtuin 2	Homo sapiens	207-212
31561106-4	2019	In the current study, we have successfully synthesized 22 indole derivatives in association with an additional triazole moiety that provide better anchoring of the ligands in the binding cavity of SIRT1 and SIRT2.	Triazoles	111-119	sirtuin 2	Homo sapiens	207-212
31604796-1	2019	Sirtuin 2 (SIRT2) is an NAD-dependent sirtuin deacetylase that regulates microtubule and chromatin dynamics, gene expression and cell cycle progression, as well as nuclear envelope reassembly.	NAD	24-27	sirtuin 2	Homo sapiens	11-16
31366618-2	2019	Here, we demonstrate that LMO2 is activated by deacetylation on lysine 74 and 78 via the nicotinamide phosphoribosyltransferase (NAMPT)/sirtuin 2 (SIRT2) pathway.	Lysine	64-70	sirtuin 2	Homo sapiens	136-145
31553614-4	2019	In this investigation, we have made an attempt to unravel the unbinding pathways of nicotinamide from SIRT1, SIRT2, and SIRT3 (SIRT1-3) using Random Acceleration Molecular Dynamics (RAMD) Simulations, and we have successfully identified various unbinding channels.	Niacinamide	84-96	sirtuin 2	Homo sapiens	109-114
31366618-2	2019	Here, we demonstrate that LMO2 is activated by deacetylation on lysine 74 and 78 via the nicotinamide phosphoribosyltransferase (NAMPT)/sirtuin 2 (SIRT2) pathway.	Lysine	64-70	sirtuin 2	Homo sapiens	147-152
31762241-5	2019	And the influence of down-regulation of SIRT2 on cell proliferation and migration was investigated by MTT and Scratch test.	monooxyethylene trimethylolpropane tristearate	102-105	sirtuin 2	Homo sapiens	40-45
31433161-7	2019	The lysine acylation of RalB is regulated by SIRT2, a member of the sirtuin family of nicotinamide adenine dinucleotide (NAD)-dependent protein lysine deacylases.	Lysine	4-10	sirtuin 2	Homo sapiens	45-50
31433161-7	2019	The lysine acylation of RalB is regulated by SIRT2, a member of the sirtuin family of nicotinamide adenine dinucleotide (NAD)-dependent protein lysine deacylases.	NAD	86-119	sirtuin 2	Homo sapiens	45-50
31433161-7	2019	The lysine acylation of RalB is regulated by SIRT2, a member of the sirtuin family of nicotinamide adenine dinucleotide (NAD)-dependent protein lysine deacylases.	NAD	121-124	sirtuin 2	Homo sapiens	45-50
31422051-0	2019	Corrigendum to "MicroRNA-140-5p aggravates doxorubicin-induced cardiotoxicity by promoting myocardial oxidative stress via targeting Nrf2 and Sirt2" [Redox Biol.	Doxorubicin	43-54	sirtuin 2	Homo sapiens	142-147
31510043-0	2019	Antiproliferative S-Trityl-l-Cysteine -Derived Compounds as SIRT2 Inhibitors: Repurposing and Solubility Enhancement.	3-tritylthio-L-alanine	18-37	sirtuin 2	Homo sapiens	60-65
31510043-5	2019	We recently identified and characterized a new class of nicotinamide adenine dinucleotide-dependent deacetylase isoform 2 of sirtuin protein (SIRT2) inhibitors that can be utilized as cytotoxic agents based on an S-trityl-l-histidine scaffold.	NAD	56-89	sirtuin 2	Homo sapiens	142-147
31510043-5	2019	We recently identified and characterized a new class of nicotinamide adenine dinucleotide-dependent deacetylase isoform 2 of sirtuin protein (SIRT2) inhibitors that can be utilized as cytotoxic agents based on an S-trityl-l-histidine scaffold.	s-trityl-l-histidine	213-233	sirtuin 2	Homo sapiens	142-147
31762241-12	2019	MTT assay and Scratch test indicated that down-regulation of SIRT2 expression inhibited the proliferation and migration of HeLa cells (P < 0.05).	monooxyethylene trimethylolpropane tristearate	0-3	sirtuin 2	Homo sapiens	61-66
30579931-2	2019	Increasing evidence and our previous studies have shown that mammalian silent information regulator 2 homolog (SIRT1) is involved in periphery sensitization and central sensitization of BCP, and the underlying mechanism of SIRT1 in bone cancer pain may provide clues for pain treatment.	bcp	186-189	sirtuin 2	Homo sapiens	71-101
30933885-12	2019	We found that the SIRT2/cMYC pathway contributed to the proliferation of CCA cells and confirmed that the downstream target is PHDA1 and the serine synthesis pathway.	Serine	141-147	sirtuin 2	Homo sapiens	18-23
30933885-13	2019	The up-regulated SIRT2 and cMYC levels resulted in low levels of mitochondrial oxidative phosphorylation and increased conversion of glucose to serine and led to poor patient survival.	Glucose	133-140	sirtuin 2	Homo sapiens	17-22
30933885-13	2019	The up-regulated SIRT2 and cMYC levels resulted in low levels of mitochondrial oxidative phosphorylation and increased conversion of glucose to serine and led to poor patient survival.	Serine	144-150	sirtuin 2	Homo sapiens	17-22
30933885-14	2019	The highly active SIRT2/cMYC pathway up-regulated the serine synthesis pathway pyruvate and increased antioxidant production, thus consequently protecting the CCA cells from oxidative stress-induced apoptosis.	Serine	54-60	sirtuin 2	Homo sapiens	18-23
30933885-14	2019	The highly active SIRT2/cMYC pathway up-regulated the serine synthesis pathway pyruvate and increased antioxidant production, thus consequently protecting the CCA cells from oxidative stress-induced apoptosis.	Pyruvic Acid	79-87	sirtuin 2	Homo sapiens	18-23
30933885-15	2019	Our data revealed that the SIRT2/cMYC pathway plays a critical role in transforming glucose oxidative metabolism to serine anabolic metabolism, thus providing antioxidants for stress resistance.	Glucose	84-91	sirtuin 2	Homo sapiens	27-32
30933885-15	2019	Our data revealed that the SIRT2/cMYC pathway plays a critical role in transforming glucose oxidative metabolism to serine anabolic metabolism, thus providing antioxidants for stress resistance.	Serine	116-122	sirtuin 2	Homo sapiens	27-32
30352233-0	2019	Vincristine ablation of Sirt2 induces cell apoptosis and mitophagy via Hsp70 acetylation in MDA-MB-231 cells.	Vincristine	0-11	sirtuin 2	Homo sapiens	24-29
30352233-5	2019	In this study, we demonstrated that vincristine induces mitophagy via the disruption of Hsp70 binding with Sirt2, leading to Hsp70 acetylation at K126 and elevated sequestration of Bcl2 by Hsp70 for autophagosome creation.	Vincristine	36-47	sirtuin 2	Homo sapiens	107-112
30352233-9	2019	In conclusion, this study describes the molecular mechanism of vincristine induction of cell apoptosis and mitophagy via ablation of Sirt2 induced Hsp70 acetylation at K126 in MDA-MB-231 cells.	Vincristine	63-74	sirtuin 2	Homo sapiens	133-138
31357491-0	2019	Discovery of (5-Phenylfuran-2-yl)methanamine Derivatives as New Human Sirtuin 2 Inhibitors.	(5-phenylfuran-2-yl)methanamine	13-44	sirtuin 2	Homo sapiens	70-79
31357491-3	2019	Using previously established fluorescence-based assays for SIRT2 activity tests, the authors screened their in-house database and identified a compound, 4-(5-((3-(quinolin-5-yl)ureido)methyl)furan-2-yl)benzoic acid (20), which displayed 63 +- 5% and 35 +- 3% inhibition against SIRT2 at 100 muM and 10 muM, respectively.	4-(5-((3-(quinolin-5-yl)ureido)methyl)furan-2-yl)benzoic acid	153-214	sirtuin 2	Homo sapiens	59-64
31357491-3	2019	Using previously established fluorescence-based assays for SIRT2 activity tests, the authors screened their in-house database and identified a compound, 4-(5-((3-(quinolin-5-yl)ureido)methyl)furan-2-yl)benzoic acid (20), which displayed 63 +- 5% and 35 +- 3% inhibition against SIRT2 at 100 muM and 10 muM, respectively.	4-(5-((3-(quinolin-5-yl)ureido)methyl)furan-2-yl)benzoic acid	153-214	sirtuin 2	Homo sapiens	278-283
31324785-5	2019	Sirt2, which level peak in S phase, sustains RNR activity at or above a threshold level required for dNTPs synthesis.	Parathion	101-106	sirtuin 2	Homo sapiens	0-5
31324785-6	2019	We also find that radiation or camptothecin-induced DNA damage promotes RRM2 deacetylation by enhancing Sirt2-RRM2 interaction.	Camptothecin	31-43	sirtuin 2	Homo sapiens	104-109
31158122-9	2019	SIRT1, SIRT2, SIRT5, and SIRT7 gene expression could be upregulated by pretreatment with resveratrol compared with TNF-alpha alone while there were no obvious differences of SIRT3, SIRT4, and SIRT6 expressions observed in TNF-alpha alone treated cells and resveratrol-TNF-alpha co-treated cells.	Resveratrol	89-100	sirtuin 2	Homo sapiens	7-12
31158122-10	2019	Interestingly, SIRT1, SIRT2, SIRT3, SIRT4, and SIRT5 siRNA could reverse the effect of resveratrol on ROS production; SIRT1 and SIRT5 siRNA could significantly increase CD40 expression inhibited by resveratrol in TNF-a treated cells.	Resveratrol	87-98	sirtuin 2	Homo sapiens	22-27
31158122-10	2019	Interestingly, SIRT1, SIRT2, SIRT3, SIRT4, and SIRT5 siRNA could reverse the effect of resveratrol on ROS production; SIRT1 and SIRT5 siRNA could significantly increase CD40 expression inhibited by resveratrol in TNF-a treated cells.	Reactive Oxygen Species	102-105	sirtuin 2	Homo sapiens	22-27
31158122-11	2019	CONCLUSIONS Our results suggest that resveratrol inhibiting oxidative stress production is associated with SIRT1, SIRT2, SIRT3, SIRT4, and SIRT5 pathways; attenuating CD40 expression was only associated with SIRT1 and SIRT5 pathways in TNF-alpha-induced endothelial cells injury.	Resveratrol	37-48	sirtuin 2	Homo sapiens	114-119
31091806-0	2019	SIRT2 Contributes to the Resistance of Melanoma Cells to the Multikinase Inhibitor Dasatinib.	Dasatinib	83-92	sirtuin 2	Homo sapiens	0-5
31091806-5	2019	A detailed transcriptomic analysis showed that SIRT2 regulates the expression of multiple genes encoding the tyrosine kinase pathways that are molecular targets of dasatinib.	Dasatinib	164-173	sirtuin 2	Homo sapiens	47-52
31091806-6	2019	Indeed, cells with low SIRT2 expression were more susceptible to dasatinib, as demonstrated by multiple techniques, e.g., neutral red uptake, 3/7 caspase activity, colony formation assay, and in vitro scratch assay.	Dasatinib	65-74	sirtuin 2	Homo sapiens	23-28
30885568-0	2019	New SIRT2 inhibitors: Histidine-based bleomycin spin-off.	Histidine	22-31	sirtuin 2	Homo sapiens	4-9
30885568-0	2019	New SIRT2 inhibitors: Histidine-based bleomycin spin-off.	Bleomycin	38-47	sirtuin 2	Homo sapiens	4-9
30885568-3	2019	In this paper, we developed inhibitors of nicotinamide adenine dinucleotide-dependent deacetylase isoform 2 of Sirtuin protein (SIRT2), based on HPH-1Trt/HPH-2Trt, and aimed to generate new anti-cancer drugs.	NAD	42-75	sirtuin 2	Homo sapiens	128-133
30885568-7	2019	Selective binding of TH-3 in the pocket of SIRT2 protein was confirmed with a molecular docking study.	th-3	21-25	sirtuin 2	Homo sapiens	43-48
30811852-7	2019	We found that 2,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indole-3-carboxamides are potent and selective SIRT2 inhibitors.	2,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1h-indole-3-carboxamides	14-79	sirtuin 2	Homo sapiens	105-110
30734528-0	2019	A Small-Molecule SIRT2 Inhibitor That Promotes K-Ras4a Lysine Fatty-Acylation.	Lysine	55-61	sirtuin 2	Homo sapiens	17-22
30734528-3	2019	Among the SIRT2-specific inhibitors, only the thiomyristoyl lysine compound TM can weakly inhibit the demyristoylation activity of SIRT2.	thiomyristoyl lysine	46-66	sirtuin 2	Homo sapiens	10-15
30734528-3	2019	Among the SIRT2-specific inhibitors, only the thiomyristoyl lysine compound TM can weakly inhibit the demyristoylation activity of SIRT2.	thiomyristoyl lysine	46-66	sirtuin 2	Homo sapiens	131-136
30734528-5	2019	Herein we report a SIRT2 inhibitor, JH-T4, which can increase K-Ras4a lysine fatty acylation.	jh-t4	36-41	sirtuin 2	Homo sapiens	19-24
30734528-5	2019	Herein we report a SIRT2 inhibitor, JH-T4, which can increase K-Ras4a lysine fatty acylation.	Lysine	70-76	sirtuin 2	Homo sapiens	19-24
30998146-2	2019	METHODS: The expression of SIRT2 and antophagy-related protein LCT, P62 in HL-60/A and HL-60 was detected by Western blot, the effect of cytorabine on the apoptosis of HL-60/A cells was detected by using Annexin V/PI double staining after targeting inhibition of SIRT2 expression resulting from transfecting HL-60/A cells with SiRNA.	cytorabine	137-147	sirtuin 2	Homo sapiens	27-32
30841446-6	2019	2-Chloro-1,4-naphtoquinone-quercetin also showed potent inhibition against SIRT2, with an IC50 value of 14 muM.	2-chloro-1,4-naphtoquinone-quercetin	0-36	sirtuin 2	Homo sapiens	75-80
30203196-8	2019	To elucidate the mechanism of SIRT2 oxidation (specific modifications of redox-sensitive cysteines) and its effect on inflammation, we performed site-directed mutations of redox-sensitive cysteines Cys221 and Cys224 on SIRT2 to serine (C221S and C224S), transfected HEK293 cells with mutants or WT SIRT2, and studied SIRT2 enzymatic activity and NFkBp65 deacetylation.	Cysteine	89-98	sirtuin 2	Homo sapiens	30-35
30616888-2	2019	Sirtuin 2 (SIRT2) is an NAD-dependent deacetylase that regulates cellular response to oxidative stress, however, its role in NIHL remains poorly understood.	NAD	24-27	sirtuin 2	Homo sapiens	0-9
30616888-2	2019	Sirtuin 2 (SIRT2) is an NAD-dependent deacetylase that regulates cellular response to oxidative stress, however, its role in NIHL remains poorly understood.	NAD	24-27	sirtuin 2	Homo sapiens	11-16
30401720-5	2019	In the nucleus, E-cadherin was acetylated by CREB-binding protein at Lysine870 and Lysine871 in its beta-catenin-binding domain, and the acetylation can be reversed by SIRT2.	lysine870	69-78	sirtuin 2	Homo sapiens	168-173
30482390-2	2019	The present study identified a novel pathway of p53 accumulation by SIRT2 suppression in HCT116(p53+/+) cells in which SIRT2 suppression led to escape from mitotic cell death caused by spindle assembly checkpoint activation induced by microtubule inhibitors such as nocodazole but not apoptosis or G1 or G2 arrest.	Nocodazole	266-276	sirtuin 2	Homo sapiens	68-73
30482390-2	2019	The present study identified a novel pathway of p53 accumulation by SIRT2 suppression in HCT116(p53+/+) cells in which SIRT2 suppression led to escape from mitotic cell death caused by spindle assembly checkpoint activation induced by microtubule inhibitors such as nocodazole but not apoptosis or G1 or G2 arrest.	Nocodazole	266-276	sirtuin 2	Homo sapiens	119-124
30482390-6	2019	Thus, the P/CAF-MDM2-p53-p21 axis enables the escape from mitotic cell death and confers resistance to nocodazole in HCT116(p53+/+) cells with SIRT2 suppression.	Nocodazole	103-113	sirtuin 2	Homo sapiens	143-148
30203196-8	2019	To elucidate the mechanism of SIRT2 oxidation (specific modifications of redox-sensitive cysteines) and its effect on inflammation, we performed site-directed mutations of redox-sensitive cysteines Cys221 and Cys224 on SIRT2 to serine (C221S and C224S), transfected HEK293 cells with mutants or WT SIRT2, and studied SIRT2 enzymatic activity and NFkBp65 deacetylation.	Cysteine	188-197	sirtuin 2	Homo sapiens	30-35
30203196-8	2019	To elucidate the mechanism of SIRT2 oxidation (specific modifications of redox-sensitive cysteines) and its effect on inflammation, we performed site-directed mutations of redox-sensitive cysteines Cys221 and Cys224 on SIRT2 to serine (C221S and C224S), transfected HEK293 cells with mutants or WT SIRT2, and studied SIRT2 enzymatic activity and NFkBp65 deacetylation.	Cysteine	188-197	sirtuin 2	Homo sapiens	219-224
30203196-8	2019	To elucidate the mechanism of SIRT2 oxidation (specific modifications of redox-sensitive cysteines) and its effect on inflammation, we performed site-directed mutations of redox-sensitive cysteines Cys221 and Cys224 on SIRT2 to serine (C221S and C224S), transfected HEK293 cells with mutants or WT SIRT2, and studied SIRT2 enzymatic activity and NFkBp65 deacetylation.	Cysteine	188-197	sirtuin 2	Homo sapiens	219-224
30203196-8	2019	To elucidate the mechanism of SIRT2 oxidation (specific modifications of redox-sensitive cysteines) and its effect on inflammation, we performed site-directed mutations of redox-sensitive cysteines Cys221 and Cys224 on SIRT2 to serine (C221S and C224S), transfected HEK293 cells with mutants or WT SIRT2, and studied SIRT2 enzymatic activity and NFkBp65 deacetylation.	Cysteine	188-197	sirtuin 2	Homo sapiens	219-224
30203196-8	2019	To elucidate the mechanism of SIRT2 oxidation (specific modifications of redox-sensitive cysteines) and its effect on inflammation, we performed site-directed mutations of redox-sensitive cysteines Cys221 and Cys224 on SIRT2 to serine (C221S and C224S), transfected HEK293 cells with mutants or WT SIRT2, and studied SIRT2 enzymatic activity and NFkBp65 deacetylation.	Serine	228-234	sirtuin 2	Homo sapiens	30-35
30213795-5	2018	Furthermore, we demonstrate that SIRT2 regulates p73 transcriptional activity by deacetylation of its C-terminal lysine residues.	Lysine	113-119	sirtuin 2	Homo sapiens	33-38
31070532-9	2018	CONCLUSIONS: Simvastatin protects against APE-induced pulmonary artery pressure, hypoxemia and inflammatory changes probably due to the regulation of SIRT2/NF-kappaB signalling pathway, which suggest that simvastatin may have promising protective effects in patients with APE.	Simvastatin	13-24	sirtuin 2	Homo sapiens	150-155
31070532-9	2018	CONCLUSIONS: Simvastatin protects against APE-induced pulmonary artery pressure, hypoxemia and inflammatory changes probably due to the regulation of SIRT2/NF-kappaB signalling pathway, which suggest that simvastatin may have promising protective effects in patients with APE.	Simvastatin	205-216	sirtuin 2	Homo sapiens	150-155
30481203-14	2018	Pirfenidone also led to increased expression of HDAC6 and sirtuin-2, and enhanced alpha-tubulin-deacetylation.	pirfenidone	0-11	sirtuin 2	Homo sapiens	58-67
30424581-6	2018	Alcohol modifies SIRT1 (Sirtuin-1; derived from Silent mating type Information Regulation) and SIRT2, and most importantly, the innate and adapted immune systems, which may explain the individual differences of injury susceptibility.	Alcohols	0-7	sirtuin 2	Homo sapiens	95-100
29807072-2	2018	In mammalian systems, toxoflavin is an inhibitor of Wnt signaling as well as of SIRT1 and SIRT2 activities, but other molecular targets in mammalian cells have been scarcely studied.	toxoflavin	22-32	sirtuin 2	Homo sapiens	90-95
29685963-0	2018	New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2.	NAD	62-66	sirtuin 2	Homo sapiens	94-103
30568770-4	2018	Substrate activity assays indicated the resulting S-NAD+ is chemically inert to human CD38 and sirtuin 2 enzymes, but capable of participating in redox reactions in a manner similar to NAD+.	NAD	52-56	sirtuin 2	Homo sapiens	95-104
29449643-11	2018	Conversely, SIRT2 inhibition attenuates H2O2-mediated cell death in HeLa cells.	Hydrogen Peroxide	40-44	sirtuin 2	Homo sapiens	12-17
30154464-0	2018	Lysine benzoylation is a histone mark regulated by SIRT2.	Lysine	0-6	sirtuin 2	Homo sapiens	51-56
29423902-5	2018	RESULTS: A significantly higher accumulation of 12-[18F]DDAHA was observed in MCF-7 and MDA-MB-435 cells in vitro as compared to U87, MiaPaCa, and MCF10A, which was consistent with levels of SIRT2 expression.	12-[18f]ddaha	48-61	sirtuin 2	Homo sapiens	191-196
29423902-7	2018	CONCLUSIONS: The next generation of SIRT2-specific radiotracers resistant to systemic defluorination should be developed using alternative sites of radiofluorination on the aliphatic chain of DDAHA.	ddaha	192-197	sirtuin 2	Homo sapiens	36-41
29957526-1	2018	Human sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacylase, and is implicated in human diseases including cancer.	NAD	29-62	sirtuin 2	Homo sapiens	6-15
29957526-1	2018	Human sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacylase, and is implicated in human diseases including cancer.	NAD	29-62	sirtuin 2	Homo sapiens	17-22
29957526-1	2018	Human sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacylase, and is implicated in human diseases including cancer.	NAD	64-67	sirtuin 2	Homo sapiens	6-15
29957526-1	2018	Human sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacylase, and is implicated in human diseases including cancer.	NAD	64-67	sirtuin 2	Homo sapiens	17-22
29957526-3	2018	Here we report the X-ray crystal structure guided structure-activity relationship studies of new N-(3-(phenoxymethyl)phenyl)acetamide derivatives with SIRT2, which led to the identification of potent, selective SIRT2 inhibitors.	n-(3-(phenoxymethyl)phenyl)acetamide	97-133	sirtuin 2	Homo sapiens	151-156
29957526-3	2018	Here we report the X-ray crystal structure guided structure-activity relationship studies of new N-(3-(phenoxymethyl)phenyl)acetamide derivatives with SIRT2, which led to the identification of potent, selective SIRT2 inhibitors.	n-(3-(phenoxymethyl)phenyl)acetamide	97-133	sirtuin 2	Homo sapiens	211-216
30111572-2	2018	Here, we found that endogenous Sirt2 was upregulated in wild-type hepatitis B virus (HBV WT)-replicating cells, leading to tubulin deacetylation; however, this was not the case in HBV replication-deficient-mutant-transfected cells and 1.3-mer HBV WT-transfected and reverse transcriptase inhibitor (entecavir or lamivudine)-treated cells, but all HBV proteins were expressed.	entecavir	299-308	sirtuin 2	Homo sapiens	31-36
30111572-2	2018	Here, we found that endogenous Sirt2 was upregulated in wild-type hepatitis B virus (HBV WT)-replicating cells, leading to tubulin deacetylation; however, this was not the case in HBV replication-deficient-mutant-transfected cells and 1.3-mer HBV WT-transfected and reverse transcriptase inhibitor (entecavir or lamivudine)-treated cells, but all HBV proteins were expressed.	Lamivudine	312-322	sirtuin 2	Homo sapiens	31-36
30114477-3	2018	In this study, we provide evidence that NAD(P)H:quinone oxidoreductase 1 (NQO1) interacts with and activates SIRT2 in an NAD-dependent manner.	NAD	40-43	sirtuin 2	Homo sapiens	109-114
30275764-1	2018	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD +)-dependent class III histone deacetylase.	NAD	23-56	sirtuin 2	Homo sapiens	0-9
30275764-1	2018	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD +)-dependent class III histone deacetylase.	NAD	23-56	sirtuin 2	Homo sapiens	11-16
30275764-1	2018	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD +)-dependent class III histone deacetylase.	NAD	58-63	sirtuin 2	Homo sapiens	0-9
30275764-1	2018	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD +)-dependent class III histone deacetylase.	NAD	58-63	sirtuin 2	Homo sapiens	11-16
29685963-6	2018	Secondly, using click chemistry with a TAMRA-azide on a propargylated sirtuin inhibitor, we prepared the first fluorescently labelled small-molecule inhibitor of Sirt2.	TAMRA-azide	39-50	sirtuin 2	Homo sapiens	162-167
29685974-1	2018	SIRT2 is a member of the human sirtuin family of proteins and possesses NAD+-dependent lysine deacetylase/deacylase activity.	NAD	72-76	sirtuin 2	Homo sapiens	0-5
29685974-5	2018	Crystallographic analysis revealed a unique mode of action, in which NPD11033 creates a hydrophobic cavity behind the substrate-binding pocket after a conformational change of the Zn-binding small domain of SIRT2.	Zinc	180-182	sirtuin 2	Homo sapiens	207-212
29189925-0	2018	Overexpression of Sirtuin2 prevents high glucose-induced vascular endothelial cell injury by regulating the p53 and NF-kappaB signaling pathways.	Glucose	41-48	sirtuin 2	Homo sapiens	18-26
29625382-4	2018	Moreover, the past two years have witnessed remarkable advances in the development of phthalimide conjugation as a strategy for the degradation instead of inhibition of the targets, including BET family proteins, Sirtuin 2, CDK 9, Smad 3, and BCR-ABL proteins.	phthalimide	86-97	sirtuin 2	Homo sapiens	213-222
29724067-7	2018	Another chromenone compound, osthole, exhibited a moderate SIRT2 inhibitory activity with an IC50 of 10 muM.	coumarin	8-18	sirtuin 2	Homo sapiens	59-64
29724067-7	2018	Another chromenone compound, osthole, exhibited a moderate SIRT2 inhibitory activity with an IC50 of 10 muM.	osthol	29-36	sirtuin 2	Homo sapiens	59-64
29516351-5	2018	ATRA significantly decreased the nuclear to cytoplasmic ratio of SIRT1 and SIRT2.1, while sirtinol inhibited that of SIRT1, and TSA increased that of SIRT1 and SIRT2.1 during early differentiation.	Tretinoin	0-4	sirtuin 2	Homo sapiens	160-165
29516351-5	2018	ATRA significantly decreased the nuclear to cytoplasmic ratio of SIRT1 and SIRT2.1, while sirtinol inhibited that of SIRT1, and TSA increased that of SIRT1 and SIRT2.1 during early differentiation.	trichostatin A	128-131	sirtuin 2	Homo sapiens	160-165
29371109-3	2018	SIRT2, a member of NAD(+)-dependent class III deacetylases, is involved in genomic stability, metabolism, inflammation, oxidative stress and autophagy.	NAD	19-25	sirtuin 2	Homo sapiens	0-5
29371109-4	2018	In maintaining metabolic homeostasis, SIRT2 regulates adipocyte differentiation, fatty acid oxidation, gluconeogenesis, and insulin sensitivity.	Fatty Acids	81-91	sirtuin 2	Homo sapiens	38-43
29679549-7	2018	Our results indicated that CHM-1 increased the expression of SIRT2 protein, an NAD-dependent tubulin deacetylase.	NAD	79-82	sirtuin 2	Homo sapiens	61-66
29653431-0	2018	Inhibition of NAMPT sensitizes MOLT4 leukemia cells for etoposide treatment through the SIRT2-p53 pathway.	Etoposide	56-65	sirtuin 2	Homo sapiens	88-93
29653431-7	2018	After combining etoposide and FK866 treatment SIRTUIN2 was further decreased and accumulation and acetylation of the downstream target p53 was further enhanced in MOLT4 cells.	Etoposide	16-25	sirtuin 2	Homo sapiens	46-54
29653431-7	2018	After combining etoposide and FK866 treatment SIRTUIN2 was further decreased and accumulation and acetylation of the downstream target p53 was further enhanced in MOLT4 cells.	N-(4-(1-benzoylpiperidin-4-yl)butyl)-3-(pyridin-3-yl)acrylamide	30-35	sirtuin 2	Homo sapiens	46-54
29595201-5	2018	Moreover, acetylation of p53 K164 is reported to be deacetylated by SIRT2 for the first time.	5,6-dihydrothymine	29-33	sirtuin 2	Homo sapiens	68-73
29516351-5	2018	ATRA significantly decreased the nuclear to cytoplasmic ratio of SIRT1 and SIRT2.1, while sirtinol inhibited that of SIRT1, and TSA increased that of SIRT1 and SIRT2.1 during early differentiation.	Tretinoin	0-4	sirtuin 2	Homo sapiens	75-80
29189925-1	2018	OBJECTIVES: To investigate the potential role and underlying mechanism of Sirtuin2 (SIRT2) in regulating high glucose (HG)-induced vascular endothelial cell injury by using human umbilical vein endothelial cells (HUVECs).	Glucose	110-117	sirtuin 2	Homo sapiens	74-82
29189925-1	2018	OBJECTIVES: To investigate the potential role and underlying mechanism of Sirtuin2 (SIRT2) in regulating high glucose (HG)-induced vascular endothelial cell injury by using human umbilical vein endothelial cells (HUVECs).	Glucose	110-117	sirtuin 2	Homo sapiens	84-89
29189925-3	2018	SIRT2 overexpression increased viability, decreased apoptosis and reduced levels of reactive oxygen species in HG-treated HUVECs.	Reactive Oxygen Species	84-107	sirtuin 2	Homo sapiens	0-5
30562735-0	2018	miR-486-3p Influences the Neurotoxicity of a-Synuclein by Targeting the SIRT2 Gene and the Polymorphisms at Target Sites Contributing to Parkinson"s Disease.	mir-486-3p	0-10	sirtuin 2	Homo sapiens	72-77
28379698-1	2018	Here we report the development of a proteolysis targeting chimera (PROTAC) based on the combination of the unique features of the sirtuin rearranging ligands (SirReals) as highly potent and isotype-selective Sirt2 inhibitors with thalidomide, a bona fide cereblon ligand.	Thalidomide	230-241	sirtuin 2	Homo sapiens	208-213
29298345-7	2018	In untreated human cells, regions with high intensity immunostaining for NQO1 co-localize with acetyl alpha-tubulin and the NAD+-dependent deacetylase Sirt2 on the centrosome(s), the mitotic spindle and midbody during cell division.	NAD	124-128	sirtuin 2	Homo sapiens	151-156
29298345-8	2018	These data provide evidence that during the centriole duplication cycle NQO1 may provide NAD+ for Sirt2-mediated deacetylation of microtubules.	NAD	89-93	sirtuin 2	Homo sapiens	98-103
28168426-3	2018	We observed that NAD+ metabolism is altered in sporadic Parkinson"s disease patient-derived cells, which contributes to Sirtuin-2 activation and subsequent decrease in acetylated-alpha-tubulin levels.	NAD	17-21	sirtuin 2	Homo sapiens	120-129
30261494-11	2018	Compared to SIRT2- cells, SIRT2+ cells formed more tumor spheres, appeared to be more resistant towards fluorouracil-induced apoptosis, and generated bigger tumors with higher frequency after serial adoptive transplantation.	Fluorouracil	104-116	sirtuin 2	Homo sapiens	26-31
30562735-7	2018	MiR-486-3p mimics can decrease the level of SIRT2 and reduce a-synuclein (alpha-syn)-induced aggregation and toxicity, which may contribute to the progression of PD.	mir-486-3p	0-10	sirtuin 2	Homo sapiens	44-49
29239724-4	2017	Sirtuin 2 (SIRT2), one of the mammalian nicotinamide adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation from K-Ras4a.	NAD	40-73	sirtuin 2	Homo sapiens	0-9
30067423-0	2018	Dichloroacetic acid (DCA) synergizes with the SIRT2 inhibitor Sirtinol and AGK2 to enhance anti-tumor efficacy in non-small cell lung cancer.	sirtinol	62-70	sirtuin 2	Homo sapiens	46-51
30067423-2	2018	The current study investigates the antitumor activity of sodium dichloroacetic acid (DCA) in combination with SIRT2 inhibitor Sirtinol and AGK2.	sirtinol	126-134	sirtuin 2	Homo sapiens	110-115
29267359-6	2017	Using a bioinformatics approach, we searched the SRF binding motif in the SIRT2 gene, and found one classic CArG element (CCATAATAGG) in the SIRT2 gene promoter, which was bound to SRF in the electrophoretic mobility shift assay (EMSA).	carg	108-112	sirtuin 2	Homo sapiens	74-79
29267359-6	2017	Using a bioinformatics approach, we searched the SRF binding motif in the SIRT2 gene, and found one classic CArG element (CCATAATAGG) in the SIRT2 gene promoter, which was bound to SRF in the electrophoretic mobility shift assay (EMSA).	carg	108-112	sirtuin 2	Homo sapiens	141-146
29239724-4	2017	Sirtuin 2 (SIRT2), one of the mammalian nicotinamide adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation from K-Ras4a.	NAD	40-73	sirtuin 2	Homo sapiens	11-16
29239724-4	2017	Sirtuin 2 (SIRT2), one of the mammalian nicotinamide adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation from K-Ras4a.	NAD	75-78	sirtuin 2	Homo sapiens	0-9
29239724-4	2017	Sirtuin 2 (SIRT2), one of the mammalian nicotinamide adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation from K-Ras4a.	NAD	75-78	sirtuin 2	Homo sapiens	11-16
29239724-5	2017	We further demonstrate that SIRT2-mediated lysine defatty-acylation promotes endomembrane localization of K-Ras4a, enhances its interaction with A-Raf, and thus promotes cellular transformation.	Lysine	43-49	sirtuin 2	Homo sapiens	28-33
28949514-11	2017	Reduced SIRT2 expression and increased p300 activity lead to a concerted mechanism of hyperacetylation at specific histone lysine sites (H3K9, H3K14, and H3K18) in CRPC.	histone lysine	115-129	sirtuin 2	Homo sapiens	8-13
29125735-0	2017	Resveratrol Exerts Antioxidant Effects by Activating SIRT2 To Deacetylate Prx1.	Resveratrol	0-11	sirtuin 2	Homo sapiens	53-58
29125735-3	2017	Here we show that resveratrol activates SIRT2 to deacetylate Prx1, leading to an increased H2O2 reduction activity and a decreased cellular H2O2 concentration.	Resveratrol	18-29	sirtuin 2	Homo sapiens	40-45
29125735-3	2017	Here we show that resveratrol activates SIRT2 to deacetylate Prx1, leading to an increased H2O2 reduction activity and a decreased cellular H2O2 concentration.	Hydrogen Peroxide	91-95	sirtuin 2	Homo sapiens	40-45
29125735-3	2017	Here we show that resveratrol activates SIRT2 to deacetylate Prx1, leading to an increased H2O2 reduction activity and a decreased cellular H2O2 concentration.	Hydrogen Peroxide	140-144	sirtuin 2	Homo sapiens	40-45
29125735-4	2017	Knockdown of SIRT2 or Prx1 by RNA interference abrogates resveratrol"s ability to reduce the H2O2 level in HepG2 cells.	Resveratrol	57-68	sirtuin 2	Homo sapiens	13-18
29125735-4	2017	Knockdown of SIRT2 or Prx1 by RNA interference abrogates resveratrol"s ability to reduce the H2O2 level in HepG2 cells.	Hydrogen Peroxide	93-97	sirtuin 2	Homo sapiens	13-18
29125735-5	2017	Using purified SIRT2 and a Prx1 mutant harboring acetyllysine at position 27 (Prx1-27AcK), we show that resveratrol enhances SIRT2"s activity to deacetylate Prx1-27AcK, resulting in a significantly increased H2O2 reducing activity.	Resveratrol	104-115	sirtuin 2	Homo sapiens	15-20
29125735-5	2017	Using purified SIRT2 and a Prx1 mutant harboring acetyllysine at position 27 (Prx1-27AcK), we show that resveratrol enhances SIRT2"s activity to deacetylate Prx1-27AcK, resulting in a significantly increased H2O2 reducing activity.	Resveratrol	104-115	sirtuin 2	Homo sapiens	125-130
29125735-5	2017	Using purified SIRT2 and a Prx1 mutant harboring acetyllysine at position 27 (Prx1-27AcK), we show that resveratrol enhances SIRT2"s activity to deacetylate Prx1-27AcK, resulting in a significantly increased H2O2 reducing activity.	Hydrogen Peroxide	208-212	sirtuin 2	Homo sapiens	125-130
29213065-2	2017	The disordered microtubule associated Tubulin Polymerization Promoting Protein (TPPP/p25) and the NAD+-dependent tubulin deacetylase sirtuin-2 (SIRT2) play key roles in oligodendrocyte differentiation by acting as dominant factors in the organization of myelin proteome.	NAD	98-102	sirtuin 2	Homo sapiens	133-142
29213065-2	2017	The disordered microtubule associated Tubulin Polymerization Promoting Protein (TPPP/p25) and the NAD+-dependent tubulin deacetylase sirtuin-2 (SIRT2) play key roles in oligodendrocyte differentiation by acting as dominant factors in the organization of myelin proteome.	NAD	98-102	sirtuin 2	Homo sapiens	144-149
29213065-7	2017	We also revealed that a new potent SIRT2 inhibitor (MZ242) and its proteolysis targeting chimera (SH1) acting together with TPPP/p25 provoke microtubule hyperacetylation, which is coupled with process elongation only in the case of the degrader SH1.	mz242	52-57	sirtuin 2	Homo sapiens	35-40
28973648-0	2017	The NAD+-dependent deacetylase SIRT2 attenuates oxidative stress and mitochondrial dysfunction and improves insulin sensitivity in hepatocytes.	NAD	4-8	sirtuin 2	Homo sapiens	31-36
28973648-5	2017	Here, we show that SIRT2 is downregulated in insulin-resistant hepatocytes and livers, and this was accompanied by increased generation of reactive oxygen species, activation of stress-sensitive ERK1/2 kinase, and mitochondrial dysfunction.	Reactive Oxygen Species	139-162	sirtuin 2	Homo sapiens	19-24
28973648-6	2017	Conversely, SIRT2 overexpression in insulin-resistant hepatocytes improved insulin sensitivity, mitigated reactive oxygen species production and ameliorated mitochondrial dysfunction.	Reactive Oxygen Species	106-129	sirtuin 2	Homo sapiens	12-17
28506746-0	2017	The NAD+-dependent deacetylase, Bifidobacterium longum Sir2 in response to oxidative stress by deacetylating SigH (sigmaH) and FOXO3a in Bifidobacterium longum and HEK293T cell respectively.	NAD	4-7	sirtuin 2	Homo sapiens	55-59
28989670-0	2017	Potent mechanism-based sirtuin-2-selective inhibition by an in situ-generated occupant of the substrate-binding site, "selectivity pocket" and NAD+-binding site.	NAD	143-147	sirtuin 2	Homo sapiens	23-32
28989670-1	2017	Sirtuin 2 (SIRT2), a member of the NAD+-dependent histone deacetylase family, has recently received increasing attention due to its potential involvement in neurodegenerative diseases and the progression of cancer.	NAD	35-38	sirtuin 2	Homo sapiens	0-9
28989670-1	2017	Sirtuin 2 (SIRT2), a member of the NAD+-dependent histone deacetylase family, has recently received increasing attention due to its potential involvement in neurodegenerative diseases and the progression of cancer.	NAD	35-38	sirtuin 2	Homo sapiens	11-16
28989670-4	2017	Compound 36 engages in a nucleophilic attack toward NAD+ at the active site of SIRT2, which affords a stable 36-ADP-ribose conjugate that simultaneously occupies the substrate-binding site, the "selectivity pocket" and the NAD+-binding site.	NAD	52-56	sirtuin 2	Homo sapiens	79-84
28989670-4	2017	Compound 36 engages in a nucleophilic attack toward NAD+ at the active site of SIRT2, which affords a stable 36-ADP-ribose conjugate that simultaneously occupies the substrate-binding site, the "selectivity pocket" and the NAD+-binding site.	36-adp-ribose	109-122	sirtuin 2	Homo sapiens	79-84
28989670-4	2017	Compound 36 engages in a nucleophilic attack toward NAD+ at the active site of SIRT2, which affords a stable 36-ADP-ribose conjugate that simultaneously occupies the substrate-binding site, the "selectivity pocket" and the NAD+-binding site.	NAD	223-227	sirtuin 2	Homo sapiens	79-84
28456446-3	2017	Our lab recently reported that the hormone of lactation, prolactin, helps the retinal pigment epithelium to survive via antioxidant actions that result in the inhibition of sirtuin2-dependent cell death (EbioMedicine issue of May).	ebiomedicine	204-216	sirtuin 2	Homo sapiens	173-181
28396174-1	2017	Sirtuin3 (Sirt3) is a member of the silent information regulator 2 (Sir2) family of proteins located in mitochondria that influences almost every major aspect of mitochondrial biology, including ATP generation and reactive oxygen species (ROS) production.	Adenosine Triphosphate	195-198	sirtuin 2	Homo sapiens	36-66
28396174-1	2017	Sirtuin3 (Sirt3) is a member of the silent information regulator 2 (Sir2) family of proteins located in mitochondria that influences almost every major aspect of mitochondrial biology, including ATP generation and reactive oxygen species (ROS) production.	Adenosine Triphosphate	195-198	sirtuin 2	Homo sapiens	68-72
28396174-1	2017	Sirtuin3 (Sirt3) is a member of the silent information regulator 2 (Sir2) family of proteins located in mitochondria that influences almost every major aspect of mitochondrial biology, including ATP generation and reactive oxygen species (ROS) production.	Reactive Oxygen Species	214-237	sirtuin 2	Homo sapiens	36-66
28396174-1	2017	Sirtuin3 (Sirt3) is a member of the silent information regulator 2 (Sir2) family of proteins located in mitochondria that influences almost every major aspect of mitochondrial biology, including ATP generation and reactive oxygen species (ROS) production.	Reactive Oxygen Species	214-237	sirtuin 2	Homo sapiens	68-72
28396174-1	2017	Sirtuin3 (Sirt3) is a member of the silent information regulator 2 (Sir2) family of proteins located in mitochondria that influences almost every major aspect of mitochondrial biology, including ATP generation and reactive oxygen species (ROS) production.	Reactive Oxygen Species	239-242	sirtuin 2	Homo sapiens	36-66
28396174-1	2017	Sirtuin3 (Sirt3) is a member of the silent information regulator 2 (Sir2) family of proteins located in mitochondria that influences almost every major aspect of mitochondrial biology, including ATP generation and reactive oxygen species (ROS) production.	Reactive Oxygen Species	239-242	sirtuin 2	Homo sapiens	68-72
28805748-0	2017	Synthesis and Evaluation of Novel Benzofuran Derivatives as Selective SIRT2 Inhibitors.	benzofuran	34-44	sirtuin 2	Homo sapiens	70-75
28805748-4	2017	The results of this research could provide informative guidance for further optimizing benzofuran derivatives as potent SIRT2 inhibitors.	benzofuran	87-97	sirtuin 2	Homo sapiens	120-125
28415012-0	2017	Discovery of 2-((4,6-dimethylpyrimidin-2-yl)thio)-N-phenylacetamide derivatives as new potent and selective human sirtuin 2 inhibitors.	2-((4,6-dimethylpyrimidin-2-yl)thio)-n-phenylacetamide	13-67	sirtuin 2	Homo sapiens	114-123
28415012-4	2017	Herein, a structure-based optimization approach led to new 2-((4,6-dimethylpyrimidin-2-yl)thio)-N-phenylacetamide derivatives as SIRT2 inhibitors.	2-((4,6-dimethylpyrimidin-2-yl)thio)-n-phenylacetamide	59-113	sirtuin 2	Homo sapiens	129-134
28506746-1	2017	Silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation.	NAD	61-64	sirtuin 2	Homo sapiens	32-36
28506746-5	2017	To this end, we knockout BL-sir2(sir2 B. longum) and LA-sir2(sir2 L.acidophilus) in low oxygen level.	Oxygen	88-94	sirtuin 2	Homo sapiens	28-32
28506746-11	2017	Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and reduced reactive oxygen species(ROS).	Hydrogen Peroxide	34-38	sirtuin 2	Homo sapiens	24-28
28506746-11	2017	Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and reduced reactive oxygen species(ROS).	Hydrogen Peroxide	34-38	sirtuin 2	Homo sapiens	82-86
28506746-11	2017	Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and reduced reactive oxygen species(ROS).	Reactive Oxygen Species	188-211	sirtuin 2	Homo sapiens	24-28
28506746-11	2017	Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and reduced reactive oxygen species(ROS).	Reactive Oxygen Species	188-211	sirtuin 2	Homo sapiens	82-86
28506746-11	2017	Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and reduced reactive oxygen species(ROS).	Reactive Oxygen Species	212-215	sirtuin 2	Homo sapiens	24-28
28506746-11	2017	Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and reduced reactive oxygen species(ROS).	Reactive Oxygen Species	212-215	sirtuin 2	Homo sapiens	82-86
28240897-0	2017	Development of 1,2,4-Oxadiazoles as Potent and Selective Inhibitors of the Human Deacetylase Sirtuin 2: Structure-Activity Relationship, X-ray Crystal Structure, and Anticancer Activity.	1,2,4-oxadiazoles	15-32	sirtuin 2	Homo sapiens	93-102
28808418-3	2017	Sirtuins are a group of conserved nicotinamide adenine dinucleotide (NAD+) dependent histone and/or protein deacetylases belonging to the silent information regulator 2 (Sir2) family.	NAD	34-67	sirtuin 2	Homo sapiens	138-168
28808418-3	2017	Sirtuins are a group of conserved nicotinamide adenine dinucleotide (NAD+) dependent histone and/or protein deacetylases belonging to the silent information regulator 2 (Sir2) family.	NAD	34-67	sirtuin 2	Homo sapiens	170-174
28808418-3	2017	Sirtuins are a group of conserved nicotinamide adenine dinucleotide (NAD+) dependent histone and/or protein deacetylases belonging to the silent information regulator 2 (Sir2) family.	NAD	69-72	sirtuin 2	Homo sapiens	138-168
28808418-3	2017	Sirtuins are a group of conserved nicotinamide adenine dinucleotide (NAD+) dependent histone and/or protein deacetylases belonging to the silent information regulator 2 (Sir2) family.	NAD	69-72	sirtuin 2	Homo sapiens	170-174
28445509-5	2017	SIRT2 is a member of sirtuin family, NAD(+)-dependent class III deacetylases.	NAD	37-43	sirtuin 2	Homo sapiens	0-5
28301150-1	2017	SIRT2, which is a NAD+ (nicotinamide adenine dinucleotide) dependent deacetylase, has been demonstrated to play an important role in the occurrence and development of a variety of diseases such as cancer, ischemia-reperfusion, and neurodegenerative diseases.	NAD	18-22	sirtuin 2	Homo sapiens	0-5
28240897-2	2017	Here we report a series of Sirt2 inhibitors based on the 1,2,4-oxadiazole scaffold.	1,2,4-Oxadiazole	57-73	sirtuin 2	Homo sapiens	27-32
28240897-4	2017	Their mechanism of inhibition is uncompetitive toward both the peptide substrate and NAD+, and the crystal structure of a 1,2,4-oxadiazole analog in complex with Sirt2 and ADP-ribose reveals its orientation in a still unexplored subcavity useful for further inhibitor development.	NAD	85-89	sirtuin 2	Homo sapiens	162-167
28240897-4	2017	Their mechanism of inhibition is uncompetitive toward both the peptide substrate and NAD+, and the crystal structure of a 1,2,4-oxadiazole analog in complex with Sirt2 and ADP-ribose reveals its orientation in a still unexplored subcavity useful for further inhibitor development.	1,2,4-Oxadiazole	122-138	sirtuin 2	Homo sapiens	162-167
28053092-2	2017	We previously reported that the inhibition of the NAD-dependent histone deacetylase (HDAC) SIRT2 induces granulocytic differentiation in leukemia cells, suggesting the involvement of protein acetylation in ATRA-induced leukemia cell differentiation.	NAD	50-53	sirtuin 2	Homo sapiens	91-96
28286128-0	2017	Deacylation Mechanism by SIRT2 Revealed in the 1"-SH-2"-O-Myristoyl Intermediate Structure.	1"-sh-2"-o-myristoyl	47-67	sirtuin 2	Homo sapiens	25-30
28286128-4	2017	Based on potent SIRT2-specific inhibitors we developed, here we report crystal structures of SIRT2 in complexes with a thiomyristoyl lysine peptide-based inhibitor and carba-NAD or NAD.	carbanicotinamide adenine dinucleotide	168-177	sirtuin 2	Homo sapiens	16-21
28286128-4	2017	Based on potent SIRT2-specific inhibitors we developed, here we report crystal structures of SIRT2 in complexes with a thiomyristoyl lysine peptide-based inhibitor and carba-NAD or NAD.	carbanicotinamide adenine dinucleotide	168-177	sirtuin 2	Homo sapiens	93-98
28286128-4	2017	Based on potent SIRT2-specific inhibitors we developed, here we report crystal structures of SIRT2 in complexes with a thiomyristoyl lysine peptide-based inhibitor and carba-NAD or NAD.	NAD	174-177	sirtuin 2	Homo sapiens	16-21
28286128-4	2017	Based on potent SIRT2-specific inhibitors we developed, here we report crystal structures of SIRT2 in complexes with a thiomyristoyl lysine peptide-based inhibitor and carba-NAD or NAD.	NAD	174-177	sirtuin 2	Homo sapiens	93-98
28135086-0	2017	Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.	THIENOPYRIMIDINONE	0-18	sirtuin 2	Homo sapiens	25-34
28135086-0	2017	Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.	THIENOPYRIMIDINONE	0-18	sirtuin 2	Homo sapiens	36-41
28135086-2	2017	Previously, we reported a novel thienopyrimidinone SIRT2 inhibitor with good potency and excellent selectivity for SIRT2.	THIENOPYRIMIDINONE	32-50	sirtuin 2	Homo sapiens	51-56
28135086-2	2017	Previously, we reported a novel thienopyrimidinone SIRT2 inhibitor with good potency and excellent selectivity for SIRT2.	THIENOPYRIMIDINONE	32-50	sirtuin 2	Homo sapiens	115-120
28127057-0	2017	Sirtinol promotes PEPCK1 degradation and inhibits gluconeogenesis by inhibiting deacetylase SIRT2.	sirtinol	0-8	sirtuin 2	Homo sapiens	92-97
28127057-3	2017	In this study, we investigated the anti-diabetic effects of sirtinol, a SIRT2 inhibitor, on cell gluconeogenesis in vivo and in vitro.	sirtinol	60-68	sirtuin 2	Homo sapiens	72-77
28127057-8	2017	Thus, SIRT2 may be a novel molecular target for diabetes therapy and may thus shed light on the underlying diabetes treatment mechanisms of sirtinol.	sirtinol	140-148	sirtuin 2	Homo sapiens	6-11
28088387-3	2017	This study aims to assess the effects of shikonin on the development and metastatic progression of colorectal cancer (CRC) through regulation of SIRT2 expression and whether this effect is related to the phosphorylation of extracellular signal-regulated kinases (ERKs).	shikonin	41-49	sirtuin 2	Homo sapiens	145-150
28053092-2	2017	We previously reported that the inhibition of the NAD-dependent histone deacetylase (HDAC) SIRT2 induces granulocytic differentiation in leukemia cells, suggesting the involvement of protein acetylation in ATRA-induced leukemia cell differentiation.	Tretinoin	206-210	sirtuin 2	Homo sapiens	91-96
28073696-1	2017	SIRT2 is a NAD-dependent deacetylase and inhibition of SIRT2 has a broad anticancer activity.	NAD	11-14	sirtuin 2	Homo sapiens	0-5
28103679-0	2017	Histone Ketoamide Adduction by 4-Oxo-2-nonenal Is a Reversible Posttranslational Modification Regulated by Sirt2.	histone ketoamide	0-17	sirtuin 2	Homo sapiens	107-112
28103679-0	2017	Histone Ketoamide Adduction by 4-Oxo-2-nonenal Is a Reversible Posttranslational Modification Regulated by Sirt2.	4-oxo-2-nonenal	31-46	sirtuin 2	Homo sapiens	107-112
28103679-6	2017	Among the tested human sirtuins, Sirt2 showed robust deacylase activity toward the Kgon-carrying histone peptides in vitro.	histone peptides	97-113	sirtuin 2	Homo sapiens	33-38
28103679-7	2017	We use alkynyl-4-ONE as a chemical reporter for Kgon to demonstrate that Sirt2 is responsible for removing histone Kgon in cells.	alkynyl-4-one	7-20	sirtuin 2	Homo sapiens	73-78
28073696-2	2017	Here we report that SPOP binds to SIRT2 and mediates its degradation by the 26S proteasome, which can be blocked by MG132 treatment.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	116-121	sirtuin 2	Homo sapiens	34-39
28634568-4	2017	SH-SY5Y viability in response to oxidative stress induced by diquat or rotenone was measured following SIRT2 overexpression or inhibition of deacetylase activity, along with alpha-synuclein aggregation.	Rotenone	71-79	sirtuin 2	Homo sapiens	103-108
28634568-6	2017	In SH-SY5Y cells, elevated SIRT2 protected cells from rotenone or diquat induced cell death and enzymatic inhibition of SIRT2 enhanced cell death.	Rotenone	54-62	sirtuin 2	Homo sapiens	27-32
28634568-6	2017	In SH-SY5Y cells, elevated SIRT2 protected cells from rotenone or diquat induced cell death and enzymatic inhibition of SIRT2 enhanced cell death.	Diquat	66-72	sirtuin 2	Homo sapiens	27-32
27875273-1	2016	Sirtuin 2 (SIRT2) is an NAD-dependent deacetylase known to regulate microtubule dynamics and cell cycle progression.	NAD	24-27	sirtuin 2	Homo sapiens	0-9
27875273-1	2016	Sirtuin 2 (SIRT2) is an NAD-dependent deacetylase known to regulate microtubule dynamics and cell cycle progression.	NAD	24-27	sirtuin 2	Homo sapiens	11-16
27933951-1	2016	Photoaffinity labeling (PAL) was used to identify the binding site of chroman-4-one-based SIRT2-selective inhibitors.	4-Chromanone	70-83	sirtuin 2	Homo sapiens	90-95
27933951-2	2016	The photoactive diazirine 4, a potent SIRT2 inhibitor, was subjected to detailed photochemical characterization.	diazirine 4	16-27	sirtuin 2	Homo sapiens	38-43
27933951-3	2016	In PAL experiments with SIRT2, a tryptic peptide originating from the covalent attachment of photoactivated 4 was identified.	Peptides	41-48	sirtuin 2	Homo sapiens	24-29
27586085-0	2016	SIRT2 activates G6PD to enhance NADPH production and promote leukaemia cell proliferation.	NADP	32-37	sirtuin 2	Homo sapiens	0-5
27793977-0	2016	Acute stimulation of glucose influx upon mitoenergetic dysfunction requires LKB1, AMPK, Sirt2 and mTOR-RAPTOR.	Glucose	21-28	sirtuin 2	Homo sapiens	88-93
27793977-7	2016	Stimulation of glucose uptake was greatly reduced by chemical inhibition of Sirt2 or mTOR-RAPTOR.	Glucose	15-22	sirtuin 2	Homo sapiens	76-81
27793977-8	2016	We propose that mitochondrial dysfunction triggers LKB1-mediated AMPK activation, which stimulates Sirt2 phosphorylation, leading to activation of mTOR-RAPTOR and Glut1-mediated glucose uptake.	Glucose	178-185	sirtuin 2	Homo sapiens	99-104
27785339-5	2016	Our FACS-based Annexin V/7-AAD assay and Hoechst staining showed that both SIRT2 inhibitor and SIRT2 siRNA led to a significant increase in apoptosis and necrosis of the cells.	7-aminoactinomycin D	25-30	sirtuin 2	Homo sapiens	75-80
27785339-5	2016	Our FACS-based Annexin V/7-AAD assay and Hoechst staining showed that both SIRT2 inhibitor and SIRT2 siRNA led to a significant increase in apoptosis and necrosis of the cells.	7-aminoactinomycin D	25-30	sirtuin 2	Homo sapiens	95-100
27785339-5	2016	Our FACS-based Annexin V/7-AAD assay and Hoechst staining showed that both SIRT2 inhibitor and SIRT2 siRNA led to a significant increase in apoptosis and necrosis of the cells.	hoechst	41-48	sirtuin 2	Homo sapiens	75-80
27785339-5	2016	Our FACS-based Annexin V/7-AAD assay and Hoechst staining showed that both SIRT2 inhibitor and SIRT2 siRNA led to a significant increase in apoptosis and necrosis of the cells.	hoechst	41-48	sirtuin 2	Homo sapiens	95-100
27785339-6	2016	Moreover, the SIRT2 inhibition led to both mitochondrial depolarization and decreases in the intracellular ATP level of the cells.	Adenosine Triphosphate	107-110	sirtuin 2	Homo sapiens	14-19
27785339-7	2016	Collectively, our study has provided the first evidence suggesting that SIRT2 plays a significant role in maintaining both the survival and the mitochondrial membrane potential of PIEC cells, which may account for the major effects of SIRT2 on the intracellular ATP level of the cells.	Adenosine Triphosphate	262-265	sirtuin 2	Homo sapiens	72-77
27785339-7	2016	Collectively, our study has provided the first evidence suggesting that SIRT2 plays a significant role in maintaining both the survival and the mitochondrial membrane potential of PIEC cells, which may account for the major effects of SIRT2 on the intracellular ATP level of the cells.	Adenosine Triphosphate	262-265	sirtuin 2	Homo sapiens	235-240
27610633-0	2016	SIRT2 Reverses 4-Oxononanoyl Lysine Modification on Histones.	Nepsilon	15-35	sirtuin 2	Homo sapiens	0-5
27610633-4	2016	Here, we report that mammalian SIRT2 can remove 4-ONyl from histones and other proteins in live cells.	4-onyl	48-54	sirtuin 2	Homo sapiens	31-36
27610633-5	2016	A crystal structure of SIRT2 in complex with a 4-ONyl peptide reveals a lone pair-pi interaction between Phe119 and the ketone oxygen of the 4-ONyl group.	Ketones	120-126	sirtuin 2	Homo sapiens	23-28
27610633-5	2016	A crystal structure of SIRT2 in complex with a 4-ONyl peptide reveals a lone pair-pi interaction between Phe119 and the ketone oxygen of the 4-ONyl group.	Oxygen	127-133	sirtuin 2	Homo sapiens	23-28
27610633-6	2016	This is the first time that a mechanism to reverse 4-ONyl lysine modification is reported and will help to understand the role of SIRT2 in oxidative stress responses and the function of 4-ONylation.	4-onyl lysine	51-64	sirtuin 2	Homo sapiens	130-135
27909079-0	2016	AMPK and Sirt2 control compensatory glucose uptake.	Glucose	36-43	sirtuin 2	Homo sapiens	9-14
27783945-5	2016	We show that SIRT2 deacetylates Slug protein at lysine residue K116 to prevent Slug degradation.	Lysine	48-54	sirtuin 2	Homo sapiens	13-18
27783945-5	2016	We show that SIRT2 deacetylates Slug protein at lysine residue K116 to prevent Slug degradation.	cis-2-(2,4-Dichlorophenyl)-2-(1H-1,2,4-triazol-1-ylmethyl)-1,3-dioxolane-4-methanol methanesulfonate	63-67	sirtuin 2	Homo sapiens	13-18
27586085-7	2016	Deacetylase SIRT2 promotes NADPH production through deacetylating G6PD at lysine 403 (K403).	NADP	27-32	sirtuin 2	Homo sapiens	12-17
27586085-7	2016	Deacetylase SIRT2 promotes NADPH production through deacetylating G6PD at lysine 403 (K403).	Lysine	74-80	sirtuin 2	Homo sapiens	12-17
27725455-1	2016	SIRT2 is a member of the human sirtuin family of proteins and possesses nicotinamide adenine dinucleotide (NAD)-dependent lysine deacetylase activity.	NAD	72-105	sirtuin 2	Homo sapiens	0-5
27311481-1	2016	Deacetylation of alpha-tubulin at lysine 40 is catalyzed by two enzymes, the NAD-dependent deacetylase SIRT2 and the NAD-independent deacetylase HDAC6, in apparently redundant reactions.	Lysine	34-40	sirtuin 2	Homo sapiens	103-108
27311481-1	2016	Deacetylation of alpha-tubulin at lysine 40 is catalyzed by two enzymes, the NAD-dependent deacetylase SIRT2 and the NAD-independent deacetylase HDAC6, in apparently redundant reactions.	NAD	77-80	sirtuin 2	Homo sapiens	103-108
27311481-1	2016	Deacetylation of alpha-tubulin at lysine 40 is catalyzed by two enzymes, the NAD-dependent deacetylase SIRT2 and the NAD-independent deacetylase HDAC6, in apparently redundant reactions.	NAD	117-120	sirtuin 2	Homo sapiens	103-108
27311481-6	2016	By contrast, SIRT2 and HDAC6 acted similarly on the morphologically different, hyperacetylated microtubule structures induced by taxol, MAP2c overexpression or hyperosmotic stress.	Paclitaxel	129-134	sirtuin 2	Homo sapiens	13-18
26820517-2	2016	Sirtuin 1 (SIRT1) and sirtuin 2 (SIRT2) are NAD(+)-dependent histone deacetylases that operate as post-translational regulators for the deacetylation of acetyllysine.	N-epsilon-Acetyl-L-lysine	153-165	sirtuin 2	Homo sapiens	22-31
26820517-2	2016	Sirtuin 1 (SIRT1) and sirtuin 2 (SIRT2) are NAD(+)-dependent histone deacetylases that operate as post-translational regulators for the deacetylation of acetyllysine.	N-epsilon-Acetyl-L-lysine	153-165	sirtuin 2	Homo sapiens	33-38
26986569-0	2016	Finding Potent Sirt Inhibitor in Coffee: Isolation, Confirmation and Synthesis of Javamide-II (N-Caffeoyltryptophan) as Sirt1/2 Inhibitor.	javamide-ii	82-93	sirtuin 2	Homo sapiens	120-127
26986569-0	2016	Finding Potent Sirt Inhibitor in Coffee: Isolation, Confirmation and Synthesis of Javamide-II (N-Caffeoyltryptophan) as Sirt1/2 Inhibitor.	N-Caffeoyltryptophan	95-115	sirtuin 2	Homo sapiens	120-127
26986569-10	2016	The amide exhibited noncompetitive Sirt2 inhibition against the NAD+ (Ki = 9.8 muM) and showed competitive inhibition against the peptide substrate (Ki = 5.3 muM).	Amides	4-9	sirtuin 2	Homo sapiens	35-40
26986569-10	2016	The amide exhibited noncompetitive Sirt2 inhibition against the NAD+ (Ki = 9.8 muM) and showed competitive inhibition against the peptide substrate (Ki = 5.3 muM).	NAD	64-68	sirtuin 2	Homo sapiens	35-40
26977881-2	2016	We have developed a thiomyristoyl lysine compound, TM, as a potent SIRT2-specific inhibitor with a broad anticancer effect in various human cancer cells and mouse models of breast cancer.	thiomyristoyl lysine	20-40	sirtuin 2	Homo sapiens	67-72
26518726-4	2016	We report here that while the activities of the four human sirtuin isoforms SIRT1, SIRT2, SIRT3 and SIRT6 are blocked by sirtuin inhibitor Ex527 in vitro, they are unaffected by the seven clinical and commonly used PARP inhibitors niraparib, olaparib, rucaparib, talazoparib, veliparib, PJ34, and XAV939.	niraparib	231-240	sirtuin 2	Homo sapiens	83-88
26518726-4	2016	We report here that while the activities of the four human sirtuin isoforms SIRT1, SIRT2, SIRT3 and SIRT6 are blocked by sirtuin inhibitor Ex527 in vitro, they are unaffected by the seven clinical and commonly used PARP inhibitors niraparib, olaparib, rucaparib, talazoparib, veliparib, PJ34, and XAV939.	olaparib	242-250	sirtuin 2	Homo sapiens	83-88
26518726-4	2016	We report here that while the activities of the four human sirtuin isoforms SIRT1, SIRT2, SIRT3 and SIRT6 are blocked by sirtuin inhibitor Ex527 in vitro, they are unaffected by the seven clinical and commonly used PARP inhibitors niraparib, olaparib, rucaparib, talazoparib, veliparib, PJ34, and XAV939.	rucaparib	252-261	sirtuin 2	Homo sapiens	83-88
26518726-4	2016	We report here that while the activities of the four human sirtuin isoforms SIRT1, SIRT2, SIRT3 and SIRT6 are blocked by sirtuin inhibitor Ex527 in vitro, they are unaffected by the seven clinical and commonly used PARP inhibitors niraparib, olaparib, rucaparib, talazoparib, veliparib, PJ34, and XAV939.	talazoparib	263-274	sirtuin 2	Homo sapiens	83-88
26518726-4	2016	We report here that while the activities of the four human sirtuin isoforms SIRT1, SIRT2, SIRT3 and SIRT6 are blocked by sirtuin inhibitor Ex527 in vitro, they are unaffected by the seven clinical and commonly used PARP inhibitors niraparib, olaparib, rucaparib, talazoparib, veliparib, PJ34, and XAV939.	veliparib	276-285	sirtuin 2	Homo sapiens	83-88
26518726-4	2016	We report here that while the activities of the four human sirtuin isoforms SIRT1, SIRT2, SIRT3 and SIRT6 are blocked by sirtuin inhibitor Ex527 in vitro, they are unaffected by the seven clinical and commonly used PARP inhibitors niraparib, olaparib, rucaparib, talazoparib, veliparib, PJ34, and XAV939.	XAV939	297-303	sirtuin 2	Homo sapiens	83-88
27291931-1	2016	SIRT2 is a member of the NAD+ dependent deacetylases.	NAD	25-28	sirtuin 2	Homo sapiens	0-5
27322457-5	2016	It also blocks the hydrogen peroxide-induced increase in deacetylase sirtuin 2 (SIRT2) expression, which inhibits the TRPM2-mediated intracellular Ca(2+) rise associated with reduced survival under oxidant conditions.	Hydrogen Peroxide	19-36	sirtuin 2	Homo sapiens	69-78
27322457-5	2016	It also blocks the hydrogen peroxide-induced increase in deacetylase sirtuin 2 (SIRT2) expression, which inhibits the TRPM2-mediated intracellular Ca(2+) rise associated with reduced survival under oxidant conditions.	Hydrogen Peroxide	19-36	sirtuin 2	Homo sapiens	80-85
26982234-0	2016	5-((3-Amidobenzyl)oxy)nicotinamides as Sirtuin 2 Inhibitors.	5-((3-amidobenzyl)oxy)nicotinamides	0-35	sirtuin 2	Homo sapiens	39-48
26982234-1	2016	Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-aminonaphthalen-1-yloxy nicotinamide core structure, 5-((3-amidobenzyl)oxy)nicotinamides offered excellent activity against SIRT2 and high isozyme selectivity over SIRT1 and SIRT3.	5-aminonaphthalen-1-yloxy nicotinamide	93-131	sirtuin 2	Homo sapiens	43-52
26982234-1	2016	Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-aminonaphthalen-1-yloxy nicotinamide core structure, 5-((3-amidobenzyl)oxy)nicotinamides offered excellent activity against SIRT2 and high isozyme selectivity over SIRT1 and SIRT3.	5-aminonaphthalen-1-yloxy nicotinamide	93-131	sirtuin 2	Homo sapiens	54-59
26982234-1	2016	Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-aminonaphthalen-1-yloxy nicotinamide core structure, 5-((3-amidobenzyl)oxy)nicotinamides offered excellent activity against SIRT2 and high isozyme selectivity over SIRT1 and SIRT3.	5-((3-amidobenzyl)oxy)nicotinamides	148-183	sirtuin 2	Homo sapiens	43-52
26982234-1	2016	Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-aminonaphthalen-1-yloxy nicotinamide core structure, 5-((3-amidobenzyl)oxy)nicotinamides offered excellent activity against SIRT2 and high isozyme selectivity over SIRT1 and SIRT3.	5-((3-amidobenzyl)oxy)nicotinamides	148-183	sirtuin 2	Homo sapiens	54-59
26982234-1	2016	Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-aminonaphthalen-1-yloxy nicotinamide core structure, 5-((3-amidobenzyl)oxy)nicotinamides offered excellent activity against SIRT2 and high isozyme selectivity over SIRT1 and SIRT3.	5-((3-amidobenzyl)oxy)nicotinamides	148-183	sirtuin 2	Homo sapiens	219-224
26982234-3	2016	Kinetic studies revealed that a representative SIRT2 inhibitor acted competitively against both NAD(+) and the peptide substrate, an inhibitory modality that was supported by our computational study.	NAD	96-102	sirtuin 2	Homo sapiens	47-52
26982234-5	2016	Therefore, 5-((3-amidobenzyl)oxy)nicotinamides represent a new class of SIRT2 inhibitors that are attractive candidates for further lead optimization in our continued effort to explore selective inhibition of SIRT2 as a potential therapy for Parkinson"s disease.	5-((3-amidobenzyl)oxy)nicotinamides	11-46	sirtuin 2	Homo sapiens	72-77
26982234-5	2016	Therefore, 5-((3-amidobenzyl)oxy)nicotinamides represent a new class of SIRT2 inhibitors that are attractive candidates for further lead optimization in our continued effort to explore selective inhibition of SIRT2 as a potential therapy for Parkinson"s disease.	5-((3-amidobenzyl)oxy)nicotinamides	11-46	sirtuin 2	Homo sapiens	209-214
26791955-3	2016	By combining a structure-based virtual screening of the Specs database with cell-based assays, we identified the 5-benzylidene-hydantoin as new scaffold for the inhibition of SIRT2 catalytic activity.	5-Benzylidenehydantoin	113-136	sirtuin 2	Homo sapiens	175-180
26696402-0	2016	Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure-Activity Relationship Study.	2-aminothiazole	0-14	sirtuin 2	Homo sapiens	39-44
26796034-4	2016	Here we report an improved fluorogenic assay for SIRT1, SIRT2, and SIRT3 using a new substrate, a myristoyl peptide with a C-terminal aminocoumarin.	Aminocoumarins	134-147	sirtuin 2	Homo sapiens	56-61
26854234-3	2016	SIRT2 interacts with and deacetylates ATRIP at lysine 32 (K32) in response to replication stress.	Lysine	47-53	sirtuin 2	Homo sapiens	0-5
27158385-7	2016	Moreover, the effects of miR-7 were counteracted by Bax and Sirt2 overexpression, respectively.	mir-7	25-30	sirtuin 2	Homo sapiens	60-65
26788965-5	2016	Novel enzymatic activities of SIRT2 were thus established in vitro, which warrant further investigation, and two known inhibitors, suramin and SirReal2, were profiled against substrates containing epsilon-N-acyllysine modifications of varying length.	Suramin	131-138	sirtuin 2	Homo sapiens	30-35
26748890-3	2016	Here, based on a crystal structure of Sirt2 in complex with an optimized sirtuin rearranging ligand (SirReal) that shows improved potency, water solubility, and cellular efficacy, we present the development of the first Sirt2-selective affinity probe.	Water	139-144	sirtuin 2	Homo sapiens	38-43
26748890-3	2016	Here, based on a crystal structure of Sirt2 in complex with an optimized sirtuin rearranging ligand (SirReal) that shows improved potency, water solubility, and cellular efficacy, we present the development of the first Sirt2-selective affinity probe.	Water	139-144	sirtuin 2	Homo sapiens	220-225
26647771-1	2016	SIRT2, one of nicotinamide adenine dinucleotide (NAD+)-dependent class III histone deacetylase family proteins, has been found to be involved in the proliferation and survival of acute myeloid leukemia (AML) cells.	NAD	14-47	sirtuin 2	Homo sapiens	0-5
26647771-1	2016	SIRT2, one of nicotinamide adenine dinucleotide (NAD+)-dependent class III histone deacetylase family proteins, has been found to be involved in the proliferation and survival of acute myeloid leukemia (AML) cells.	NAD	49-53	sirtuin 2	Homo sapiens	0-5
26647771-8	2016	Furthermore, blockage of ERK1/2 signaling pathway with the chemical inhibitor PD98059, further induced apoptosis of HL60/A cells conferred by SIRT2 depletion.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	78-85	sirtuin 2	Homo sapiens	142-147
26647771-10	2016	Thus, our findings collectively suggested that the expression level of SIRT2 has a positive relationship with DNR/Ara-C resistance and activity of ERK1/2 signaling pathway.	aspartylasparagylarginine	110-113	sirtuin 2	Homo sapiens	71-76
26647771-10	2016	Thus, our findings collectively suggested that the expression level of SIRT2 has a positive relationship with DNR/Ara-C resistance and activity of ERK1/2 signaling pathway.	Cytarabine	114-119	sirtuin 2	Homo sapiens	71-76
26647771-11	2016	SIRT2 might regulate DNR/Ara-C sensitivity in AML cells at least partially through the ERK1/2 pathway.	aspartylasparagylarginine	21-24	sirtuin 2	Homo sapiens	0-5
26647771-11	2016	SIRT2 might regulate DNR/Ara-C sensitivity in AML cells at least partially through the ERK1/2 pathway.	Cytarabine	25-30	sirtuin 2	Homo sapiens	0-5
27725455-1	2016	SIRT2 is a member of the human sirtuin family of proteins and possesses nicotinamide adenine dinucleotide (NAD)-dependent lysine deacetylase activity.	NAD	107-110	sirtuin 2	Homo sapiens	0-5
26794150-0	2016	Functional characterization of NAD dependent de-acetylases SIRT1 and SIRT2 in B-Cell Chronic Lymphocytic Leukemia (CLL).	NAD	31-34	sirtuin 2	Homo sapiens	69-74
26414199-1	2016	The nicotinamide adenine dinucleotide-dependent protein deacetylase silent information regulator 2 (Sir2) regulates cellular lifespan in several organisms.	NAD	4-37	sirtuin 2	Homo sapiens	68-98
26414199-1	2016	The nicotinamide adenine dinucleotide-dependent protein deacetylase silent information regulator 2 (Sir2) regulates cellular lifespan in several organisms.	NAD	4-37	sirtuin 2	Homo sapiens	100-104
26433268-11	2015	Further, repeated treatment with the class IIa Hdac inhibitor MC1568 and the Sirt2 inhibitor 33i for three weeks increased synaptic plasticity in the prefrontal cortex.	6-(4-amino-4-methylpiperidin-1-yl)-3-(3-chlorophenyl)-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one	93-96	sirtuin 2	Homo sapiens	77-82
25924011-11	2015	Interestingly, at concentrations where resveratrol induced premature senescence we show a significant decrease in SIRT1 and SIRT2 levels by Western Blot and quantitative RT-PCR analysis.	Resveratrol	39-50	sirtuin 2	Homo sapiens	124-129
26538315-4	2015	We discuss the different functions and targets of SIRT2 in various physiological processes, including adipogenesis, fatty acid oxidation, gluconeogenesis, and insulin sensitivity.	Fatty Acids	116-126	sirtuin 2	Homo sapiens	50-55
29124170-3	2015	In this study we identified the sirtuin 1/sirtuin 2 (SIRT1/2) inhibitor cambinol acts as a drug that inhibits lysosome redistribution and tumor invasion.	cambinol	72-80	sirtuin 2	Homo sapiens	42-51
25912555-3	2015	Here, we show for the first time that AC-93253, a SIRT2 inhibitor, exerts a negative effect on the expression of a set of genes involved in the progression and chemoresistance (e.g., oncogenes, apoptosis-related genes, ABC transporter genes, and cell cycle control genes) of melanoma cells.	AC 93253	38-46	sirtuin 2	Homo sapiens	50-55
25971769-0	2015	Discovery of bicyclic pyrazoles as class III histone deacetylase SIRT1 and SIRT2 inhibitors.	bicyclic pyrazoles	13-31	sirtuin 2	Homo sapiens	75-80
25971769-3	2015	These bicyclic pyrazole compounds represent a new class of sirtuin inhibitors with a preference for SIRT1 over SIRT2.	pyrazole	15-23	sirtuin 2	Homo sapiens	111-116
26407304-4	2015	Here, we provide the first full-length molecular models of SIRT2 in the absence and presence of NAD+.	NAD	96-100	sirtuin 2	Homo sapiens	59-64
25897714-7	2015	Though the rate of nucleophilic attack of the 2"-hydroxyl on the C1"-O-alkylimidate intermediate varies with acyl substrate chain length, this step remains rate-determining for SIRT2 and SIRT3; however, for SIRT6, this step is no longer rate-limiting for long chain substrates.	2"-hydroxyl	46-57	sirtuin 2	Homo sapiens	177-182
25897714-7	2015	Though the rate of nucleophilic attack of the 2"-hydroxyl on the C1"-O-alkylimidate intermediate varies with acyl substrate chain length, this step remains rate-determining for SIRT2 and SIRT3; however, for SIRT6, this step is no longer rate-limiting for long chain substrates.	c1"-o-alkylimidate	65-83	sirtuin 2	Homo sapiens	177-182
25897714-8	2015	Cocrystallization of SIRT2 with myristoylated peptide and NAD(+) yielded a co-complex structure with reaction product 2"-O-myristoyl-ADP-ribose, revealing a latent hydrophobic cavity to accommodate the long chain acyl group, and suggesting a general mechanism for long chain deacylation.	NAD	58-64	sirtuin 2	Homo sapiens	21-26
25897714-8	2015	Cocrystallization of SIRT2 with myristoylated peptide and NAD(+) yielded a co-complex structure with reaction product 2"-O-myristoyl-ADP-ribose, revealing a latent hydrophobic cavity to accommodate the long chain acyl group, and suggesting a general mechanism for long chain deacylation.	2"-o-myristoyl-adp-ribose	118-143	sirtuin 2	Homo sapiens	21-26
25829495-3	2015	Sirtinol, a cell-permeable lactone ring derived from naphthol, is a dual Sirt1/Sirt2 inhibitor of low potency, whereas EX-527 is a potent and selective Sirt1 inhibitor.	sirtinol	0-8	sirtuin 2	Homo sapiens	79-84
25924011-0	2015	Resveratrol Induced Premature Senescence Is Associated with DNA Damage Mediated SIRT1 and SIRT2 Down-Regulation.	Resveratrol	0-11	sirtuin 2	Homo sapiens	90-95
25666612-0	2015	Propofol inhibits SIRT2 deacetylase through a conformation-specific, allosteric site.	Propofol	0-8	sirtuin 2	Homo sapiens	18-23
25626146-0	2015	Boehmeriasin A as new lead compound for the inhibition of topoisomerases and SIRT2.	boehmeriasin A	0-14	sirtuin 2	Homo sapiens	77-82
25924011-12	2015	Conversely inhibition of SIRT1 and SIRT2 via siRNA or sirtinol treatment also induced senescence in BJ fibroblasts associated with increased SA-beta-gal activity, gamma-H2AX phosphorylation and p53, p21CIP1 and p16INK4A levels.	sirtinol	54-62	sirtuin 2	Homo sapiens	35-40
25924011-12	2015	Conversely inhibition of SIRT1 and SIRT2 via siRNA or sirtinol treatment also induced senescence in BJ fibroblasts associated with increased SA-beta-gal activity, gamma-H2AX phosphorylation and p53, p21CIP1 and p16INK4A levels.	2-(2-quinolinyl)-1H-indene--1,3(2H)-dione-6'-sulfonic acid	141-152	sirtuin 2	Homo sapiens	35-40
25924011-14	2015	In conclusion our data reveal that resveratrol induced premature senescence is associated with SIRT1 and SIRT2 down regulation in human dermal fibroblasts.	Resveratrol	35-46	sirtuin 2	Homo sapiens	105-110
24681946-8	2015	Moreover, a pharmacological agent that increased the intracellular NAD(+)/NADH ratio led to the degradation of HIF-1alpha by increasing SIRT2-mediated deacetylation and subsequent hydroxylation.	NAD	67-73	sirtuin 2	Homo sapiens	136-141
24681946-8	2015	Moreover, a pharmacological agent that increased the intracellular NAD(+)/NADH ratio led to the degradation of HIF-1alpha by increasing SIRT2-mediated deacetylation and subsequent hydroxylation.	NAD	74-78	sirtuin 2	Homo sapiens	136-141
25549554-0	2015	Functionalized tetrahydro-1H-pyrido[4,3-b]indoles: a novel chemotype with Sirtuin 2 inhibitory activity.	tetrahydro-1h-pyrido[4,3-b]indoles	15-49	sirtuin 2	Homo sapiens	74-83
25549554-2	2015	Functionalized tetrahydro-1H-pyrido[4,3-b]indoles were identified as preferential sirtuin 2 inhibitors, with in vitro inhibitory potencies in the low micromolar concentrations (IC50 3-4 muM) for the more promising candidates.	tetrahydro-1h-pyrido[4,3-b]indoles	15-49	sirtuin 2	Homo sapiens	82-91
25549554-4	2015	Molecular docking showed that the tetrahydropyridoindole scaffold was positioned in the NAD + pocket and the acetylated substrate channel of the sirtuin 2 protein by van der Waals/hydrophobic, H bonding and stacking interactions.	tetrahydropyridoindole	34-56	sirtuin 2	Homo sapiens	145-154
25549554-4	2015	Molecular docking showed that the tetrahydropyridoindole scaffold was positioned in the NAD + pocket and the acetylated substrate channel of the sirtuin 2 protein by van der Waals/hydrophobic, H bonding and stacking interactions.	NAD	88-93	sirtuin 2	Homo sapiens	145-154
25549554-5	2015	Functionalized tetrahydropyridoindoles represent a novel class of sirtuin 2 inhibitors that could be further explored for its therapeutic potential.	tetrahydropyridoindole	15-38	sirtuin 2	Homo sapiens	66-75
24697269-2	2014	In an effort to identify small molecule inhibitors of sirtuins for potential use as chemotherapeutics as well as tools to modulate sirtuin activity, we previously identified a nonselective sirtuin inhibitor called cambinol (IC50   50 muM for SIRT1 and SIRT2) with in vitro and in vivo antilymphoma activity.	cambinol	214-222	sirtuin 2	Homo sapiens	252-257
25870619-5	2015	In comparison, class III HDACs (also known as the sirtuins) are composed of a family of NAD(+)-dependent protein-modifying enzymes related to the Sir2 gene.	NAD	88-94	sirtuin 2	Homo sapiens	146-150
25502412-3	2015	In this study, a series of SIRT2 inhibitors with a 2-anilinobenzamide core was analysed using a combination of molecular modelling techniques.	2-(phenylamino)benzamide	51-69	sirtuin 2	Homo sapiens	27-32
24469059-4	2015	Using a focused RNA interference library for genes involved in epigenetic regulation, we identify sirtuin2 (SIRT2), an NAD(+)-dependent deacetylase, as a modulator of the response to EGFR inhibitors in colon and lung cancer.	NAD	119-125	sirtuin 2	Homo sapiens	98-106
24469059-4	2015	Using a focused RNA interference library for genes involved in epigenetic regulation, we identify sirtuin2 (SIRT2), an NAD(+)-dependent deacetylase, as a modulator of the response to EGFR inhibitors in colon and lung cancer.	NAD	119-125	sirtuin 2	Homo sapiens	108-113
25476551-6	2015	The results also show that Sirt2 can regulate the acylation of lysine residues, of proteins, with fatty acids within cells.	Lysine	63-69	sirtuin 2	Homo sapiens	27-32
25476551-6	2015	The results also show that Sirt2 can regulate the acylation of lysine residues, of proteins, with fatty acids within cells.	Fatty Acids	98-109	sirtuin 2	Homo sapiens	27-32
25383691-4	2014	Herein we report novel chroman-4-one and chromone-based SIRT2 inhibitors containing various heterofunctionalities to improve pharmacokinetic properties.	Chromones	41-49	sirtuin 2	Homo sapiens	56-61
25384215-2	2014	Here, we determined that ALDH1A1 activity is inhibited by acetylation of lysine 353 (K353) and that acetyltransferase P300/CBP-associated factor (PCAF) and deacetylase sirtuin 2 (SIRT2) are responsible for regulating the acetylation state of ALDH1A1 K353.	Lysine	73-79	sirtuin 2	Homo sapiens	179-184
24814981-10	2014	Furthermore, we provide evidence confirming that the NAD-dependent regulation of tubulin acetylation is mediated by SIRT2.	NAD	53-56	sirtuin 2	Homo sapiens	116-121
24996174-5	2014	We found that the protein levels of SIRT2 were decreased by c-Src, and subsequently rescued by the addition of a Src specific inhibitor, SU6656, or by siRNA-mediated knockdown of c-Src.	SU 6656	137-143	sirtuin 2	Homo sapiens	36-41
24786789-7	2014	Increased levels of reactive oxygen species stimulate PGAM2 deacetylation and activity by promoting its interaction with SIRT2.	Reactive Oxygen Species	20-43	sirtuin 2	Homo sapiens	121-126
24792244-5	2014	Interestingly, 6OHDA decreased the activity of tubulin deacetylases, specifically sirtuin 2 (SIRT2), through more than one mechanism.	Oxidopamine	15-20	sirtuin 2	Homo sapiens	82-91
24792244-5	2014	Interestingly, 6OHDA decreased the activity of tubulin deacetylases, specifically sirtuin 2 (SIRT2), through more than one mechanism.	Oxidopamine	15-20	sirtuin 2	Homo sapiens	93-98
24939540-1	2014	Sirtuin 2 (SIRT2) is an NAD(+) (nicotinamide adenine dinucleotide)-dependent deacetylase.	NAD	24-30	sirtuin 2	Homo sapiens	0-9
24939540-1	2014	Sirtuin 2 (SIRT2) is an NAD(+) (nicotinamide adenine dinucleotide)-dependent deacetylase.	NAD	24-30	sirtuin 2	Homo sapiens	11-16
24939540-1	2014	Sirtuin 2 (SIRT2) is an NAD(+) (nicotinamide adenine dinucleotide)-dependent deacetylase.	NAD	32-65	sirtuin 2	Homo sapiens	0-9
24939540-1	2014	Sirtuin 2 (SIRT2) is an NAD(+) (nicotinamide adenine dinucleotide)-dependent deacetylase.	NAD	32-65	sirtuin 2	Homo sapiens	11-16
24939540-4	2014	We have recently shown the involvement of SIRT2 in the antiproliferative effects of resveratrol on primary cultures of human glioblastoma stem cells.	Resveratrol	84-95	sirtuin 2	Homo sapiens	42-47
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	azipm	0-5	sirtuin 2	Homo sapiens	25-30
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	azipm	0-5	sirtuin 2	Homo sapiens	201-206
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	Tyrosine	41-44	sirtuin 2	Homo sapiens	25-30
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	Phenylalanine	51-54	sirtuin 2	Homo sapiens	25-30
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	Propofol	133-141	sirtuin 2	Homo sapiens	25-30
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	Propofol	133-141	sirtuin 2	Homo sapiens	201-206
25666612-3	2015	AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190), and Met(206)) that are located in a single allosteric protein site, and propofol inhibited [(3)H]AziPm photolabeling of this site in myelin SIRT2.	azipm	158-163	sirtuin 2	Homo sapiens	25-30
25666612-4	2015	Structural modeling and in vitro experiments with recombinant human SIRT2 determined that propofol and [(3)H]AziPm only bind specifically and competitively to the enzyme when co-equilibrated with other substrates, which suggests that the anesthetic site is either created or stabilized in enzymatic conformations that are induced by substrate binding.	Propofol	90-98	sirtuin 2	Homo sapiens	68-73
25666612-4	2015	Structural modeling and in vitro experiments with recombinant human SIRT2 determined that propofol and [(3)H]AziPm only bind specifically and competitively to the enzyme when co-equilibrated with other substrates, which suggests that the anesthetic site is either created or stabilized in enzymatic conformations that are induced by substrate binding.	[(3)h]azipm	103-114	sirtuin 2	Homo sapiens	68-73
25666612-6	2015	Residues that line the propofol binding site on SIRT2 contact the sirtuin co-substrate NAD(+) during enzymatic catalysis, and assays that measured SIRT2 deacetylation of acetylated alpha-tubulin revealed that propofol inhibits enzymatic function.	Propofol	23-31	sirtuin 2	Homo sapiens	48-53
25666612-6	2015	Residues that line the propofol binding site on SIRT2 contact the sirtuin co-substrate NAD(+) during enzymatic catalysis, and assays that measured SIRT2 deacetylation of acetylated alpha-tubulin revealed that propofol inhibits enzymatic function.	NAD	87-93	sirtuin 2	Homo sapiens	48-53
25666612-6	2015	Residues that line the propofol binding site on SIRT2 contact the sirtuin co-substrate NAD(+) during enzymatic catalysis, and assays that measured SIRT2 deacetylation of acetylated alpha-tubulin revealed that propofol inhibits enzymatic function.	Propofol	209-217	sirtuin 2	Homo sapiens	48-53
25666612-7	2015	We conclude that propofol inhibits the mammalian deacetylase SIRT2 through a conformation-specific, allosteric protein site that is unique from the previously described binding sites of other inhibitors.	Propofol	17-25	sirtuin 2	Homo sapiens	61-66
25312940-4	2015	To investigate the role of SIRT2 in colon cancer, we treated HCT116 human colon cancer cells with the SIRT2-specific inhibitor AK-1, a cell-permeable benzylsulfonamide.	Phenylmethanesulfonamide	150-167	sirtuin 2	Homo sapiens	102-107
25515955-0	2015	Design, synthesis and structure-activity relationship studies of novel sirtuin 2 (SIRT2) inhibitors with a benzamide skeleton.	benzamide	107-116	sirtuin 2	Homo sapiens	71-80
25515955-0	2015	Design, synthesis and structure-activity relationship studies of novel sirtuin 2 (SIRT2) inhibitors with a benzamide skeleton.	benzamide	107-116	sirtuin 2	Homo sapiens	82-87
25515955-2	2015	We designed and synthesized a series of benzamide derivatives as SIRT2 inhibitor candidates.	benzamide	40-49	sirtuin 2	Homo sapiens	65-70
25614674-2	2015	Sirtuin 1 (SIRT1), which belongs to the family of sirtuins (Sir2; silent information regulator 2 protein) participates in the regulation of skeletal muscle glucose and lipid metabolism.	Glucose	156-163	sirtuin 2	Homo sapiens	66-96
25395356-0	2015	The discovery of a highly selective 5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one SIRT2 inhibitor that is neuroprotective in an in vitro Parkinson"s disease model.	5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3h)	36-92	sirtuin 2	Homo sapiens	97-102
25395356-6	2015	In concordance with the recent reports that suggest SIRT2 inhibition is a potential strategy for the treatment of Parkinson"s disease, we find that compound ICL-SIRT078 has a significant neuroprotective effect in a lactacystin-induced model of Parkinsonian neuronal cell death in the N27 cell line.	lactacystin	215-226	sirtuin 2	Homo sapiens	52-57
26075037-2	2015	Sirtuins (silent information regulator 2 (Sir2) proteins), NAD(+) dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity, are emerging as key antiaging molecules and regulators in many diseases.	NAD	59-65	sirtuin 2	Homo sapiens	10-40
26075037-2	2015	Sirtuins (silent information regulator 2 (Sir2) proteins), NAD(+) dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity, are emerging as key antiaging molecules and regulators in many diseases.	NAD	59-65	sirtuin 2	Homo sapiens	42-46
25369635-5	2014	We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins.	Lysine	69-75	sirtuin 2	Homo sapiens	21-26
25369635-5	2014	We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins.	histone peptides	89-105	sirtuin 2	Homo sapiens	21-26
24814981-0	2014	Regulation of SIRT2-dependent alpha-tubulin deacetylation by cellular NAD levels.	NAD	70-73	sirtuin 2	Homo sapiens	14-19
24814981-2	2014	The acetylation reaction is catalyzed by alpha-tubulin N-acetyltransferase and the modification can be reversed by either the NAD-independent class II histone deacetylase HDAC6 or the NAD-dependent deacetylase SIRT2.	NAD	126-129	sirtuin 2	Homo sapiens	210-215
24814981-2	2014	The acetylation reaction is catalyzed by alpha-tubulin N-acetyltransferase and the modification can be reversed by either the NAD-independent class II histone deacetylase HDAC6 or the NAD-dependent deacetylase SIRT2.	NAD	184-187	sirtuin 2	Homo sapiens	210-215
25189993-2	2014	In this study, we screened derivatives of several groups of natural products and identified a novel SIRT1 inhibitor JQ-101, a synthetic derivative of the polyprenylated acylphloroglucinol (PPAP) natural products, with an IC(50) for SIRT1 of 30 microM in vitro, with 5-fold higher activity for SIRT1 vs. SIRT2.	jq-101	116-122	sirtuin 2	Homo sapiens	303-308
25285631-0	2014	Deacetylation of the mitotic checkpoint protein BubR1 at lysine 250 by SIRT2 and subsequent effects on BubR1 degradation during the prometaphase/anaphase transition.	Lysine	57-63	sirtuin 2	Homo sapiens	71-76
25195573-4	2014	Over-expression of SIRT2 or mutations at the acetylatable lysines of PGAM attenuates cancer cell proliferation with a concomitant decrease in PGAM activity.	Lysine	58-65	sirtuin 2	Homo sapiens	19-24
24814870-4	2014	provide evidence that sirtuin-2 (SIRT2), a NAD+-dependent deacetylase, inhibits the expression of keratin 15 and keratin 19, epidermal stem cell markers, while it stimulates the expression of loricrin, a marker of terminal keratinocyte differentiation.	NAD	43-46	sirtuin 2	Homo sapiens	22-31
24814870-4	2014	provide evidence that sirtuin-2 (SIRT2), a NAD+-dependent deacetylase, inhibits the expression of keratin 15 and keratin 19, epidermal stem cell markers, while it stimulates the expression of loricrin, a marker of terminal keratinocyte differentiation.	NAD	43-46	sirtuin 2	Homo sapiens	33-38
24992072-1	2014	Two series of novel benzimidazole derivatives were designed, synthesized and evaluated for their SIRT1 and SIRT2 inhibitory activity.	benzimidazole	20-33	sirtuin 2	Homo sapiens	107-112
24992072-4	2014	Docking analysis of representative compound 4j into SIRT2 indicated that the interaction with receptor was primarily due to hydrogen bonding and pi-pi stacking interactions.	Hydrogen	124-132	sirtuin 2	Homo sapiens	52-57
24825350-0	2014	SIRT2 controls the pentose phosphate switch.	Pentosephosphates	19-36	sirtuin 2	Homo sapiens	0-5
24497179-5	2014	Overall, the results show that the SIRT2 SNP is associated with human AD risk in the comparison models (T vs. C: OR 1.140, 95% CI 1.034-1.258; TC vs. CC: OR 1.178, 95% CI 1.019-1.361; TT + TC vs. CC: OR 1.197, 95% CI 1.043-1.373).	Technetium	143-145	sirtuin 2	Homo sapiens	35-40
24497179-5	2014	Overall, the results show that the SIRT2 SNP is associated with human AD risk in the comparison models (T vs. C: OR 1.140, 95% CI 1.034-1.258; TC vs. CC: OR 1.178, 95% CI 1.019-1.361; TT + TC vs. CC: OR 1.197, 95% CI 1.043-1.373).	Technetium	189-191	sirtuin 2	Homo sapiens	35-40
24697269-4	2014	Our ongoing efforts to optimize cambinol analogues for potency and selectivity have resulted in the identification of isoform selective analogues: 17 with &gt;7.8-fold selectivity for SIRT1, 24 with &gt;15.4-fold selectivity for SIRT2, and 8 with 6.8- and 5.3-fold selectivity for SIRT3 versus SIRT1 and SIRT2, respectively.	cambinol	32-40	sirtuin 2	Homo sapiens	229-234
24697269-4	2014	Our ongoing efforts to optimize cambinol analogues for potency and selectivity have resulted in the identification of isoform selective analogues: 17 with &gt;7.8-fold selectivity for SIRT1, 24 with &gt;15.4-fold selectivity for SIRT2, and 8 with 6.8- and 5.3-fold selectivity for SIRT3 versus SIRT1 and SIRT2, respectively.	cambinol	32-40	sirtuin 2	Homo sapiens	304-309
24322591-7	2014	PI3 K/Akt specific inhibitor wortmannin decreased Sirt2 expression, proliferation, and synthetic phenotype transformation of VSMCs, but had no effect on IGF-1R.	Wortmannin	29-39	sirtuin 2	Homo sapiens	50-55
24602787-0	2014	Development and characterization of 3-(benzylsulfonamido)benzamides as potent and selective SIRT2 inhibitors.	3-(benzylsulfonamido)benzamides	36-67	sirtuin 2	Homo sapiens	92-97
24602787-2	2014	The present study was directed at optimizing the potency of SIRT2 inhibitors containing the neuroprotective sulfobenzoic acid scaffold and improving their pharmacology.	2-sulfobenzoic acid	108-125	sirtuin 2	Homo sapiens	60-65
23955573-11	2014	Pharmacological blockade of SIRT2 activity or down-regulation of SIRT2 expression with siRNAs counteracted the inhibitory effect of resveratrol on cell proliferation.	Resveratrol	132-143	sirtuin 2	Homo sapiens	28-33
24203696-2	2014	Here, we present for the first time that SIRT2, a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, regulates ciliogenesis and centrosome amplification.	NAD	50-83	sirtuin 2	Homo sapiens	41-46
24203696-2	2014	Here, we present for the first time that SIRT2, a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, regulates ciliogenesis and centrosome amplification.	NAD	85-88	sirtuin 2	Homo sapiens	41-46
24203696-3	2014	Overexpression of SIRT2 in renal epithelial cells appeared to disrupt cilia formation, causing decreased numbers of cells with cilia and decreased cilia length, while inhibition of SIRT2 activity by nicotinamide treatment or knockdown of SIRT2 with siRNA was shown to block cilia disassembly during the cell cycle.	Niacinamide	199-211	sirtuin 2	Homo sapiens	18-23
24551254-6	2014	The apo-form of human SIRT2 and the same structure solved in complex with its co-substrate NAD(+) allowed the modeling of TcSir2rp1 in the open and closed conformational states.	NAD	91-97	sirtuin 2	Homo sapiens	22-27
24446434-8	2014	This regulation involved a novel AMP-activated kinase-dependent Sirt2 phosphorylation at Thr(101).	Threonine	89-92	sirtuin 2	Homo sapiens	64-69
24572426-0	2014	Retraction: The NAD-dependent deacetylase SIRT2 is required for programmed necrosis.	NAD	16-19	sirtuin 2	Homo sapiens	42-47
24389023-1	2014	SIRT2 deacetylates specific acetyllysine residues in diverse proteins and is implicated in a variety of cellular processes.	N-epsilon-Acetyl-L-lysine	28-40	sirtuin 2	Homo sapiens	0-5
24389023-6	2014	A structural comparison of the SIRT2-S2iL5 complex with SIRT2 in the free form, and in complex with ADP-ribose, revealed that S2iL5 induces an open-to-closed domain movement and an unexpected helix-to-coil transition in a SIRT2-specific region.	Adenosine Diphosphate Ribose	100-110	sirtuin 2	Homo sapiens	31-36
23955573-11	2014	Pharmacological blockade of SIRT2 activity or down-regulation of SIRT2 expression with siRNAs counteracted the inhibitory effect of resveratrol on cell proliferation.	Resveratrol	132-143	sirtuin 2	Homo sapiens	65-70
24183459-11	2014	In the ER+ve cohort, high SIRT2 nuclear levels were associated with shorter disease-free survival and time to recurrence whilst on Tamoxifen, in patients with Grade 3 tumours.	Tamoxifen	131-140	sirtuin 2	Homo sapiens	26-31
24387981-1	2014	A total of 15 novel benzimidazole derivatives were designed, synthesized and evaluated for their SIRT1 and SIRT2 inhibitory activity.	benzimidazole	20-33	sirtuin 2	Homo sapiens	107-112
24343700-1	2014	Silent information regulator type-1 (SIRT1) is the best-studied member of the Sirtuin (Sir2) family of nicotinamide dinucleotide (NAD)-dependent class III histone deacetylases (HDACs), but has not yet been explored in cutaneous T-cell lymphoma (CTCL).	NAD	103-128	sirtuin 2	Homo sapiens	87-91
24343700-1	2014	Silent information regulator type-1 (SIRT1) is the best-studied member of the Sirtuin (Sir2) family of nicotinamide dinucleotide (NAD)-dependent class III histone deacetylases (HDACs), but has not yet been explored in cutaneous T-cell lymphoma (CTCL).	NAD	130-133	sirtuin 2	Homo sapiens	87-91
23798679-5	2013	There is also evidence that metabolites such as NAD(+) (acting via deacetylases such as SIRT1 and SIRT2) and succinate (which regulates hypoxia-inducible factor 1alpha) are signals that regulate innate immunity.	NAD	48-54	sirtuin 2	Homo sapiens	98-103
23900402-4	2013	SIRT2 activity was also inhibited by toxoflavin less potently than SIRT1 in deacetylase assay in vitro.	toxoflavin	37-47	sirtuin 2	Homo sapiens	0-5
23900402-7	2013	The acetylation levels of alpha-tubulin, a SIRT2 substrate, were also increased by toxoflavin treatment dose-dependently.	toxoflavin	83-93	sirtuin 2	Homo sapiens	43-48
23956326-0	2013	Sirtuin 2 (SIRT2) enhances 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced nigrostriatal damage via deacetylating forkhead box O3a (Foxo3a) and activating Bim protein.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	27-71	sirtuin 2	Homo sapiens	0-9
23956326-0	2013	Sirtuin 2 (SIRT2) enhances 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced nigrostriatal damage via deacetylating forkhead box O3a (Foxo3a) and activating Bim protein.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	27-71	sirtuin 2	Homo sapiens	11-16
23956326-0	2013	Sirtuin 2 (SIRT2) enhances 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced nigrostriatal damage via deacetylating forkhead box O3a (Foxo3a) and activating Bim protein.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	73-77	sirtuin 2	Homo sapiens	0-9
23956326-0	2013	Sirtuin 2 (SIRT2) enhances 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced nigrostriatal damage via deacetylating forkhead box O3a (Foxo3a) and activating Bim protein.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	73-77	sirtuin 2	Homo sapiens	11-16
23915912-6	2013	Further analysis showed that SIRT2 overexpression increased the ROS (reactive oxygen species) production and p27 levels.	Reactive Oxygen Species	64-67	sirtuin 2	Homo sapiens	29-34
23915912-6	2013	Further analysis showed that SIRT2 overexpression increased the ROS (reactive oxygen species) production and p27 levels.	Reactive Oxygen Species	69-92	sirtuin 2	Homo sapiens	29-34
23915912-7	2013	Moreover, up-regulation of SIRT2 in NSCLC cells increased the sensitivity to Cisplatin treatment.	Cisplatin	77-86	sirtuin 2	Homo sapiens	27-32
24093018-1	2013	Silent information regulator 2 proteins (sirtuins or SIRTs) are a group of deacetylases (or deacylases) whose activities are dependent on and regulated by nicotinamide adenine dinucleotide (NAD(+)).	NAD	155-188	sirtuin 2	Homo sapiens	0-30
24093018-1	2013	Silent information regulator 2 proteins (sirtuins or SIRTs) are a group of deacetylases (or deacylases) whose activities are dependent on and regulated by nicotinamide adenine dinucleotide (NAD(+)).	NAD	190-196	sirtuin 2	Homo sapiens	0-30
23806683-6	2013	In contrast, U0126, an inhibitor of mitogen-activated kinase kinase, suppressed SIRT2 protein level.	U 0126	13-18	sirtuin 2	Homo sapiens	80-85
23499872-5	2013	Sirtinol, an inhibitor of SIRT1 and SIRT2 structurally related to cambinol, also decreased macrophage response to TLR stimulation.	cambinol	66-74	sirtuin 2	Homo sapiens	36-41
23502856-4	2013	Inducers of the NLRP3 inflammasome caused aberrant mitochondrial homeostasis to diminish the concentration of the coenzyme NAD(+), which in turn inactivated the NAD(+)-dependent alpha-tubulin deacetylase sirtuin 2; this resulted in the accumulation of acetylated alpha-tubulin.	NAD	123-129	sirtuin 2	Homo sapiens	204-213
23570514-0	2013	Discovery of thieno[3,2-d]pyrimidine-6-carboxamides as potent inhibitors of SIRT1, SIRT2, and SIRT3.	thieno[3,2-d]pyrimidine-6-carboxamides	13-51	sirtuin 2	Homo sapiens	83-88
23499872-2	2013	Cambinol was originally described as a compound inhibiting the activity of SIRT1 and SIRT2, with efficient anti-tumor activity in vivo.	cambinol	0-8	sirtuin 2	Homo sapiens	85-90
23499872-5	2013	Sirtinol, an inhibitor of SIRT1 and SIRT2 structurally related to cambinol, also decreased macrophage response to TLR stimulation.	sirtinol	0-8	sirtuin 2	Homo sapiens	36-41
23502856-4	2013	Inducers of the NLRP3 inflammasome caused aberrant mitochondrial homeostasis to diminish the concentration of the coenzyme NAD(+), which in turn inactivated the NAD(+)-dependent alpha-tubulin deacetylase sirtuin 2; this resulted in the accumulation of acetylated alpha-tubulin.	NAD	161-167	sirtuin 2	Homo sapiens	204-213
23175188-5	2013	Consistent with this finding, SIRT2 repressed NEDD4 gene expression by directly binding to the NEDD4 gene core promoter and deacetylating histone H4 lysine 16.	Lysine	149-155	sirtuin 2	Homo sapiens	30-35
23478437-1	2013	The NAD+-dependent deacetylases Sirt1 and Sirt2 mediate cellular stress responses and are highly expressed in vascular endothelial cells.	NAD	4-7	sirtuin 2	Homo sapiens	42-47
23478437-4	2013	We found that Sirt2 knock down changed expression of 340 genes, which are mainly involved in cellular processes including actin binding, cellular amino acid metabolic process, transmembrane receptor protein serine/threonine kinase signaling, ferrous iron transport, protein transport and localization, cell morphogenesis, and functions associated with endosome membrane and the trans-Golgi network.	Iron	250-254	sirtuin 2	Homo sapiens	14-19
23092269-9	2013	It was also observed that BNIPDaCHM inhibited the activity of SIRT2 in vitro, but not of SIRT1.	bisnaphthalimidopropyl diaminodicyclohexylmethane	26-35	sirtuin 2	Homo sapiens	62-67
23092269-11	2013	To determine the binding potential of BNIPDaCHM on hSIRT2 and to further validate its inhibitory action, in silico docking studies were carried out, which revealed that BNIPDaCHM is composed of an entirely new SIRT2- inhibiting structural scaffold.	bisnaphthalimidopropyl diaminodicyclohexylmethane	38-47	sirtuin 2	Homo sapiens	51-57
23092269-11	2013	To determine the binding potential of BNIPDaCHM on hSIRT2 and to further validate its inhibitory action, in silico docking studies were carried out, which revealed that BNIPDaCHM is composed of an entirely new SIRT2- inhibiting structural scaffold.	bisnaphthalimidopropyl diaminodicyclohexylmethane	38-47	sirtuin 2	Homo sapiens	52-57
23092269-12	2013	In conclusion, this study indicates that BNIP derivatives with a novel structural backbone, such as BNIPDaCHM, may have potential as building blocks for novel antitumour agents which might selectively bind to hSIRT-2.	bnip	41-45	sirtuin 2	Homo sapiens	209-216
23358244-0	2013	Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation.	Lysine	70-76	sirtuin 2	Homo sapiens	12-17
23340254-8	2013	We demonstrate that the use of cambinol and the SIRT1/2 inhibitor VII, 2 small molecule inhibitors of SIRT1 and SIRT2, as well as small molecule inhibitors and small interfering RNA specific to SIRT1, all reduce the levels of aromatase mRNA.	cambinol	31-39	sirtuin 2	Homo sapiens	112-117
23454361-0	2013	Crystal structure analysis of human Sirt2 and its ADP-ribose complex.	Adenosine Diphosphate	50-53	sirtuin 2	Homo sapiens	36-41
23454361-0	2013	Crystal structure analysis of human Sirt2 and its ADP-ribose complex.	Ribose	54-60	sirtuin 2	Homo sapiens	36-41
23454361-3	2013	We crystallized Sirt2 in complex with a product analog, ADP-ribose, and solved this first crystal structure of a Sirt2 ligand complex at 2.3A resolution.	Adenosine Diphosphate Ribose	56-66	sirtuin 2	Homo sapiens	16-21
23454361-3	2013	We crystallized Sirt2 in complex with a product analog, ADP-ribose, and solved this first crystal structure of a Sirt2 ligand complex at 2.3A resolution.	Adenosine Diphosphate Ribose	56-66	sirtuin 2	Homo sapiens	113-118
24020002-1	2013	The cellular NAD(+)/NADH level controls Sir2 (silent information regulator 2) deacetylase activity in regulating aging in lower species.	NAD	13-19	sirtuin 2	Homo sapiens	40-44
24020002-1	2013	The cellular NAD(+)/NADH level controls Sir2 (silent information regulator 2) deacetylase activity in regulating aging in lower species.	NAD	13-19	sirtuin 2	Homo sapiens	46-76
24020002-1	2013	The cellular NAD(+)/NADH level controls Sir2 (silent information regulator 2) deacetylase activity in regulating aging in lower species.	NAD	20-24	sirtuin 2	Homo sapiens	40-44
24020002-1	2013	The cellular NAD(+)/NADH level controls Sir2 (silent information regulator 2) deacetylase activity in regulating aging in lower species.	NAD	20-24	sirtuin 2	Homo sapiens	46-76
23358244-6	2013	The NAD-dependent deacetylase sirtuin 2 (SIRT2) associated with and deacetylated K8.	NAD	4-7	sirtuin 2	Homo sapiens	30-39
23358244-6	2013	The NAD-dependent deacetylase sirtuin 2 (SIRT2) associated with and deacetylated K8.	NAD	4-7	sirtuin 2	Homo sapiens	41-46
23358244-9	2013	Therefore, K8 acetylation at Lys-207, a highly conserved residue among type II keratins and other IFs, is up-regulated upon hyperglycemia and down-regulated by SIRT2.	Lysine	29-32	sirtuin 2	Homo sapiens	160-165
22876953-1	2013	Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of evolutionarily conserved intracellular protein deacetylases that can catalyze the acetyl group removal from the specific Nepsilon-acetyl-lysine (AcK) side chains on a variety of proteins from all kingdoms of life.	N-epsilon-acetyllysine	195-217	sirtuin 2	Homo sapiens	0-30
22876953-1	2013	Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of evolutionarily conserved intracellular protein deacetylases that can catalyze the acetyl group removal from the specific Nepsilon-acetyl-lysine (AcK) side chains on a variety of proteins from all kingdoms of life.	N-epsilon-acetyllysine	195-217	sirtuin 2	Homo sapiens	32-36
24512730-2	2013	Here we investigated antitumor effects of tenovin-6, a small-molecule inhibitor of SIRT1 and SIRT2, in various colon cancer cell lines.	tenovin-6	42-51	sirtuin 2	Homo sapiens	93-98
23527151-5	2013	Hence, we performed 5 ns molecular dynamics (MD) simulation on SIRT2 Apo-form and complexes with substrate/NAD(+) and inhibitor of wild type (WT), Q167A, and H187A.	NAD	107-113	sirtuin 2	Homo sapiens	63-68
23527151-10	2013	Our study unveiled the structural changes of SIRT2 in presence of NAD(+) and inhibitor which should be helpful to improve the inhibitory potency of SIRT2.	NAD	66-72	sirtuin 2	Homo sapiens	45-50
23527151-10	2013	Our study unveiled the structural changes of SIRT2 in presence of NAD(+) and inhibitor which should be helpful to improve the inhibitory potency of SIRT2.	NAD	66-72	sirtuin 2	Homo sapiens	148-153
23460888-0	2013	Inhibition of the NAD-dependent protein deacetylase SIRT2 induces granulocytic differentiation in human leukemia cells.	NAD	18-21	sirtuin 2	Homo sapiens	52-57
23382805-4	2013	To elucidate the molecular basis of the small molecules interactions to inhibit the SIRT2 function we employed the molecular docking, molecular dynamics simulations, and the molecular mechanism Poisson-Boltzmann/surface area (MM-PBSA) calculations.	poly(tetramethylene succinate-co-tetramethylene adipate)	229-233	sirtuin 2	Homo sapiens	84-89
23382805-5	2013	Five well know inhibitors such as suramin, mol-6, sirtinol, 67, and nf675 were selected to establish the nature of the binding mode of the inhibitors in the SIRT2 active site.	Suramin	34-41	sirtuin 2	Homo sapiens	157-162
23382805-5	2013	Five well know inhibitors such as suramin, mol-6, sirtinol, 67, and nf675 were selected to establish the nature of the binding mode of the inhibitors in the SIRT2 active site.	mol-6	43-48	sirtuin 2	Homo sapiens	157-162
23382805-5	2013	Five well know inhibitors such as suramin, mol-6, sirtinol, 67, and nf675 were selected to establish the nature of the binding mode of the inhibitors in the SIRT2 active site.	sirtinol	50-58	sirtuin 2	Homo sapiens	157-162
23382805-6	2013	The molecular docking and dynamics simulations results revealed that the hydrogen bonds between Arg97 and Gln167 are crucial to inhibit the function of SIRT2.	Hydrogen	73-81	sirtuin 2	Homo sapiens	152-157
23382805-7	2013	In addition, the MM-PBSA calculations revealed that binding of inhibitors to SIRT2 is mainly driven by van der Waals/non-polar interactions.	poly(tetramethylene succinate-co-tetramethylene adipate)	20-24	sirtuin 2	Homo sapiens	77-82
22819792-8	2012	Overexpression of SIRT2 inhibits lysosome-mediated autophagic turnover by interfering with aggresome formation and also makes cells more vulnerable to accumulated protein-mediated cytotoxicity by MG132 and amyloid beta.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	196-201	sirtuin 2	Homo sapiens	18-23
22819792-9	2012	Moreover, MG132-induced accumulation of ubiquitinated proteins and p62 as well as cytotoxicity are attenuated in siRNA-mediated SIRT2-silencing cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	10-15	sirtuin 2	Homo sapiens	128-133
22742936-5	2012	The results showed that hydrogen-rich saline reduced the level of malondialdehyde (MDA) and elevated the level of silent information regulator 2 (Sir2).	Hydrogen	24-32	sirtuin 2	Homo sapiens	114-144
23079492-0	2012	Discovery and validation of SIRT2 inhibitors based on tenovin-6: use of a 1H-NMR method to assess deacetylase activity.	Hydrogen	74-76	sirtuin 2	Homo sapiens	28-33
22743824-1	2012	Sirtuin 6 (Sirt6), a mammalian Sir2 (silent information regulator-2) ortholog, is an NAD (+) -dependent histone deacetylase that modulates chromatin structure and genomic stability.	NAD	85-92	sirtuin 2	Homo sapiens	31-35
22743824-1	2012	Sirtuin 6 (Sirt6), a mammalian Sir2 (silent information regulator-2) ortholog, is an NAD (+) -dependent histone deacetylase that modulates chromatin structure and genomic stability.	NAD	85-92	sirtuin 2	Homo sapiens	37-67
23019416-0	2012	Inhibition of SIRT2 potentiates the anti-motility activity of taxanes: implications for antineoplastic combination therapies.	Taxoids	62-69	sirtuin 2	Homo sapiens	14-19
23019416-5	2012	Consistent with the hypothesis that tubulin deacetylase activity might affect cell response to the anti-motility activity of taxanes, we found that overexpression of the tubulin deacetylase SIRT2 increased cell motility and reduced cell response to the anti-motility activity of paclitaxel.	Taxoids	125-132	sirtuin 2	Homo sapiens	190-195
23019416-5	2012	Consistent with the hypothesis that tubulin deacetylase activity might affect cell response to the anti-motility activity of taxanes, we found that overexpression of the tubulin deacetylase SIRT2 increased cell motility and reduced cell response to the anti-motility activity of paclitaxel.	Paclitaxel	279-289	sirtuin 2	Homo sapiens	190-195
23019416-6	2012	Conversely, the SIRT2 inhibitor splitomicin reduced cell motility and potentiated the anti-motility activity of paclitaxel.	Paclitaxel	112-122	sirtuin 2	Homo sapiens	16-21
23019416-9	2012	This study indicates a role for SIRT2 in the regulation of cell motility and suggests that therapies combining sirtuin inhibitors and taxanes could be used to treat cell motility-based pathologic processes such as tumor angiogenesis, invasion, and metastasis.	Taxoids	134-141	sirtuin 2	Homo sapiens	32-37
22742936-5	2012	The results showed that hydrogen-rich saline reduced the level of malondialdehyde (MDA) and elevated the level of silent information regulator 2 (Sir2).	Hydrogen	24-32	sirtuin 2	Homo sapiens	146-150
22742936-5	2012	The results showed that hydrogen-rich saline reduced the level of malondialdehyde (MDA) and elevated the level of silent information regulator 2 (Sir2).	Sodium Chloride	38-44	sirtuin 2	Homo sapiens	114-144
22742936-5	2012	The results showed that hydrogen-rich saline reduced the level of malondialdehyde (MDA) and elevated the level of silent information regulator 2 (Sir2).	Sodium Chloride	38-44	sirtuin 2	Homo sapiens	146-150
22932127-5	2012	SIRT2, an NAD-dependent class III histone deacetylase, contributes to H4-K16Ac deacetylation and DNA compaction in human fibroblast cell lines that assemble striking senescence-associated heterochromatin foci (SAHFs).	NAD	10-13	sirtuin 2	Homo sapiens	0-5
22564257-2	2012	Owing to the absence of complex structure of sirtuin 2 (SIRT2), sirtinol was docked in the NAD(+) binding site and subjected to 5-nseconds molecular dynamics (MD) simulation.	sirtinol	64-72	sirtuin 2	Homo sapiens	56-61
22746324-0	2012	Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as sirtuin 2-selective inhibitors.	4-Chromanone	40-53	sirtuin 2	Homo sapiens	82-91
22746324-0	2012	Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as sirtuin 2-selective inhibitors.	Chromones	58-66	sirtuin 2	Homo sapiens	82-91
22746324-1	2012	A series of substituted chromone/chroman-4-one derivatives has been synthesized and evaluated as novel inhibitors of SIRT2, an enzyme involved in aging-related diseases, e.g., neurodegenerative disorders.	Chromones	24-32	sirtuin 2	Homo sapiens	117-122
22746324-1	2012	A series of substituted chromone/chroman-4-one derivatives has been synthesized and evaluated as novel inhibitors of SIRT2, an enzyme involved in aging-related diseases, e.g., neurodegenerative disorders.	4-Chromanone	33-46	sirtuin 2	Homo sapiens	117-122
22746324-5	2012	The most potent inhibitor of SIRT2 was 6,8-dibromo-2-pentylchroman-4-one with an IC(50) of 1.5 muM.	6,8-dibromo-2-pentylchroman-4-one	39-72	sirtuin 2	Homo sapiens	29-34
22634165-1	2012	Splitomicin, is a cell-permeable lactone derived from naphthol and known to be a potent selective inhibitor of Sir2 (silent information regulator 2).	splitomicin	0-11	sirtuin 2	Homo sapiens	111-115
22634165-1	2012	Splitomicin, is a cell-permeable lactone derived from naphthol and known to be a potent selective inhibitor of Sir2 (silent information regulator 2).	splitomicin	0-11	sirtuin 2	Homo sapiens	117-147
22634165-1	2012	Splitomicin, is a cell-permeable lactone derived from naphthol and known to be a potent selective inhibitor of Sir2 (silent information regulator 2).	Lactones	33-40	sirtuin 2	Homo sapiens	111-115
24340169-0	2012	The Discovery of Novel 10,11-Dihydro-5H-dibenz[b,f]azepine SIRT2 Inhibitors.	dibenzylamine	23-58	sirtuin 2	Homo sapiens	59-64
22642300-2	2012	On the basis of homology models of SIRT1 and SIRT2, we designed and prepared a series of 2-anilinobenzamide analogues.	2-(phenylamino)benzamide	89-107	sirtuin 2	Homo sapiens	45-50
22642300-3	2012	Enzyme assays using recombinant SIRT1 and SIRT2 revealed that 3"-phenethyloxy-2-anilinobenzamide analogues such as 33a and 33i are potent and selective SIRT2 inhibitors, showing more than 3.5-fold greater SIRT2-inhibitory activity and more than 35-fold greater SIRT2-selectivity compared with AGK2 (3), a previously reported SIRT2-selective inhibitor.	3"-phenethyloxy-2-anilinobenzamide	62-96	sirtuin 2	Homo sapiens	42-47
22642300-3	2012	Enzyme assays using recombinant SIRT1 and SIRT2 revealed that 3"-phenethyloxy-2-anilinobenzamide analogues such as 33a and 33i are potent and selective SIRT2 inhibitors, showing more than 3.5-fold greater SIRT2-inhibitory activity and more than 35-fold greater SIRT2-selectivity compared with AGK2 (3), a previously reported SIRT2-selective inhibitor.	3"-phenethyloxy-2-anilinobenzamide	62-96	sirtuin 2	Homo sapiens	152-157
22642300-3	2012	Enzyme assays using recombinant SIRT1 and SIRT2 revealed that 3"-phenethyloxy-2-anilinobenzamide analogues such as 33a and 33i are potent and selective SIRT2 inhibitors, showing more than 3.5-fold greater SIRT2-inhibitory activity and more than 35-fold greater SIRT2-selectivity compared with AGK2 (3), a previously reported SIRT2-selective inhibitor.	3"-phenethyloxy-2-anilinobenzamide	62-96	sirtuin 2	Homo sapiens	152-157
22642300-3	2012	Enzyme assays using recombinant SIRT1 and SIRT2 revealed that 3"-phenethyloxy-2-anilinobenzamide analogues such as 33a and 33i are potent and selective SIRT2 inhibitors, showing more than 3.5-fold greater SIRT2-inhibitory activity and more than 35-fold greater SIRT2-selectivity compared with AGK2 (3), a previously reported SIRT2-selective inhibitor.	3"-phenethyloxy-2-anilinobenzamide	62-96	sirtuin 2	Homo sapiens	152-157
22642300-3	2012	Enzyme assays using recombinant SIRT1 and SIRT2 revealed that 3"-phenethyloxy-2-anilinobenzamide analogues such as 33a and 33i are potent and selective SIRT2 inhibitors, showing more than 3.5-fold greater SIRT2-inhibitory activity and more than 35-fold greater SIRT2-selectivity compared with AGK2 (3), a previously reported SIRT2-selective inhibitor.	3"-phenethyloxy-2-anilinobenzamide	62-96	sirtuin 2	Homo sapiens	152-157
22642300-5	2012	These 3"-phenethyloxy-2-anilinobenzamide derivatives represent an entry into a new class of SIRT2-selective inhibitors.	3"-phenethyloxy-2-anilinobenzamide	6-40	sirtuin 2	Homo sapiens	92-97
22446090-0	2012	3-(N-arylsulfamoyl)benzamides, inhibitors of human sirtuin type 2 (SIRT2).	3-(n-arylsulfamoyl)benzamides	0-29	sirtuin 2	Homo sapiens	51-65
22446090-0	2012	3-(N-arylsulfamoyl)benzamides, inhibitors of human sirtuin type 2 (SIRT2).	3-(n-arylsulfamoyl)benzamides	0-29	sirtuin 2	Homo sapiens	67-72
22446090-3	2012	Here we report that N-methylation of 1a greatly increases its potency and results in excellent selectivity for SIRT2 over SIRT1 and SIRT3 isoforms.	Nitrogen	20-21	sirtuin 2	Homo sapiens	111-116
22446090-4	2012	Structure-activity relationships observed for 1a analogs and docking simulation data suggest that the para-substituted amido moiety of these compounds could occupy two potential hydrophobic binding pockets in SIRT2.	amido	119-124	sirtuin 2	Homo sapiens	209-214
21801305-2	2012	Salermide, a reverse amide compound that inhibits Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2), has been shown to induce apoptosis in human cancer cells.	N-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamide	0-9	sirtuin 2	Homo sapiens	72-81
21801305-2	2012	Salermide, a reverse amide compound that inhibits Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2), has been shown to induce apoptosis in human cancer cells.	N-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamide	0-9	sirtuin 2	Homo sapiens	83-88
21801305-2	2012	Salermide, a reverse amide compound that inhibits Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2), has been shown to induce apoptosis in human cancer cells.	Amides	21-26	sirtuin 2	Homo sapiens	72-81
22089141-6	2012	We demonstrated             that by using SIRT2-specific siRNA combined with tubacin treatment, the cell migratory             and invasive abilities were dramatically suppressed.	tubacin	77-84	sirtuin 2	Homo sapiens	42-47
22204321-5	2012	For examples, the key NAD(+)-dependent enzymes SIRT1 and SIRT2 have been indicated to strongly affect the pathological changes of PD and AD; PARP-1 inhibition can profoundly reduce the brain injury in the animal models of multiple neurological diseases; and administration of either NAD(+) or nicotinamide can also decrease ischemic brain damage.	NAD	22-28	sirtuin 2	Homo sapiens	57-62
22204321-5	2012	For examples, the key NAD(+)-dependent enzymes SIRT1 and SIRT2 have been indicated to strongly affect the pathological changes of PD and AD; PARP-1 inhibition can profoundly reduce the brain injury in the animal models of multiple neurological diseases; and administration of either NAD(+) or nicotinamide can also decrease ischemic brain damage.	NAD	283-289	sirtuin 2	Homo sapiens	57-62
22302938-0	2012	Dietary obesity-associated Hif1alpha activation in adipocytes restricts fatty acid oxidation and energy expenditure via suppression of the Sirt2-NAD+ system.	Fatty Acids	72-82	sirtuin 2	Homo sapiens	139-144
22204321-5	2012	For examples, the key NAD(+)-dependent enzymes SIRT1 and SIRT2 have been indicated to strongly affect the pathological changes of PD and AD; PARP-1 inhibition can profoundly reduce the brain injury in the animal models of multiple neurological diseases; and administration of either NAD(+) or nicotinamide can also decrease ischemic brain damage.	Niacinamide	293-305	sirtuin 2	Homo sapiens	57-62
22302938-0	2012	Dietary obesity-associated Hif1alpha activation in adipocytes restricts fatty acid oxidation and energy expenditure via suppression of the Sirt2-NAD+ system.	NAD	145-149	sirtuin 2	Homo sapiens	139-144
22302938-6	2012	Thus, by negatively regulating the Sirt2-Pgc1alpha regulatory axis, Hif1alpha negates adipocyte-intrinsic pathways of fatty acid catabolism, thereby creating a metabolic state supporting the development of obesity.	Fatty Acids	118-128	sirtuin 2	Homo sapiens	35-40
22157016-1	2012	SIRT1 is one of seven mammalian sirtuin (silent information regulator 2-related) proteins that harbor NAD(+)-dependent protein deacetylase activity and is implicated in multiple metabolic and age-associated pathways and disorders.	NAD	102-108	sirtuin 2	Homo sapiens	41-71
21244356-5	2011	Because sirtuin-2 activity depends on cellular NAD+ availability, mitochondrial regulation of NAD+ levels may contribute to an increase in sirtuin-mediated tubulin deacetylation.	NAD	47-51	sirtuin 2	Homo sapiens	8-17
22694102-3	2012	Unfortunately, SIRT2 complex structure is not available yet, hence molecular docking was carried out to dock the substrate (NAD(+) and acetylated lysine) and inhibitor (sirtinol) in the NAD(+) binding site.	NAD	124-130	sirtuin 2	Homo sapiens	15-20
22694102-3	2012	Unfortunately, SIRT2 complex structure is not available yet, hence molecular docking was carried out to dock the substrate (NAD(+) and acetylated lysine) and inhibitor (sirtinol) in the NAD(+) binding site.	Lysine	146-152	sirtuin 2	Homo sapiens	15-20
22694102-3	2012	Unfortunately, SIRT2 complex structure is not available yet, hence molecular docking was carried out to dock the substrate (NAD(+) and acetylated lysine) and inhibitor (sirtinol) in the NAD(+) binding site.	sirtinol	169-177	sirtuin 2	Homo sapiens	15-20
22694102-3	2012	Unfortunately, SIRT2 complex structure is not available yet, hence molecular docking was carried out to dock the substrate (NAD(+) and acetylated lysine) and inhibitor (sirtinol) in the NAD(+) binding site.	NAD	186-192	sirtuin 2	Homo sapiens	15-20
22511966-5	2012	SIRT2 is a NAD(+)-dependent deacetylase that has been proposed to deacetylate alpha-tubulin, histone H4 K16 and to regulate cholesterol biogenesis - a pathway which is dysregulated in HD patients and HD mouse models.	Cholesterol	124-135	sirtuin 2	Homo sapiens	0-5
21950728-1	2011	SIRT1 belongs to the silent information regulator 2 (Sir2) protein family of enzymes and functions as a NAD(+) -dependent class III histone deacetylase.	NAD	104-110	sirtuin 2	Homo sapiens	21-51
21950728-1	2011	SIRT1 belongs to the silent information regulator 2 (Sir2) protein family of enzymes and functions as a NAD(+) -dependent class III histone deacetylase.	NAD	104-110	sirtuin 2	Homo sapiens	53-57
21892612-9	2011	Mercaptosuccinate, a glutathione peroxidase (GPx-1) inhibitor or nicotinamide, a silent information regulator 2/sirtuin 1 (SIRT1) inhibitor could attenuate the antiapoptotic action of RSV on PMVECs; and RSV treatment upregulated GPx-1 and SIRT1 expression in PMVECs.	2-thiomalic acid	0-17	sirtuin 2	Homo sapiens	81-111
21892612-9	2011	Mercaptosuccinate, a glutathione peroxidase (GPx-1) inhibitor or nicotinamide, a silent information regulator 2/sirtuin 1 (SIRT1) inhibitor could attenuate the antiapoptotic action of RSV on PMVECs; and RSV treatment upregulated GPx-1 and SIRT1 expression in PMVECs.	Niacinamide	65-77	sirtuin 2	Homo sapiens	81-111
21892612-9	2011	Mercaptosuccinate, a glutathione peroxidase (GPx-1) inhibitor or nicotinamide, a silent information regulator 2/sirtuin 1 (SIRT1) inhibitor could attenuate the antiapoptotic action of RSV on PMVECs; and RSV treatment upregulated GPx-1 and SIRT1 expression in PMVECs.	Resveratrol	184-187	sirtuin 2	Homo sapiens	81-111
21244356-5	2011	Because sirtuin-2 activity depends on cellular NAD+ availability, mitochondrial regulation of NAD+ levels may contribute to an increase in sirtuin-mediated tubulin deacetylation.	NAD	94-98	sirtuin 2	Homo sapiens	8-17
21059157-1	2011	We previously reported that sirtuin 2 (SIRT2), a mammalian member of the NAD+-dependent protein deacetylases, participates in mitotic regulation, specifically, in efficient mitotic cell death caused by the spindle checkpoint.	NAD	73-76	sirtuin 2	Homo sapiens	28-37
21528845-2	2011	The new synthetic dinucleotides act as sirtuin (SIRT) inhibitors and show isoform selectivity for SIRT2 over SIRT1.	Dinucleoside Phosphates	18-31	sirtuin 2	Homo sapiens	98-103
21421831-1	2011	Sirtuins, the mammalian homologs of the silent information regulator 2 gene of Saccharomyces cerevisiae, are members of the NAD(+)-dependent family of histone deacetylases.	NAD	124-130	sirtuin 2	Homo sapiens	40-70
21306905-2	2011	In the first series (5a-t) we report a number of 2-substituted-1,2-dihydrobenzo[f]chromen-3-ones with a marked selectivity for the inhibition of SIRT2 over SIRT1.	2-substituted-1,2-dihydrobenzo[f]chromen-3-ones	49-96	sirtuin 2	Homo sapiens	145-150
21176092-1	2011	Silent information regulator 2 (Sir2) orthologs are an evolutionarily conserved family of NAD-dependent protein deacetylases that regulate aging and longevity in model organisms.	NAD	90-93	sirtuin 2	Homo sapiens	0-30
21176092-1	2011	Silent information regulator 2 (Sir2) orthologs are an evolutionarily conserved family of NAD-dependent protein deacetylases that regulate aging and longevity in model organisms.	NAD	90-93	sirtuin 2	Homo sapiens	32-36
21059157-1	2011	We previously reported that sirtuin 2 (SIRT2), a mammalian member of the NAD+-dependent protein deacetylases, participates in mitotic regulation, specifically, in efficient mitotic cell death caused by the spindle checkpoint.	NAD	73-76	sirtuin 2	Homo sapiens	39-44
21311214-6	2010	Furthermore we will discuss a particularly important role of several ROS-regulated genes and adapter proteins such as the p66shc, FOXO3a, and Sirt2.	Reactive Oxygen Species	69-72	sirtuin 2	Homo sapiens	142-147
20844277-1	2011	Human sirtuin (SIRT) 1 and SIRT2, which possess nicotinamide adenosine dinucleotide (NAD(+))-dependent deacetylase activity, exhibit anti-inflammatory actions.	nicotinamide adenosine dinucleotide	48-83	sirtuin 2	Homo sapiens	27-32
20844277-1	2011	Human sirtuin (SIRT) 1 and SIRT2, which possess nicotinamide adenosine dinucleotide (NAD(+))-dependent deacetylase activity, exhibit anti-inflammatory actions.	NAD	85-91	sirtuin 2	Homo sapiens	27-32
22132052-0	2010	Design of a novel nucleoside analog as potent inhibitor of the NAD dependent deacetylase, SIRT2.	Nucleosides	18-28	sirtuin 2	Homo sapiens	90-95
20962278-6	2010	PRLR dimerization and subsequent signaling are enhanced by treating the cells with deacetylase sirtuin (SIRT) inhibitor nicotinamide or histone deacetylase (HDAC) inhibitor trichostatin A but inhibited by expressing exogenous deacetylase SIRT2 or HDAC6.	Niacinamide	120-132	sirtuin 2	Homo sapiens	238-243
20798610-4	2010	In response to stress, FoxO1 dissociated from an NAD(+)-dependent histone deacetylase SIRT2 and FoxO1 thus became acetylated and in turn bound to Atg7, an E1-like protein, to influence the autophagic process leading to cell death.	NAD	49-55	sirtuin 2	Homo sapiens	86-91
20649551-3	2010	We demonstrated that excess ROS produced by defective mitochondria could increase the acetylation of microtubule proteins through the suppression of Sirt2, which results in perinuclear distribution of mitochondria in skin fibroblasts of patients with CPEO syndrome.	ros	28-31	sirtuin 2	Homo sapiens	149-154
20595677-1	2010	Sirtuins (silent information regulator 2 [Sir2] proteins) belong to an ancient family of evolutionary conserved nicotinamide adenine dinucleotide (NAD)(+)-dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity.	NAD	112-145	sirtuin 2	Homo sapiens	10-40
20595677-1	2010	Sirtuins (silent information regulator 2 [Sir2] proteins) belong to an ancient family of evolutionary conserved nicotinamide adenine dinucleotide (NAD)(+)-dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity.	NAD	112-145	sirtuin 2	Homo sapiens	42-46
20595677-1	2010	Sirtuins (silent information regulator 2 [Sir2] proteins) belong to an ancient family of evolutionary conserved nicotinamide adenine dinucleotide (NAD)(+)-dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity.	NAD	147-154	sirtuin 2	Homo sapiens	10-40
20595677-1	2010	Sirtuins (silent information regulator 2 [Sir2] proteins) belong to an ancient family of evolutionary conserved nicotinamide adenine dinucleotide (NAD)(+)-dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity.	NAD	147-154	sirtuin 2	Homo sapiens	42-46
20630764-0	2010	N(epsilon)-Modified lysine containing inhibitors for SIRT1 and SIRT2.	n(epsilon)-modified	0-19	sirtuin 2	Homo sapiens	63-68
20630764-0	2010	N(epsilon)-Modified lysine containing inhibitors for SIRT1 and SIRT2.	Lysine	20-26	sirtuin 2	Homo sapiens	63-68
20630764-2	2010	Here, an easy-to-synthesize Ac-Ala-Lys-Ala sequence has been used as a probe for the screening of novel N(epsilon)-modified lysine containing inhibitors against SIRT1 and SIRT2.	ac-ala-lys-ala	28-42	sirtuin 2	Homo sapiens	171-176
20630764-2	2010	Here, an easy-to-synthesize Ac-Ala-Lys-Ala sequence has been used as a probe for the screening of novel N(epsilon)-modified lysine containing inhibitors against SIRT1 and SIRT2.	n(epsilon)-modified	104-123	sirtuin 2	Homo sapiens	171-176
20630764-2	2010	Here, an easy-to-synthesize Ac-Ala-Lys-Ala sequence has been used as a probe for the screening of novel N(epsilon)-modified lysine containing inhibitors against SIRT1 and SIRT2.	Lysine	124-130	sirtuin 2	Homo sapiens	171-176
20237298-5	2010	Here we show that 2-hydroxy naphthyl derivatives, a previously identified subclass of NAD(+) analog inhibitors of sirtuin 2 (SIRT2), are direct gamma-secretase inhibitors.	2-hydroxy naphthyl	18-36	sirtuin 2	Homo sapiens	114-123
20237298-5	2010	Here we show that 2-hydroxy naphthyl derivatives, a previously identified subclass of NAD(+) analog inhibitors of sirtuin 2 (SIRT2), are direct gamma-secretase inhibitors.	2-hydroxy naphthyl	18-36	sirtuin 2	Homo sapiens	125-130
20237298-5	2010	Here we show that 2-hydroxy naphthyl derivatives, a previously identified subclass of NAD(+) analog inhibitors of sirtuin 2 (SIRT2), are direct gamma-secretase inhibitors.	NAD	86-92	sirtuin 2	Homo sapiens	114-123
20237298-5	2010	Here we show that 2-hydroxy naphthyl derivatives, a previously identified subclass of NAD(+) analog inhibitors of sirtuin 2 (SIRT2), are direct gamma-secretase inhibitors.	NAD	86-92	sirtuin 2	Homo sapiens	125-130
20371709-7	2010	Consistently, Sirtinol and Salermide, but not EX527, treatment resulted in the in vivo acetylation of the SIRT1/2 target p53 and SIRT2 target tubulin in MCF-7 cells, suggesting that EX527 is ineffective in inhibiting SIRT2 and that p53 mediates the cytotoxic function of Sirtinol and Salermide.	sirtinol	14-22	sirtuin 2	Homo sapiens	129-134
20378838-0	2010	SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis.	Sterols	56-62	sirtuin 2	Homo sapiens	0-5
20378838-3	2010	Genetic or pharmacologic inhibition of SIRT2 in a striatal neuron model of HD resulted in gene expression changes including significant down-regulation of RNAs responsible for sterol biosynthesis.	Sterols	176-182	sirtuin 2	Homo sapiens	39-44
20378838-5	2010	Importantly, manipulation of sterol biosynthesis at the transcriptional level mimicked SIRT2 inhibition, demonstrating that the metabolic effects of SIRT2 inhibition are sufficient to diminish mutant huntingtin toxicity.	Sterols	29-35	sirtuin 2	Homo sapiens	87-92
20378838-5	2010	Importantly, manipulation of sterol biosynthesis at the transcriptional level mimicked SIRT2 inhibition, demonstrating that the metabolic effects of SIRT2 inhibition are sufficient to diminish mutant huntingtin toxicity.	Sterols	29-35	sirtuin 2	Homo sapiens	149-154
20543840-5	2010	In response to stress, FoxO1 was acetylated by dissociation from sirtuin-2 (SIRT2), a NAD(+)-dependent histone deacetylase, and the acetylated FoxO1 bound to Atg7, an E1-like protein, to influence the autophagic process leading to cell death.	NAD	86-92	sirtuin 2	Homo sapiens	65-74
20543840-5	2010	In response to stress, FoxO1 was acetylated by dissociation from sirtuin-2 (SIRT2), a NAD(+)-dependent histone deacetylase, and the acetylated FoxO1 bound to Atg7, an E1-like protein, to influence the autophagic process leading to cell death.	NAD	86-92	sirtuin 2	Homo sapiens	76-81
20226541-0	2010	Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases.	NAD	13-16	sirtuin 2	Homo sapiens	27-31
20226541-1	2010	Since the discovery of NAD-dependent deacetylase activity of the silent information regulator-2 (SIR2) family ("sirtuins"), many exciting connections between protein deacetylation and energy metabolism have been revealed.	NAD	23-26	sirtuin 2	Homo sapiens	65-95
20226541-1	2010	Since the discovery of NAD-dependent deacetylase activity of the silent information regulator-2 (SIR2) family ("sirtuins"), many exciting connections between protein deacetylation and energy metabolism have been revealed.	NAD	23-26	sirtuin 2	Homo sapiens	97-101
20371709-7	2010	Consistently, Sirtinol and Salermide, but not EX527, treatment resulted in the in vivo acetylation of the SIRT1/2 target p53 and SIRT2 target tubulin in MCF-7 cells, suggesting that EX527 is ineffective in inhibiting SIRT2 and that p53 mediates the cytotoxic function of Sirtinol and Salermide.	sirtinol	14-22	sirtuin 2	Homo sapiens	217-222
20371709-7	2010	Consistently, Sirtinol and Salermide, but not EX527, treatment resulted in the in vivo acetylation of the SIRT1/2 target p53 and SIRT2 target tubulin in MCF-7 cells, suggesting that EX527 is ineffective in inhibiting SIRT2 and that p53 mediates the cytotoxic function of Sirtinol and Salermide.	N-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamide	27-36	sirtuin 2	Homo sapiens	129-134
20371709-7	2010	Consistently, Sirtinol and Salermide, but not EX527, treatment resulted in the in vivo acetylation of the SIRT1/2 target p53 and SIRT2 target tubulin in MCF-7 cells, suggesting that EX527 is ineffective in inhibiting SIRT2 and that p53 mediates the cytotoxic function of Sirtinol and Salermide.	N-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamide	27-36	sirtuin 2	Homo sapiens	217-222
19749157-3	2009	The measurement of MitoSox fluorescence showed that resveratrol attenuates both steady-state and high glucose (30 mM)-induced mtROS production in CAECs, an effect that was prevented by the knockdown of the protein deacetylase silent information regulator 2/sirtuin 1 (SIRT1), an intracellular target of resveratrol.	Resveratrol	52-63	sirtuin 2	Homo sapiens	226-256
19914676-1	2010	Peptides containing L-N(epsilon)-acetyl-lysine (L-AcK) or its side chain modified analogs were prepared and assayed using SIRT1, the prototypical human silent information regulator 2 (Sir2) enzyme.	Peptides	0-8	sirtuin 2	Homo sapiens	184-188
19914676-2	2010	While previous studies showed that the side chain acetyl group of L-AcK can be extended to bulkier acyl groups for Sir2 (including SIRT1)-catalyzed lysine N(epsilon)-deacylation reaction, our current study suggested that SIRT1-catalyzed deacetylation reaction had a very stringent requirement for the distance between the alpha-carbon and the side chain acetamido group, with that found in L-AcK being optimal.	Lysine	148-154	sirtuin 2	Homo sapiens	115-119
19914676-2	2010	While previous studies showed that the side chain acetyl group of L-AcK can be extended to bulkier acyl groups for Sir2 (including SIRT1)-catalyzed lysine N(epsilon)-deacylation reaction, our current study suggested that SIRT1-catalyzed deacetylation reaction had a very stringent requirement for the distance between the alpha-carbon and the side chain acetamido group, with that found in L-AcK being optimal.	Carbon	328-334	sirtuin 2	Homo sapiens	115-119
19749157-3	2009	The measurement of MitoSox fluorescence showed that resveratrol attenuates both steady-state and high glucose (30 mM)-induced mtROS production in CAECs, an effect that was prevented by the knockdown of the protein deacetylase silent information regulator 2/sirtuin 1 (SIRT1), an intracellular target of resveratrol.	Glucose	102-109	sirtuin 2	Homo sapiens	226-256
19268440-5	2009	The isotypes responsible for tubulin deacetylation are HDAC6 and the NAD(+)-dependent histone deacetylase (sirtuin) Sirt2.	NAD	69-75	sirtuin 2	Homo sapiens	116-121
19559674-2	2009	In this study, we identified a novel SIRT2 inhibitor, AC-93253, with IC(50) of 6 microM in vitro.	AC 93253	54-62	sirtuin 2	Homo sapiens	37-42
19559674-4	2009	AC-93253 significantly enhanced acetylation of tubulin, p53, and histone H4, confirming SIRT2 and SIRT1 as its cellular targets.	AC 93253	0-8	sirtuin 2	Homo sapiens	88-93
19559674-7	2009	Taken together, SIRT2 selective inhibitor AC-93253 may serve as a novel chemical scaffold for structure-activity relationship study and future lead development.	AC 93253	42-50	sirtuin 2	Homo sapiens	16-21
19285066-2	2009	Additionally, resveratrol is a potent activator of the Sirt1/Sir2 (silent information regulator 2) family of NAD-dependent deacetylases which plays a role in calorie restriction-mediated tumor suppression.	Resveratrol	14-25	sirtuin 2	Homo sapiens	61-65
19327818-1	2009	Splitomicin is derived from beta-naphthol and is an inhibitor of Silent Information Regulator 2 (SIR2).	splitomicin	0-11	sirtuin 2	Homo sapiens	65-95
19327818-1	2009	Splitomicin is derived from beta-naphthol and is an inhibitor of Silent Information Regulator 2 (SIR2).	splitomicin	0-11	sirtuin 2	Homo sapiens	97-101
19413317-2	2009	Among the compounds thus designed and synthesized, we found that 2k, which contains an ethoxycarbonyl group at the alpha position to the acetamide of acetylated lysine substrate analogue 1, showed potent inhibitory activity in an in vitro assay using recombinant SIRT1, with high selectivity over SIRT2 and SIRT3.	acetamide	137-146	sirtuin 2	Homo sapiens	297-302
19413317-2	2009	Among the compounds thus designed and synthesized, we found that 2k, which contains an ethoxycarbonyl group at the alpha position to the acetamide of acetylated lysine substrate analogue 1, showed potent inhibitory activity in an in vitro assay using recombinant SIRT1, with high selectivity over SIRT2 and SIRT3.	Lysine	161-167	sirtuin 2	Homo sapiens	297-302
19285066-2	2009	Additionally, resveratrol is a potent activator of the Sirt1/Sir2 (silent information regulator 2) family of NAD-dependent deacetylases which plays a role in calorie restriction-mediated tumor suppression.	Resveratrol	14-25	sirtuin 2	Homo sapiens	67-97
19060927-1	2009	Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2) belong to the family of NAD+ (nicotinamide adenine dinucleotide-positive)-dependent class III histone deacetylases and are involved in regulating lifespan.	NAD	64-68	sirtuin 2	Homo sapiens	22-31
19282667-1	2009	We previously identified SIRT2, a deacetylase for tubulin and histone H4, as a protein downregulated in gliomas, and reported that exogenously-expressed SIRT2 arrests the cell cycle prior to entry into mitosis to prevent chromosomal instability in response to microtubule inhibitors (MTIs) such as nocodazole, characteristics previously reported for the CHFR protein.	Nocodazole	298-308	sirtuin 2	Homo sapiens	25-30
19282667-1	2009	We previously identified SIRT2, a deacetylase for tubulin and histone H4, as a protein downregulated in gliomas, and reported that exogenously-expressed SIRT2 arrests the cell cycle prior to entry into mitosis to prevent chromosomal instability in response to microtubule inhibitors (MTIs) such as nocodazole, characteristics previously reported for the CHFR protein.	Nocodazole	298-308	sirtuin 2	Homo sapiens	153-158
19282667-5	2009	Consistent with this notion, BubR1 downregulation was dominant over SIRT2 knockdown in regard to mitotic regulation in the presence of nocodazole.	Nocodazole	135-145	sirtuin 2	Homo sapiens	68-73
19282667-7	2009	We also found that SIRT2 downregulation caused centrosome fragmentation in response to nocodazole prior to the alteration in spindle checkpoint function, implying not only a novel function of SIRT2 for centrosome maintenance upon exposure to mitotic stress caused by MTIs, but also the existence of a centrosome-mediated signaling pathway to sustain the spindle checkpoint.	Nocodazole	87-97	sirtuin 2	Homo sapiens	19-24
19060927-1	2009	Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2) belong to the family of NAD+ (nicotinamide adenine dinucleotide-positive)-dependent class III histone deacetylases and are involved in regulating lifespan.	NAD	64-68	sirtuin 2	Homo sapiens	33-38
19060927-1	2009	Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2) belong to the family of NAD+ (nicotinamide adenine dinucleotide-positive)-dependent class III histone deacetylases and are involved in regulating lifespan.	NAD	70-103	sirtuin 2	Homo sapiens	22-31
19060927-1	2009	Sirtuin 1 (Sirt1) and Sirtuin 2 (Sirt2) belong to the family of NAD+ (nicotinamide adenine dinucleotide-positive)-dependent class III histone deacetylases and are involved in regulating lifespan.	NAD	70-103	sirtuin 2	Homo sapiens	33-38
19060927-3	2009	Here we present Salermide (N-{3-[(2-hydroxy-naphthalen-1-ylmethylene)-amino]-phenyl}-2-phenyl-propionamide), a reverse amide with a strong in vitro inhibitory effect on Sirt1 and Sirt2.	N-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamide	16-25	sirtuin 2	Homo sapiens	179-184
19060927-3	2009	Here we present Salermide (N-{3-[(2-hydroxy-naphthalen-1-ylmethylene)-amino]-phenyl}-2-phenyl-propionamide), a reverse amide with a strong in vitro inhibitory effect on Sirt1 and Sirt2.	N-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamide	27-106	sirtuin 2	Homo sapiens	179-184
19060927-3	2009	Here we present Salermide (N-{3-[(2-hydroxy-naphthalen-1-ylmethylene)-amino]-phenyl}-2-phenyl-propionamide), a reverse amide with a strong in vitro inhibitory effect on Sirt1 and Sirt2.	Amides	101-106	sirtuin 2	Homo sapiens	179-184
19010386-2	2009	The lifespan extension effect of CR has been strongly associated with an increased level and activation of the silent information regulator 2 (Sir2) histone deacetylase and its mammalian ortholog Sirt1.	Chromium	33-35	sirtuin 2	Homo sapiens	111-141
19010386-2	2009	The lifespan extension effect of CR has been strongly associated with an increased level and activation of the silent information regulator 2 (Sir2) histone deacetylase and its mammalian ortholog Sirt1.	Chromium	33-35	sirtuin 2	Homo sapiens	143-147
19037106-7	2009	Intraperitoneal injection of a beta-adrenergic agonist (isoproterenol) enhances SIRT2 expression in white adipose tissue.	Isoproterenol	56-69	sirtuin 2	Homo sapiens	80-85
19037106-9	2009	SIRT2 inhibits 3T3-L1 adipocyte differentiation in low-glucose (1 g/l) or low-insulin (100 nM) condition.	Glucose	55-62	sirtuin 2	Homo sapiens	0-5
18722353-2	2008	Sirt proteins are mammalian members of the Sir2 family of NAD+ (nicotinamide adenine dinucleotide)-dependent protein deacetylases.	NAD	58-62	sirtuin 2	Homo sapiens	43-47
18985648-7	2008	The analyses suggested a molecular basis for the interaction of the identified thiobarbiturate derivatives with human Sirt2.	thiobarbituric acid	79-94	sirtuin 2	Homo sapiens	118-123
18995842-3	2008	We found that the NAD(+)-dependent histone deacetylase SIRT2 deacetylates p300 in vitro and in cells.	NAD	18-24	sirtuin 2	Homo sapiens	55-60
18995842-4	2008	SIRT2 deacetylates lysine residues in the catalytic domain of p300 and restores binding of p300 to the PIC.	Lysine	19-25	sirtuin 2	Homo sapiens	0-5
18722353-2	2008	Sirt proteins are mammalian members of the Sir2 family of NAD+ (nicotinamide adenine dinucleotide)-dependent protein deacetylases.	NAD	64-97	sirtuin 2	Homo sapiens	43-47
18332217-3	2008	We identify on protein expression arrays novel cyclin E-Cdk2 substrates, including SIRT2, a member of the Sirtuin family of NAD(+)-dependent deacetylases that targets alpha-tubulin.	NAD	124-130	sirtuin 2	Homo sapiens	83-88
18642893-0	2008	Oxadiazole-carbonylaminothioureas as SIRT1 and SIRT2 inhibitors.	Oxadiazoles	0-10	sirtuin 2	Homo sapiens	47-52
18701307-0	2008	Characterization of the binding properties of SIRT2 inhibitors with a N-(3-phenylpropenoyl)-glycine tryptamide backbone.	n-(3-phenylpropenoyl)-glycine tryptamide	70-110	sirtuin 2	Homo sapiens	46-51
18701307-6	2008	The N-(3-phenylpropenoyl)-glycine tryptamide backbone is also a good backbone for SIRT2 inhibitors, and the series of compounds includes several potent SIRT2 inhibitors.	n-(3-phenylpropenoyl)-glycine tryptamide	4-44	sirtuin 2	Homo sapiens	82-87
18701307-6	2008	The N-(3-phenylpropenoyl)-glycine tryptamide backbone is also a good backbone for SIRT2 inhibitors, and the series of compounds includes several potent SIRT2 inhibitors.	n-(3-phenylpropenoyl)-glycine tryptamide	4-44	sirtuin 2	Homo sapiens	152-157
18249187-1	2008	Sirt2 is a mammalian member of the Sirtuin family of NAD(+) (nicotinamide adenine dinucleotide)-dependent protein deacetylases.	NAD	53-59	sirtuin 2	Homo sapiens	0-5
18332217-5	2008	Importantly, phosphorylation at Ser-331 inhibits the catalytic activity of SIRT2.	Serine	32-35	sirtuin 2	Homo sapiens	75-80
18044719-1	2008	The mammalian silent information regulator 2 (SIRT2) is an NAD-dependent histone deacetylase with known roles in the regulation of the cell cycle.	NAD	59-62	sirtuin 2	Homo sapiens	14-44
18249187-5	2008	Treatment of cells with nicotinamide, an inhibitor of Sirtuins, relieves the inhibition of p53 by Sirt2 and 14-3-3 beta/gamma.	Niacinamide	24-36	sirtuin 2	Homo sapiens	98-119
18044719-1	2008	The mammalian silent information regulator 2 (SIRT2) is an NAD-dependent histone deacetylase with known roles in the regulation of the cell cycle.	NAD	59-62	sirtuin 2	Homo sapiens	46-51
18221243-6	2008	The protein implicated in this protective process is the silent information regulator 2 (SIR2, SIRT1 in mammals), an enzyme that belongs to a nicotinamide adenine dinucleotide (NAD)+-dependent protein deacetylases.	NAD	142-175	sirtuin 2	Homo sapiens	57-87
18269226-6	2008	These analyses suggested a molecular basis for the interaction of the beta-phenylsplitomicins with human Sirt2.	beta-phenylsplitomicins	70-93	sirtuin 2	Homo sapiens	105-110
18221243-6	2008	The protein implicated in this protective process is the silent information regulator 2 (SIR2, SIRT1 in mammals), an enzyme that belongs to a nicotinamide adenine dinucleotide (NAD)+-dependent protein deacetylases.	NAD	142-175	sirtuin 2	Homo sapiens	89-93
17628866-7	2007	We tested a diverse set of suramin analogues to elucidate the inhibition of the NAD(+)-dependent histone deacetylases SIRT1 and SIRT2 and discovered selective inhibitors of human sirtuins with potency in the two-digit nanomolar range.	Suramin	27-34	sirtuin 2	Homo sapiens	128-133
17951578-1	2007	Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2"-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.	NAD	63-67	sirtuin 2	Homo sapiens	32-36
17951578-1	2007	Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2"-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.	N(alpha)-acetyllysine	92-105	sirtuin 2	Homo sapiens	32-36
17951578-1	2007	Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2"-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.	Niacinamide	118-130	sirtuin 2	Homo sapiens	32-36
17951578-1	2007	Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2"-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.	2-O-acetyl-ADP-ribose	132-154	sirtuin 2	Homo sapiens	32-36
17951578-1	2007	Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2"-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.	2-O-acetyl-ADP-ribose	156-162	sirtuin 2	Homo sapiens	32-36
17951578-1	2007	Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2"-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.	Lysine	99-105	sirtuin 2	Homo sapiens	32-36
17951578-5	2007	Interestingly, propionyl- and butyryl-lysine peptides were found to bind tighter to Hst2 compared with acetyl-lysine peptide and showed measurable rates of catalysis with Hst2, Sirt1, Sirt2, and Sirt3, suggesting propionyl- and butyryl-lysine proteins may be sirtuin substrates in vivo.	Lysine	38-44	sirtuin 2	Homo sapiens	184-189
18027980-1	2007	Sir2 protein deacetylases (or sirtuins) catalyze NAD+-dependent conversion of epsilon-amino-acetylated lysine residues to deacetylated lysine, nicotinamide, and 2"-O-acetyl-ADP-ribose.	NAD	49-53	sirtuin 2	Homo sapiens	0-4
18027980-1	2007	Sir2 protein deacetylases (or sirtuins) catalyze NAD+-dependent conversion of epsilon-amino-acetylated lysine residues to deacetylated lysine, nicotinamide, and 2"-O-acetyl-ADP-ribose.	Lysine	103-109	sirtuin 2	Homo sapiens	0-4
18027980-1	2007	Sir2 protein deacetylases (or sirtuins) catalyze NAD+-dependent conversion of epsilon-amino-acetylated lysine residues to deacetylated lysine, nicotinamide, and 2"-O-acetyl-ADP-ribose.	Lysine	135-141	sirtuin 2	Homo sapiens	0-4
18027980-1	2007	Sir2 protein deacetylases (or sirtuins) catalyze NAD+-dependent conversion of epsilon-amino-acetylated lysine residues to deacetylated lysine, nicotinamide, and 2"-O-acetyl-ADP-ribose.	Niacinamide	143-155	sirtuin 2	Homo sapiens	0-4
18027980-1	2007	Sir2 protein deacetylases (or sirtuins) catalyze NAD+-dependent conversion of epsilon-amino-acetylated lysine residues to deacetylated lysine, nicotinamide, and 2"-O-acetyl-ADP-ribose.	2-O-acetyl-ADP-ribose	161-183	sirtuin 2	Homo sapiens	0-4
18027980-4	2007	Although all substituted peptides yielded inhibition of the deacetylation reaction, the thioacetyl-lysine peptide exhibited exceptionally potent inhibition of sirtuins Sirt1, Sirt2, Sirt3, and Hst2.	thioacetyl-lysine peptide	88-113	sirtuin 2	Homo sapiens	175-180
17628866-7	2007	We tested a diverse set of suramin analogues to elucidate the inhibition of the NAD(+)-dependent histone deacetylases SIRT1 and SIRT2 and discovered selective inhibitors of human sirtuins with potency in the two-digit nanomolar range.	NAD	80-86	sirtuin 2	Homo sapiens	128-133
17628866-9	2007	The recently published X-ray crystal structure of human SIRT5 in complex with suramin and the human SIRT2 structure were used to analyze the interaction mode of the novel suramin derivatives.	Suramin	171-178	sirtuin 2	Homo sapiens	100-105
17726514-1	2007	The human NAD+-dependent protein deacetylase SIRT2 resides predominantly in the cytoplasm where it functions as a tubulin deacetylase.	NAD	10-14	sirtuin 2	Homo sapiens	45-50
17516032-5	2007	In addition, we show that replacement of specific serines with alanines in either isoform of SIRT2 regulates its enzymatic activity.	Serine	50-57	sirtuin 2	Homo sapiens	93-98
17516032-5	2007	In addition, we show that replacement of specific serines with alanines in either isoform of SIRT2 regulates its enzymatic activity.	Alanine	63-71	sirtuin 2	Homo sapiens	93-98
17516032-7	2007	SIRT2 was found to be phosphorylated at serines 368 and 372, outside the conserved core domain of the Sir2 protein family.	Serine	40-47	sirtuin 2	Homo sapiens	0-5
17516032-9	2007	Replacements of other serine, threonine, and tyrosine residues, which did not alter the phosphorylation pattern, had varying effects on SIRT2 deacetylase activity but no effect on tubulin/HDAC6 binding.	Serine	22-28	sirtuin 2	Homo sapiens	136-141
17516032-9	2007	Replacements of other serine, threonine, and tyrosine residues, which did not alter the phosphorylation pattern, had varying effects on SIRT2 deacetylase activity but no effect on tubulin/HDAC6 binding.	Tyrosine	45-53	sirtuin 2	Homo sapiens	136-141
17726514-3	2007	We identified a functional, leptomycin B-sensitive, nuclear export signal sequence within SIRT2.	leptomycin B	28-40	sirtuin 2	Homo sapiens	90-95
17456799-1	2007	Sirtuins or Sir2 (silent information regulator 2)-related enzymes have originally been defined as a family of nicotinamide adenine dinucleotide-dependent enzymes that deacetylate lysine residue on various proteins.	NAD	110-143	sirtuin 2	Homo sapiens	12-16
17694090-6	2007	One of the key factors that might have contributed to this preservation is the intimate relationship between some members of this group of proteins (SirT1, SirT2 and SirT3) and deacetylation of a specific residue in histone H4, lysine 16 (H4K16).	Lysine	228-234	sirtuin 2	Homo sapiens	156-161
17521387-7	2007	Oxidative stress, such as hydrogen peroxide treatment, also increases SIRT2 expression in cells.	Hydrogen Peroxide	26-43	sirtuin 2	Homo sapiens	70-75
17521387-10	2007	As a consequence, SIRT2 decreases cellular levels of reactive oxygen species.	Reactive Oxygen Species	53-76	sirtuin 2	Homo sapiens	18-23
17456799-1	2007	Sirtuins or Sir2 (silent information regulator 2)-related enzymes have originally been defined as a family of nicotinamide adenine dinucleotide-dependent enzymes that deacetylate lysine residue on various proteins.	NAD	110-143	sirtuin 2	Homo sapiens	18-48
17456799-1	2007	Sirtuins or Sir2 (silent information regulator 2)-related enzymes have originally been defined as a family of nicotinamide adenine dinucleotide-dependent enzymes that deacetylate lysine residue on various proteins.	Lysine	179-185	sirtuin 2	Homo sapiens	12-16
17456799-1	2007	Sirtuins or Sir2 (silent information regulator 2)-related enzymes have originally been defined as a family of nicotinamide adenine dinucleotide-dependent enzymes that deacetylate lysine residue on various proteins.	Lysine	179-185	sirtuin 2	Homo sapiens	18-48
17583434-5	2007	We study the role of the mammalian silent information regulator 2 (SIRT1) in the process of neuroprotection mediated by resveratrol.	Resveratrol	120-131	sirtuin 2	Homo sapiens	35-65
17574768-5	2007	Nicotinamide but not 3-aminobenzamide, an inhibitor for poly(ADP)ribose polymerase, enhanced tubulin acetylation and resistance to axonal degeneration in cultured cerebellar granule cells from wild-type (WT) mice, suggesting that mammalian Sir2-related protein (SIRT) 2, a nicotinamide adenine dinucleotide (NAD)--dependent tubulin deacetylase, could modulate resistance to axonal degeneration.	Niacinamide	0-12	sirtuin 2	Homo sapiens	240-269
17457050-1	2007	Sir2, an NAD+-dependent protein deacetylase, extends the lifespan in diverse species from yeast to flies.	NAD	9-12	sirtuin 2	Homo sapiens	0-4
17488717-3	2007	Here, we demonstrate that SIRT2 is phosphorylated both in vitro and in vivo on serine 368 by the cell-cycle regulator, cyclin-dependent kinase 1, and dephosphorylated by the phosphatases CDC14A and CDC14B.	Serine	79-85	sirtuin 2	Homo sapiens	26-31
17488717-4	2007	Overexpression of SIRT2 mediates a delay in cellular proliferation that is dependent on serine 368 phosphorylation.	Serine	88-94	sirtuin 2	Homo sapiens	18-23
17329104-0	2007	N-(3-(4-Hydroxyphenyl)-propenoyl)-amino acid tryptamides as SIRT2 inhibitors.	n-(3-(4-hydroxyphenyl)-propenoyl)-amino acid tryptamides	0-56	sirtuin 2	Homo sapiens	60-65
17329104-1	2007	A series of N-(3-(4-hydroxyphenyl)-propenoyl)-amino acid tryptamides was based on a previously reported new SIRT2 inhibitor from our group, and it was designed to study if the molecular size of the compound could be reduced.	n-(3-(4-hydroxyphenyl)-propenoyl)-amino acid tryptamides	12-68	sirtuin 2	Homo sapiens	108-113
17329104-2	2007	The most potent compounds, N-(3-(4-hydroxyphenyl)-propenoyl)-2-aminoisobutyric acid tryptamide and N-(3-(4-hydroxyphenyl)-propenoyl)-L-alanine tryptamide, were equipotent, 30% smaller in molecular weight, and slightly more selective (SIRT2/SIRT1) than the parent compound.	n-(3-(4-hydroxyphenyl)-propenoyl)-2-aminoisobutyric acid tryptamide	27-94	sirtuin 2	Homo sapiens	234-239
17329104-2	2007	The most potent compounds, N-(3-(4-hydroxyphenyl)-propenoyl)-2-aminoisobutyric acid tryptamide and N-(3-(4-hydroxyphenyl)-propenoyl)-L-alanine tryptamide, were equipotent, 30% smaller in molecular weight, and slightly more selective (SIRT2/SIRT1) than the parent compound.	n-(3-(4-hydroxyphenyl)-propenoyl)-l-alanine tryptamide	99-153	sirtuin 2	Homo sapiens	234-239
16909107-7	2007	Although SIRT2 is normally exclusively located in the cytoplasm, the rapid accumulation of SIRT2 in the nucleus was observed after treatment with a nuclear export inhibitor, leptomycin B and ionizing radiation in normal human fibroblasts, suggesting that nucleo-cytoplasmic shuttling regulates the SIRT2 function.	leptomycin B	174-186	sirtuin 2	Homo sapiens	91-96
16909107-1	2007	We previously identified SIRT2, an nicotinamide adenine dinucleotide (NAD)-dependent tubulin deacetylase, as a protein downregulated in gliomas and glioma cell lines, which are characterized by aneuploidy.	NAD	35-68	sirtuin 2	Homo sapiens	25-30
16909107-7	2007	Although SIRT2 is normally exclusively located in the cytoplasm, the rapid accumulation of SIRT2 in the nucleus was observed after treatment with a nuclear export inhibitor, leptomycin B and ionizing radiation in normal human fibroblasts, suggesting that nucleo-cytoplasmic shuttling regulates the SIRT2 function.	leptomycin B	174-186	sirtuin 2	Homo sapiens	91-96
16909107-1	2007	We previously identified SIRT2, an nicotinamide adenine dinucleotide (NAD)-dependent tubulin deacetylase, as a protein downregulated in gliomas and glioma cell lines, which are characterized by aneuploidy.	NAD	70-73	sirtuin 2	Homo sapiens	25-30
17181175-0	2006	N,N"-Bisbenzylidenebenzene-1,4-diamines and N,N"-Bisbenzylidenenaphthalene-1,4-diamines as Sirtuin Type 2 (SIRT2) Inhibitors.	n,n"-bisbenzylidenebenzene-1,4-diamines	0-39	sirtuin 2	Homo sapiens	91-105
17516596-0	2007	Phloroglucinol derivatives guttiferone G, aristoforin, and hyperforin: inhibitors of human sirtuins SIRT1 and SIRT2.	Phloroglucinol	0-14	sirtuin 2	Homo sapiens	110-115
17516596-0	2007	Phloroglucinol derivatives guttiferone G, aristoforin, and hyperforin: inhibitors of human sirtuins SIRT1 and SIRT2.	guttiferone G	27-40	sirtuin 2	Homo sapiens	110-115
17516596-0	2007	Phloroglucinol derivatives guttiferone G, aristoforin, and hyperforin: inhibitors of human sirtuins SIRT1 and SIRT2.	Aristoforin	42-53	sirtuin 2	Homo sapiens	110-115
17516596-0	2007	Phloroglucinol derivatives guttiferone G, aristoforin, and hyperforin: inhibitors of human sirtuins SIRT1 and SIRT2.	hyperforin	59-69	sirtuin 2	Homo sapiens	110-115
17214740-1	2007	Silent information regulator 2 (Sir2)-related proteins or sirtuins function as NAD(+)-dependent deacetylases or ADP ribosylases that target a range of substrates, thereby influencing chromatin structure and a diverse range of other biological functions.	NAD	79-85	sirtuin 2	Homo sapiens	0-30
17181175-0	2006	N,N"-Bisbenzylidenebenzene-1,4-diamines and N,N"-Bisbenzylidenenaphthalene-1,4-diamines as Sirtuin Type 2 (SIRT2) Inhibitors.	n,n"-bisbenzylidenebenzene-1,4-diamines	0-39	sirtuin 2	Homo sapiens	107-112
17181175-0	2006	N,N"-Bisbenzylidenebenzene-1,4-diamines and N,N"-Bisbenzylidenenaphthalene-1,4-diamines as Sirtuin Type 2 (SIRT2) Inhibitors.	n,n"-bisbenzylidenenaphthalene-1,4-diamines	44-87	sirtuin 2	Homo sapiens	91-105
17181175-0	2006	N,N"-Bisbenzylidenebenzene-1,4-diamines and N,N"-Bisbenzylidenenaphthalene-1,4-diamines as Sirtuin Type 2 (SIRT2) Inhibitors.	n,n"-bisbenzylidenenaphthalene-1,4-diamines	44-87	sirtuin 2	Homo sapiens	107-112
17181175-1	2006	A series of N,N"-bisbenzylidenebenzene-1,4-diamine and N,N"-bisbenzylidenenaphthalene-1,4-diamine derivatives were synthesized as inhibitors for human sirtuin type 2 (SIRT2).	n,n"-bisbenzylidenebenzene-1,4-diamine	12-50	sirtuin 2	Homo sapiens	151-165
17181175-1	2006	A series of N,N"-bisbenzylidenebenzene-1,4-diamine and N,N"-bisbenzylidenenaphthalene-1,4-diamine derivatives were synthesized as inhibitors for human sirtuin type 2 (SIRT2).	n,n"-bisbenzylidenebenzene-1,4-diamine	12-50	sirtuin 2	Homo sapiens	167-172
17181175-1	2006	A series of N,N"-bisbenzylidenebenzene-1,4-diamine and N,N"-bisbenzylidenenaphthalene-1,4-diamine derivatives were synthesized as inhibitors for human sirtuin type 2 (SIRT2).	n,n"-bisbenzylidenenaphthalene-1,4-diamine	55-97	sirtuin 2	Homo sapiens	151-165
17181175-1	2006	A series of N,N"-bisbenzylidenebenzene-1,4-diamine and N,N"-bisbenzylidenenaphthalene-1,4-diamine derivatives were synthesized as inhibitors for human sirtuin type 2 (SIRT2).	n,n"-bisbenzylidenenaphthalene-1,4-diamine	55-97	sirtuin 2	Homo sapiens	167-172
17181175-3	2006	The most potent compound was N,N"-bis(2-hydroxybenzylidene)benzene-1,4-diamine, which was equipotent with the most potent hit compound and well-known SIRT2 inhibitor sirtinol.	N,N'-bis(2-hydroxybenzylidene)benzene-1,4-diamine	29-78	sirtuin 2	Homo sapiens	150-155
17181175-3	2006	The most potent compound was N,N"-bis(2-hydroxybenzylidene)benzene-1,4-diamine, which was equipotent with the most potent hit compound and well-known SIRT2 inhibitor sirtinol.	sirtinol	166-174	sirtuin 2	Homo sapiens	150-155
16565078-6	2006	Using cell-based assays and RNA interference, we show that puromycin-induced cell death is greatly diminished by nicotinamide (a potent sirtuin inhibitor), and by decreased expression of sirtuins SIRT2 and SIRT3.	Puromycin	59-68	sirtuin 2	Homo sapiens	196-201
16982188-2	2006	The molecular electrostatic potentials (MESP), the cavity depth analysis, and LmSIR2-hSIRT2 models" superposition suggested that the nicotinamide binding catalytic domain has several minor but potentially important structural differences.	Niacinamide	133-145	sirtuin 2	Homo sapiens	85-91
16395277-1	2006	Recent studies in a variety of species including mammals showed that resveratrol (trans-3, 5, 4""-trihydroxystibene) treatment and caloric restriction increased silent information regulator 2/sirtuin 1 activity, which mediated increase in life span/cell survival.	Resveratrol	69-80	sirtuin 2	Homo sapiens	161-191
16395277-1	2006	Recent studies in a variety of species including mammals showed that resveratrol (trans-3, 5, 4""-trihydroxystibene) treatment and caloric restriction increased silent information regulator 2/sirtuin 1 activity, which mediated increase in life span/cell survival.	trans-3, 5, 4""-trihydroxystibene	82-115	sirtuin 2	Homo sapiens	161-191
17075046-0	2006	The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases.	O-Acetyl-ADP-Ribose	59-78	sirtuin 2	Homo sapiens	97-101
17075046-1	2006	The silent information regulator 2 (Sir2) family of NAD-dependent N-acetyl-protein deacetylases participates in the regulation of gene silencing, chromatin structure, and longevity.	NAD	52-55	sirtuin 2	Homo sapiens	4-34
17075046-1	2006	The silent information regulator 2 (Sir2) family of NAD-dependent N-acetyl-protein deacetylases participates in the regulation of gene silencing, chromatin structure, and longevity.	NAD	52-55	sirtuin 2	Homo sapiens	36-40
17075046-2	2006	In the Sir2-catalyzed reaction, the acetyl moiety of N-acetyl-histone is transferred to the ADP-ribose of NAD, yielding O-acetyl-ADP-ribose and nicotinamide.	n-acetyl-histone	53-69	sirtuin 2	Homo sapiens	7-11
17075046-2	2006	In the Sir2-catalyzed reaction, the acetyl moiety of N-acetyl-histone is transferred to the ADP-ribose of NAD, yielding O-acetyl-ADP-ribose and nicotinamide.	Adenosine Diphosphate Ribose	92-102	sirtuin 2	Homo sapiens	7-11
17075046-2	2006	In the Sir2-catalyzed reaction, the acetyl moiety of N-acetyl-histone is transferred to the ADP-ribose of NAD, yielding O-acetyl-ADP-ribose and nicotinamide.	NAD	106-109	sirtuin 2	Homo sapiens	7-11
17075046-2	2006	In the Sir2-catalyzed reaction, the acetyl moiety of N-acetyl-histone is transferred to the ADP-ribose of NAD, yielding O-acetyl-ADP-ribose and nicotinamide.	O-Acetyl-ADP-Ribose	120-139	sirtuin 2	Homo sapiens	7-11
17075046-2	2006	In the Sir2-catalyzed reaction, the acetyl moiety of N-acetyl-histone is transferred to the ADP-ribose of NAD, yielding O-acetyl-ADP-ribose and nicotinamide.	Niacinamide	144-156	sirtuin 2	Homo sapiens	7-11
17075046-10	2006	All data support the conclusion that the Sir2 reaction product O-acetyl-ADP-ribose is degraded by ARH3.	O-Acetyl-ADP-Ribose	63-82	sirtuin 2	Homo sapiens	41-45
16648462-0	2006	SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis.	Lysine	62-65	sirtuin 2	Homo sapiens	0-5
16648462-1	2006	The mammalian cytoplasmic protein SirT2 is a member of the Sir2 family of NAD+-dependent protein deacetylases involved in caloric restriction-dependent life span extension.	NAD	74-77	sirtuin 2	Homo sapiens	34-39
16648462-2	2006	We found that SirT2 and its yeast counterpart Hst2 have a strong preference for histone H4K16Ac in their deacetylation activity in vitro and in vivo.	histone h4k16ac	80-95	sirtuin 2	Homo sapiens	14-19
16618762-2	2006	Hereby, we describe the identification of a compound we named cambinol that inhibits NAD-dependent deacetylase activity of human SIRT1 and SIRT2.	cambinol	62-70	sirtuin 2	Homo sapiens	139-144
16618762-2	2006	Hereby, we describe the identification of a compound we named cambinol that inhibits NAD-dependent deacetylase activity of human SIRT1 and SIRT2.	NAD	85-88	sirtuin 2	Homo sapiens	139-144
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	NAD	122-128	sirtuin 2	Homo sapiens	0-4
16484774-1	2006	Sirtuin 5 (SIRT5) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase and belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs), which play a central role in epigenetic gene silencing, DNA repair and recombination, cell-cycle, microtubule organization, and in the regulation of aging.	NAD	23-56	sirtuin 2	Homo sapiens	137-141
16484774-1	2006	Sirtuin 5 (SIRT5) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase and belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs), which play a central role in epigenetic gene silencing, DNA repair and recombination, cell-cycle, microtubule organization, and in the regulation of aging.	NAD	58-61	sirtuin 2	Homo sapiens	137-141
16211212-0	2005	FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2).	NAD	45-48	sirtuin 2	Homo sapiens	85-94
16211212-0	2005	FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2).	NAD	45-48	sirtuin 2	Homo sapiens	96-101
16211212-1	2005	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD(+))-dependent deacetylase, which belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs).	NAD	23-56	sirtuin 2	Homo sapiens	0-9
16211212-1	2005	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD(+))-dependent deacetylase, which belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs).	NAD	23-56	sirtuin 2	Homo sapiens	11-16
16211212-1	2005	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD(+))-dependent deacetylase, which belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs).	NAD	23-56	sirtuin 2	Homo sapiens	110-140
16211212-1	2005	Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD(+))-dependent deacetylase, which belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs).	NAD	23-56	sirtuin 2	Homo sapiens	142-146
15749705-1	2005	The NAD+-dependent protein deacetylase family, Sir2 (or sirtuins), is important for many cellular processes including gene silencing, regulation of p53, fatty acid metabolism, cell cycle regulation, and life span extension.	Fatty Acids	153-163	sirtuin 2	Homo sapiens	47-51
15749705-2	2005	Resveratrol, a polyphenol found in wines and thought to harbor major health benefits, was reported to be an activator of Sir2 enzymes in vivo and in vitro.	Resveratrol	0-11	sirtuin 2	Homo sapiens	121-125
15749705-2	2005	Resveratrol, a polyphenol found in wines and thought to harbor major health benefits, was reported to be an activator of Sir2 enzymes in vivo and in vitro.	Polyphenols	15-25	sirtuin 2	Homo sapiens	121-125
15749705-3	2005	In addition, resveratrol was shown to increase life span in three model organisms through a Sir2-dependent pathway.	Resveratrol	13-24	sirtuin 2	Homo sapiens	92-96
15749705-4	2005	Here, we investigated the molecular basis for Sir2 activation by resveratrol.	Resveratrol	65-76	sirtuin 2	Homo sapiens	46-50
15566299-1	2004	Type 2 human sirtuin (SIRT2) is a NAD(+)-dependent cytoplasmic protein that is colocalized with HDAC6 on microtubules.	NAD	34-40	sirtuin 2	Homo sapiens	22-27
15566299-8	2004	On the basis of our results, a phenol moiety on the active compound is suggested to be important for SIRT2 inhibitory activity.	Phenol	31-37	sirtuin 2	Homo sapiens	101-106
15566299-9	2004	This phenol group, together with a hydrophobic moiety and hydrogen-bonding features, is suggested to form an active SIRT2 pharmacophore.	Phenol	5-11	sirtuin 2	Homo sapiens	116-121
15566299-9	2004	This phenol group, together with a hydrophobic moiety and hydrogen-bonding features, is suggested to form an active SIRT2 pharmacophore.	Hydrogen	58-66	sirtuin 2	Homo sapiens	116-121
15486319-5	2004	NAM induced a significant increase in nuclear fragmentation (2.2-fold) and cleaved caspase-3, as did sirtinol, a specific Sir2 inhibitor, and expression of dominant-negative Sir2alpha.	sirtinol	101-109	sirtuin 2	Homo sapiens	122-126
16302818-2	2005	Two analogues, namely, 3- and 4-[(2-hydroxy-1-naphthalenylmethylene)amino]-N-(1-phenylethyl)benzamide (i.e., m- and p-sirtinol), were 2- to 10-fold more potent than sirtinol against human SIRT1 and SIRT2 enzymes.	3- and 4-[(2-hydroxy-1-naphthalenylmethylene)amino]-n-(1-phenylethyl)benzamide	23-101	sirtuin 2	Homo sapiens	198-203
16076959-2	2005	We previously reported that Foxo1, a member of the FOXO family, is regulated through reversible acetylation catalyzed by histone acetyltransferase cAMP-response element-binding protein (CREB)-binding protein (CBP) and NAD-dependent histone deacetylase silent information regulator 2, and that the acetylation at Lys-242, Lys-245, and Lys-262 of Foxo1 attenuates its transcriptional activity.	Cyclic AMP	147-151	sirtuin 2	Homo sapiens	252-282
16076959-2	2005	We previously reported that Foxo1, a member of the FOXO family, is regulated through reversible acetylation catalyzed by histone acetyltransferase cAMP-response element-binding protein (CREB)-binding protein (CBP) and NAD-dependent histone deacetylase silent information regulator 2, and that the acetylation at Lys-242, Lys-245, and Lys-262 of Foxo1 attenuates its transcriptional activity.	NAD	218-221	sirtuin 2	Homo sapiens	252-282
16076959-2	2005	We previously reported that Foxo1, a member of the FOXO family, is regulated through reversible acetylation catalyzed by histone acetyltransferase cAMP-response element-binding protein (CREB)-binding protein (CBP) and NAD-dependent histone deacetylase silent information regulator 2, and that the acetylation at Lys-242, Lys-245, and Lys-262 of Foxo1 attenuates its transcriptional activity.	Lysine	312-315	sirtuin 2	Homo sapiens	252-282
16076959-2	2005	We previously reported that Foxo1, a member of the FOXO family, is regulated through reversible acetylation catalyzed by histone acetyltransferase cAMP-response element-binding protein (CREB)-binding protein (CBP) and NAD-dependent histone deacetylase silent information regulator 2, and that the acetylation at Lys-242, Lys-245, and Lys-262 of Foxo1 attenuates its transcriptional activity.	Lysine	321-324	sirtuin 2	Homo sapiens	252-282
16076959-2	2005	We previously reported that Foxo1, a member of the FOXO family, is regulated through reversible acetylation catalyzed by histone acetyltransferase cAMP-response element-binding protein (CREB)-binding protein (CBP) and NAD-dependent histone deacetylase silent information regulator 2, and that the acetylation at Lys-242, Lys-245, and Lys-262 of Foxo1 attenuates its transcriptional activity.	Lysine	321-324	sirtuin 2	Homo sapiens	252-282
16006743-1	2005	Sir2 (silent information regulator 2) is an NAD-dependent deacetylase that is broadly conserved from bacteria to humans.	NAD	44-47	sirtuin 2	Homo sapiens	0-4
16006743-1	2005	Sir2 (silent information regulator 2) is an NAD-dependent deacetylase that is broadly conserved from bacteria to humans.	NAD	44-47	sirtuin 2	Homo sapiens	6-36
15860278-3	2005	Here, we have shown that Sirtinol, a commercially available inhibitor of SIR2 deacetylases, significantly inhibits the in vitro proliferation of Leishmania infantum axenic amastigotes in a dose-dependent manner.	sirtinol	25-33	sirtuin 2	Homo sapiens	73-77
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	NAD	122-128	sirtuin 2	Homo sapiens	6-36
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	Niacinamide	142-154	sirtuin 2	Homo sapiens	0-4
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	Niacinamide	142-154	sirtuin 2	Homo sapiens	6-36
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	O-Acetyl-ADP-Ribose	190-209	sirtuin 2	Homo sapiens	0-4
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	O-Acetyl-ADP-Ribose	190-209	sirtuin 2	Homo sapiens	6-36
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	O-Acetyl-ADP-Ribose	211-217	sirtuin 2	Homo sapiens	0-4
15269219-1	2004	Sir2 (silent information regulator 2) enzymes catalyze a unique protein deacetylation reaction that requires the coenzyme NAD(+) and produces nicotinamide and a newly discovered metabolite, O-acetyl-ADP-ribose (OAADPr).	O-Acetyl-ADP-Ribose	211-217	sirtuin 2	Homo sapiens	6-36
15269219-3	2004	Here we examine the role of NAD(+) metabolites/derivatives and salvage pathway intermediates as activators, inhibitors, or coenzyme substrates of Sir2 enzymes in vitro.	NAD	28-34	sirtuin 2	Homo sapiens	146-150
15269219-5	2004	Sir2 enzymes showed an exquisite selectivity for the nicotinamide base coenzyme, with the most dramatic losses in binding affinity/reactivity resulting from relatively minor changes in the nicotinamide ring, either by reduction, as in NADH, or by converting the amide to its acid analogue.	Niacinamide	53-65	sirtuin 2	Homo sapiens	0-4
15269219-5	2004	Sir2 enzymes showed an exquisite selectivity for the nicotinamide base coenzyme, with the most dramatic losses in binding affinity/reactivity resulting from relatively minor changes in the nicotinamide ring, either by reduction, as in NADH, or by converting the amide to its acid analogue.	Niacinamide	189-201	sirtuin 2	Homo sapiens	0-4
15269219-5	2004	Sir2 enzymes showed an exquisite selectivity for the nicotinamide base coenzyme, with the most dramatic losses in binding affinity/reactivity resulting from relatively minor changes in the nicotinamide ring, either by reduction, as in NADH, or by converting the amide to its acid analogue.	NAD	235-239	sirtuin 2	Homo sapiens	0-4
15269219-5	2004	Sir2 enzymes showed an exquisite selectivity for the nicotinamide base coenzyme, with the most dramatic losses in binding affinity/reactivity resulting from relatively minor changes in the nicotinamide ring, either by reduction, as in NADH, or by converting the amide to its acid analogue.	Amides	60-65	sirtuin 2	Homo sapiens	0-4
15269219-11	2004	We propose that changes in both free nicotinamide and free NAD(+) afford the greatest contribution to cellular activity of Sir2 enzymes but with nicotinamide having a more dramatic effect during smaller fluctuations in concentration.	Niacinamide	37-49	sirtuin 2	Homo sapiens	123-127
15269219-11	2004	We propose that changes in both free nicotinamide and free NAD(+) afford the greatest contribution to cellular activity of Sir2 enzymes but with nicotinamide having a more dramatic effect during smaller fluctuations in concentration.	NAD	59-65	sirtuin 2	Homo sapiens	123-127
14522996-0	2003	Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases.	Niacinamide	13-25	sirtuin 2	Homo sapiens	63-67
15301953-5	2004	Using this method, the kinetics of the reaction of the cosubstrate nicotinamide adenine dinucleotide and the competitive inhibitor nicotinamide with SIRT1 and SIRT2 has been analyzed.	NAD	67-100	sirtuin 2	Homo sapiens	159-164
15301953-5	2004	Using this method, the kinetics of the reaction of the cosubstrate nicotinamide adenine dinucleotide and the competitive inhibitor nicotinamide with SIRT1 and SIRT2 has been analyzed.	Niacinamide	67-79	sirtuin 2	Homo sapiens	159-164
15053627-5	2004	Hydrosilanes R2SiH2 (R2 = Ph2, PhMe, Me2, Dipp(H); Dipp = 2,6-diisopropylphenyl) were shown to react with 4 in double Si-H bond activation reactions to give the silylene complexes [Cp*(dmpe)H2W = SiR2][B(C6F5)4] (8a-d).	hydrosilanes	0-12	sirtuin 2	Homo sapiens	196-200
15053627-5	2004	Hydrosilanes R2SiH2 (R2 = Ph2, PhMe, Me2, Dipp(H); Dipp = 2,6-diisopropylphenyl) were shown to react with 4 in double Si-H bond activation reactions to give the silylene complexes [Cp*(dmpe)H2W = SiR2][B(C6F5)4] (8a-d).	r2sih2	13-19	sirtuin 2	Homo sapiens	196-200
15053627-5	2004	Hydrosilanes R2SiH2 (R2 = Ph2, PhMe, Me2, Dipp(H); Dipp = 2,6-diisopropylphenyl) were shown to react with 4 in double Si-H bond activation reactions to give the silylene complexes [Cp*(dmpe)H2W = SiR2][B(C6F5)4] (8a-d).	ph2	26-29	sirtuin 2	Homo sapiens	196-200
15053627-5	2004	Hydrosilanes R2SiH2 (R2 = Ph2, PhMe, Me2, Dipp(H); Dipp = 2,6-diisopropylphenyl) were shown to react with 4 in double Si-H bond activation reactions to give the silylene complexes [Cp*(dmpe)H2W = SiR2][B(C6F5)4] (8a-d).	Silicon	15-17	sirtuin 2	Homo sapiens	196-200
15128440-1	2004	Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases dependent on nicotine adenine dinucleotide (NAD) and are found in organisms ranging from bacteria to humans.	nicotine adenine dinucleotide	99-128	sirtuin 2	Homo sapiens	0-30
15128440-1	2004	Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases dependent on nicotine adenine dinucleotide (NAD) and are found in organisms ranging from bacteria to humans.	nicotine adenine dinucleotide	99-128	sirtuin 2	Homo sapiens	32-36
15128440-1	2004	Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases dependent on nicotine adenine dinucleotide (NAD) and are found in organisms ranging from bacteria to humans.	nadide	130-133	sirtuin 2	Homo sapiens	0-30
15128440-1	2004	Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases dependent on nicotine adenine dinucleotide (NAD) and are found in organisms ranging from bacteria to humans.	nadide	130-133	sirtuin 2	Homo sapiens	32-36
15128440-4	2004	The Sir2 catalytic domain, which is shared among all sirtuins, consists of two distinct domains that bind NAD and the acetyl-lysine substrate, respectively.	nadide	106-109	sirtuin 2	Homo sapiens	4-8
15128440-4	2004	The Sir2 catalytic domain, which is shared among all sirtuins, consists of two distinct domains that bind NAD and the acetyl-lysine substrate, respectively.	N(alpha)-acetyllysine	118-131	sirtuin 2	Homo sapiens	4-8
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	NAD	72-78	sirtuin 2	Homo sapiens	4-34
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	NAD	72-78	sirtuin 2	Homo sapiens	36-40
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	NAD	156-162	sirtuin 2	Homo sapiens	4-34
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	NAD	156-162	sirtuin 2	Homo sapiens	36-40
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	Niacinamide	220-232	sirtuin 2	Homo sapiens	4-34
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	Niacinamide	220-232	sirtuin 2	Homo sapiens	36-40
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	O-Acetyl-ADP-Ribose	285-304	sirtuin 2	Homo sapiens	4-34
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	O-Acetyl-ADP-Ribose	285-304	sirtuin 2	Homo sapiens	36-40
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	O-Acetyl-ADP-Ribose	306-312	sirtuin 2	Homo sapiens	4-34
15274642-1	2004	The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the deacetylated product, and the novel metabolite O-acetyl-ADP-ribose (OAADPR).	O-Acetyl-ADP-Ribose	306-312	sirtuin 2	Homo sapiens	36-40
15274642-4	2004	Bisubstrate kinetic analysis indicates that Sir2 enzymes follow a sequential mechanism, where both the acetylated substrate and NAD(+) must bind to form a ternary complex, prior to any catalytic step.	NAD	128-134	sirtuin 2	Homo sapiens	44-48
15220471-6	2004	Conversely, Sir2 binds and deacetylates Foxo1 at residues acetylated by cAMP-response element-binding protein-binding protein.	Cyclic AMP	72-76	sirtuin 2	Homo sapiens	12-16
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	NAD	55-59	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	NAD	55-59	sirtuin 2	Homo sapiens	32-36
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Lysine	133-139	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Lysine	133-139	sirtuin 2	Homo sapiens	32-36
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Adenosine Diphosphate	182-185	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Adenosine Diphosphate	182-185	sirtuin 2	Homo sapiens	32-36
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Ribose	186-192	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Ribose	186-192	sirtuin 2	Homo sapiens	32-36
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	NAD	203-207	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	NAD	203-207	sirtuin 2	Homo sapiens	32-36
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Niacinamide	219-231	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	Niacinamide	219-231	sirtuin 2	Homo sapiens	32-36
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	O-Acetyl-ADP-Ribose	257-276	sirtuin 2	Homo sapiens	0-30
14522996-1	2003	Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose.	O-Acetyl-ADP-Ribose	257-276	sirtuin 2	Homo sapiens	32-36
14522996-3	2003	Recently, nicotinamide has been implicated as a direct negative regulator of cellular Sir2 function; however, the mechanism of nicotinamide inhibition was not established.	Niacinamide	10-22	sirtuin 2	Homo sapiens	86-90
14522996-4	2003	Sir2 enzymes are multifunctional in that the deacetylase reaction involves the cleavage of the nicotinamide-ribosyl, cleavage of an amide bond, and transfer of the acetyl group ultimately to the 2"-ribose hydroxyl of ADP-ribose.	Niacinamide	95-107	sirtuin 2	Homo sapiens	0-4
14522996-4	2003	Sir2 enzymes are multifunctional in that the deacetylase reaction involves the cleavage of the nicotinamide-ribosyl, cleavage of an amide bond, and transfer of the acetyl group ultimately to the 2"-ribose hydroxyl of ADP-ribose.	Amides	102-107	sirtuin 2	Homo sapiens	0-4
14522996-4	2003	Sir2 enzymes are multifunctional in that the deacetylase reaction involves the cleavage of the nicotinamide-ribosyl, cleavage of an amide bond, and transfer of the acetyl group ultimately to the 2"-ribose hydroxyl of ADP-ribose.	2"-ribose hydroxyl	195-213	sirtuin 2	Homo sapiens	0-4
14522996-4	2003	Sir2 enzymes are multifunctional in that the deacetylase reaction involves the cleavage of the nicotinamide-ribosyl, cleavage of an amide bond, and transfer of the acetyl group ultimately to the 2"-ribose hydroxyl of ADP-ribose.	Adenosine Diphosphate Ribose	217-227	sirtuin 2	Homo sapiens	0-4
12697818-0	2003	Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle.	NAD	21-24	sirtuin 2	Homo sapiens	15-20
12919668-1	2003	A new report reveals a role for the mammalian NAD-dependent deacetylase Sir2 in repressing the muscle cell differentiation program and implicates the cellular redox state as a critical determinant of transcriptional activity of differentiation-specific genes.	NAD	46-49	sirtuin 2	Homo sapiens	72-76
12697818-3	2003	The SIRT2 protein is a NAD-dependent deacetylase (NDAC), the abundance of which increases dramatically during mitosis and is multiply phosphorylated at the G(2)/M transition of the cell cycle.	NAD	23-26	sirtuin 2	Homo sapiens	4-9
12648681-3	2003	It has been shown that NAD affects longevity and transcriptional silencing through the regulation of the Sir2p family, which are NAD-dependent deacetylases.	NAD	23-26	sirtuin 2	Homo sapiens	105-110
12648681-4	2003	Many human diseases are associated with changes in NAD level and/or the NAD : NADH ratio, raising the possibility that the Sir2p family might play a role in these diseases.	NAD	51-54	sirtuin 2	Homo sapiens	123-128
12648681-4	2003	Many human diseases are associated with changes in NAD level and/or the NAD : NADH ratio, raising the possibility that the Sir2p family might play a role in these diseases.	NAD	72-75	sirtuin 2	Homo sapiens	123-128
12648681-4	2003	Many human diseases are associated with changes in NAD level and/or the NAD : NADH ratio, raising the possibility that the Sir2p family might play a role in these diseases.	NAD	78-82	sirtuin 2	Homo sapiens	123-128
12220851-1	2002	Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family are nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylases.	NAD	97-130	sirtuin 2	Homo sapiens	40-70
12574164-2	2003	In addition, NAD also serves as a substrate for ADP-ribosylation of a number of nuclear proteins, for silent information regulator 2 (Sir2)-like histone deacetylase that is involved in gene silencing regulation, and for cyclic ADP ribose (cADPR)-dependent Ca(2+) signaling.	nadide	13-16	sirtuin 2	Homo sapiens	102-132
12574164-2	2003	In addition, NAD also serves as a substrate for ADP-ribosylation of a number of nuclear proteins, for silent information regulator 2 (Sir2)-like histone deacetylase that is involved in gene silencing regulation, and for cyclic ADP ribose (cADPR)-dependent Ca(2+) signaling.	nadide	13-16	sirtuin 2	Homo sapiens	134-138
12620231-0	2003	The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase.	NAD	38-41	sirtuin 2	Homo sapiens	10-14
12620231-0	2003	The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase.	NAD	38-41	sirtuin 2	Homo sapiens	25-30
12620231-3	2003	SIRT2 deacetylates lysine-40 of alpha-tubulin both in vitro and in vivo.	Lysine	19-25	sirtuin 2	Homo sapiens	0-5
12220851-1	2002	Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family are nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylases.	NAD	97-130	sirtuin 2	Homo sapiens	72-76
12220851-1	2002	Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family are nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylases.	NAD	132-139	sirtuin 2	Homo sapiens	40-70
12220851-1	2002	Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family are nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylases.	NAD	132-139	sirtuin 2	Homo sapiens	72-76
12186850-1	2002	The yeast silent information regulator (Sir)2 protein links cellular metabolism and transcriptional silencing through its nicotinamide adenine dinucleotide (NAD)-dependent histone deacetylase activity.	NAD	122-155	sirtuin 2	Homo sapiens	40-45
12186850-1	2002	The yeast silent information regulator (Sir)2 protein links cellular metabolism and transcriptional silencing through its nicotinamide adenine dinucleotide (NAD)-dependent histone deacetylase activity.	NAD	157-160	sirtuin 2	Homo sapiens	40-45
11935028-1	2002	The conserved Sir2 family of proteins has protein deacetylase activity that is dependent on NAD (the oxidized form of nicotinamide adenine dinucleotide).	NAD	92-95	sirtuin 2	Homo sapiens	14-18
11935028-1	2002	The conserved Sir2 family of proteins has protein deacetylase activity that is dependent on NAD (the oxidized form of nicotinamide adenine dinucleotide).	NAD	118-151	sirtuin 2	Homo sapiens	14-18
11427894-2	2001	The 1.7 A crystal structure of the 323 amino acid catalytic core of human SIRT2, a homolog of yeast Sir2, reveals an NAD-binding domain, which is a variant of the Rossmann fold, and a smaller domain composed of a helical module and a zinc-binding module.	NAD	117-120	sirtuin 2	Homo sapiens	74-79
11106374-0	2000	Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose.	NAD	41-44	sirtuin 2	Homo sapiens	0-30
11106374-0	2000	Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose.	1-O-acetyl-ADP-ribose	113-134	sirtuin 2	Homo sapiens	0-30
11106374-1	2000	Conflicting reports have suggested that the silent information regulator 2 (SIR2) protein family employs NAD(+) to ADP-ribosylate histones [Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H. &amp; Moazed, D. (1999) Cell 99, 735-745; Frye, R. A.	NAD	105-111	sirtuin 2	Homo sapiens	44-74
11106374-1	2000	Conflicting reports have suggested that the silent information regulator 2 (SIR2) protein family employs NAD(+) to ADP-ribosylate histones [Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H. &amp; Moazed, D. (1999) Cell 99, 735-745; Frye, R. A.	NAD	105-111	sirtuin 2	Homo sapiens	76-80
10381378-0	1999	Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity.	NAD	116-119	sirtuin 2	Homo sapiens	64-68
10381378-0	1999	Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity.	NAD	116-119	sirtuin 2	Homo sapiens	75-79
10381378-8	1999	Recombinant E. coli cobB and human SIRT2 sirtuin proteins were able to cause radioactivity to be transferred from [32P]NAD to bovine serum albumin (BSA).	Phosphorus-32	115-118	sirtuin 2	Homo sapiens	35-40
10381378-8	1999	Recombinant E. coli cobB and human SIRT2 sirtuin proteins were able to cause radioactivity to be transferred from [32P]NAD to bovine serum albumin (BSA).	NAD	119-122	sirtuin 2	Homo sapiens	35-40
10381378-9	1999	When a conserved histidine within the human SIRT2 sirtuin was converted to a tyrosine, the mutant recombinant protein was unable to transfer radioactivity from [32P]NAD to BSA.	Histidine	17-26	sirtuin 2	Homo sapiens	44-49
10381378-9	1999	When a conserved histidine within the human SIRT2 sirtuin was converted to a tyrosine, the mutant recombinant protein was unable to transfer radioactivity from [32P]NAD to BSA.	Tyrosine	77-85	sirtuin 2	Homo sapiens	44-49
11893743-0	2002	Structural identification of 2"- and 3"-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases.	2"- and 3"-o-acetyl-adp-ribose	29-59	sirtuin 2	Homo sapiens	98-102
11893743-3	2002	Sir2 enzymes have been shown to couple substrate deacetylation and beta-NAD(+) cleavage to the formation of O-acetyl-ADP-ribose, a newly described metabolite.	NAD	67-78	sirtuin 2	Homo sapiens	0-4
11893743-3	2002	Sir2 enzymes have been shown to couple substrate deacetylation and beta-NAD(+) cleavage to the formation of O-acetyl-ADP-ribose, a newly described metabolite.	O-Acetyl-ADP-Ribose	108-127	sirtuin 2	Homo sapiens	0-4
11893743-5	2002	Through the use of mass spectrometry, rapid quenching techniques, and NMR structural analyses, 2"-O-acetyl-ADP-ribose and 3"-O-acetyl-ADP-ribose were found to be the solution products produced by the Sir2 family of enzymes.	2-O-acetyl-ADP-ribose	95-117	sirtuin 2	Homo sapiens	200-204
11893743-5	2002	Through the use of mass spectrometry, rapid quenching techniques, and NMR structural analyses, 2"-O-acetyl-ADP-ribose and 3"-O-acetyl-ADP-ribose were found to be the solution products produced by the Sir2 family of enzymes.	3-O-acetyl-ADP-ribose	122-144	sirtuin 2	Homo sapiens	200-204
11095969-0	2000	Role of NAD(+) in the deacetylase activity of the SIR2-like proteins.	NAD	8-14	sirtuin 2	Homo sapiens	50-54
11095969-1	2000	In this report we describe the role of NAD(+) in the deacetylation reaction catalyzed by the SIR2 family of enzymes.	NAD	39-45	sirtuin 2	Homo sapiens	93-97