{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T10:11:17Z","timestamp":1790763077686,"version":"4.1.0"},"reference-count":71,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,12,14]],"date-time":"2018-12-14T00:00:00Z","timestamp":1544745600000},"content-version":"am","delay-in-days":347,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2018,1]]},"DOI":"10.1016\/j.abb.2017.12.009","type":"journal-article","created":{"date-parts":[[2017,12,9]],"date-time":"2017-12-09T17:08:41Z","timestamp":1512839321000},"page":"8-17","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":57,"special_numbering":"C","title":["Trichostatin A inhibits deacetylation of histone H3 and p53 by SIRT6"],"prefix":"10.1016","volume":"638","author":[{"given":"Marci","family":"Wood","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stacia","family":"Rymarchyk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Song","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6436-5744","authenticated-orcid":false,"given":"Yana","family":"Cen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.abb.2017.12.009_bib1","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.biochem.74.082803.133500","article-title":"The biochemistry of sirtuins","volume":"75","author":"Sauve","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.abb.2017.12.009_bib2","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1146\/annurev.pathol.4.110807.092250","article-title":"Mammalian sirtuins: biological insights and disease relevance","volume":"5","author":"Haigis","year":"2010","journal-title":"Annu. Rev. Pathol."},{"key":"10.1016\/j.abb.2017.12.009_bib3","doi-asserted-by":"crossref","first-page":"9787","DOI":"10.1038\/srep09787","article-title":"Sirt7 promotes gastric cancer growth and inhibits apoptosis by epigenetically inhibiting miR-34a","volume":"5","author":"Zhang","year":"2015","journal-title":"Sci. Rep."},{"issue":"6","key":"10.1016\/j.abb.2017.12.009_bib4","doi-asserted-by":"crossref","first-page":"9267","DOI":"10.18632\/oncotarget.14035","article-title":"Reducing Smad3\/ATF4 was essential for Sirt1 inhibiting ER stress-induced apoptosis in mice brown adipose tissue","volume":"8","author":"Liu","year":"2017","journal-title":"Oncotarget"},{"issue":"47","key":"10.1016\/j.abb.2017.12.009_bib5","doi-asserted-by":"crossref","first-page":"36776","DOI":"10.1074\/jbc.M110.168039","article-title":"SIRT6 deficiency results in severe hypoglycemia by enhancing both basal and insulin-stimulated glucose uptake in mice","volume":"285","author":"Xiao","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"44","key":"10.1016\/j.abb.2017.12.009_bib6","doi-asserted-by":"crossref","first-page":"23318","DOI":"10.1074\/jbc.M116.737114","article-title":"Histone deacetylase SIRT1 controls proliferation, circadian rhythm, and lipid metabolism during liver regeneration in mice","volume":"291","author":"Bellet","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2017.12.009_bib7","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.mad.2016.02.003","article-title":"Regulation of SIRT1 in aging: roles in mitochondrial function and biogenesis","volume":"155","author":"Yuan","year":"2016","journal-title":"Mech. Ageing Dev."},{"issue":"3","key":"10.1016\/j.abb.2017.12.009_bib8","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1093\/humrep\/dev345","article-title":"Role of Sirt3 in mitochondrial biogenesis and developmental competence of human in vitro matured oocytes","volume":"31","author":"Zhao","year":"2016","journal-title":"Hum. Reprod."},{"issue":"7","key":"10.1016\/j.abb.2017.12.009_bib9","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1016\/j.celrep.2015.10.006","article-title":"Lamin a is an endogenous SIRT6 activator and promotes SIRT6-mediated DNA repair","volume":"13","author":"Ghosh","year":"2015","journal-title":"Cell Rep."},{"issue":"16","key":"10.1016\/j.abb.2017.12.009_bib10","doi-asserted-by":"crossref","first-page":"2299","DOI":"10.2174\/1381612823666170125153334","article-title":"A review on SIRtuins in diabetes","volume":"23","author":"Aditya","year":"2017","journal-title":"Curr. Pharmaceut. Des."},{"issue":"11","key":"10.1016\/j.abb.2017.12.009_bib11","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1038\/jcbfm.2015.123","article-title":"Sirtuin 3 mediates neuroprotection of ketones against ischemic stroke","volume":"35","author":"Yin","year":"2015","journal-title":"J. Cerebr. Blood Flow Metabol. Off. J. Int. Soc. Cereb. Blood Flow Metabol."},{"key":"10.1016\/j.abb.2017.12.009_bib12","doi-asserted-by":"crossref","first-page":"48","DOI":"10.3389\/fnagi.2013.00048","article-title":"Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration","volume":"5","author":"Kincaid","year":"2013","journal-title":"Front. Aging Neurosci."},{"issue":"3","key":"10.1016\/j.abb.2017.12.009_bib13","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.mad.2010.01.006","article-title":"Functional dissection of SIRT6: identification of domains that regulate histone deacetylase activity and chromatin localization","volume":"131","author":"Tennen","year":"2010","journal-title":"Mech. Ageing Dev."},{"issue":"7186","key":"10.1016\/j.abb.2017.12.009_bib14","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1038\/nature06736","article-title":"SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin","volume":"452","author":"Michishita","year":"2008","journal-title":"Nature"},{"issue":"16","key":"10.1016\/j.abb.2017.12.009_bib15","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.4161\/cc.8.16.9367","article-title":"Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6","volume":"8","author":"Michishita","year":"2009","journal-title":"Cell Cycle"},{"issue":"5997","key":"10.1016\/j.abb.2017.12.009_bib16","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1126\/science.1192049","article-title":"Human SIRT6 promotes DNA end resection through CtIP deacetylation","volume":"329","author":"Kaidi","year":"2010","journal-title":"Science"},{"issue":"7388","key":"10.1016\/j.abb.2017.12.009_bib17","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1038\/nature10815","article-title":"The sirtuin SIRT6 regulates lifespan in male mice","volume":"483","author":"Kanfi","year":"2012","journal-title":"Nature"},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib18","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.cell.2005.11.044","article-title":"Genomic instability and aging-like phenotype in the absence of mammalian SIRT6","volume":"124","author":"Mostoslavsky","year":"2006","journal-title":"Cell"},{"issue":"17","key":"10.1016\/j.abb.2017.12.009_bib19","doi-asserted-by":"crossref","first-page":"2274","DOI":"10.1016\/j.febslet.2015.06.043","article-title":"Putative tumor suppression function of SIRT6 in endometrial cancer","volume":"589","author":"Fukuda","year":"2015","journal-title":"FEBS Lett."},{"issue":"6","key":"10.1016\/j.abb.2017.12.009_bib20","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1016\/j.cell.2012.10.047","article-title":"The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism","volume":"151","author":"Sebastian","year":"2012","journal-title":"Cell"},{"issue":"6036","key":"10.1016\/j.abb.2017.12.009_bib21","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1126\/science.1202723","article-title":"SIRT6 promotes DNA repair under stress by activating PARP1","volume":"332","author":"Mao","year":"2011","journal-title":"Science"},{"issue":"7443","key":"10.1016\/j.abb.2017.12.009_bib22","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/nature12038","article-title":"SIRT6 regulates TNF-alpha secretion through hydrolysis of long-chain fatty acyl lysine","volume":"496","author":"Jiang","year":"2013","journal-title":"Nature"},{"issue":"43","key":"10.1016\/j.abb.2017.12.009_bib23","doi-asserted-by":"crossref","first-page":"31350","DOI":"10.1074\/jbc.C113.511261","article-title":"Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins","volume":"288","author":"Feldman","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2017.12.009_bib24","article-title":"SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation","volume":"6","author":"Zhang","year":"2017","journal-title":"eLife"},{"issue":"5","key":"10.1016\/j.abb.2017.12.009_bib25","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.febslet.2008.01.019","article-title":"Regulation of SIRT6 protein levels by nutrient availability","volume":"582","author":"Kanfi","year":"2008","journal-title":"FEBS Lett."},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib26","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1038\/nm.1906","article-title":"Intracellular NAD levels regulate tumor necrosis factor protein synthesis in a sirtuin-dependent manner","volume":"15","author":"Van Gool","year":"2009","journal-title":"Nat. Med."},{"issue":"11","key":"10.1016\/j.abb.2017.12.009_bib27","doi-asserted-by":"crossref","first-page":"4796","DOI":"10.1021\/jm500487d","article-title":"Discovery of novel and selective SIRT6 inhibitors","volume":"57","author":"Parenti","year":"2014","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.abb.2017.12.009_bib28","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/j.ejmech.2015.08.024","article-title":"Quinazolinedione SIRT6 inhibitors sensitize cancer cells to chemotherapeutics","volume":"102","author":"Sociali","year":"2015","journal-title":"Eur. J. Med. Chem."},{"issue":"38","key":"10.1016\/j.abb.2017.12.009_bib29","doi-asserted-by":"crossref","first-page":"7498","DOI":"10.1039\/C4OB00860J","article-title":"Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors","volume":"12","author":"He","year":"2014","journal-title":"Org. Biomol. Chem."},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib30","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0092-8674(01)00527-X","article-title":"hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase","volume":"107","author":"Vaziri","year":"2001","journal-title":"Cell"},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib31","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0092-8674(01)00524-4","article-title":"Negative control of p53 by Sir2alpha promotes cell survival under stress","volume":"107","author":"Luo","year":"2001","journal-title":"Cell"},{"issue":"29","key":"10.1016\/j.abb.2017.12.009_bib32","doi-asserted-by":"crossref","first-page":"10684","DOI":"10.1073\/pnas.1411026111","article-title":"Tumor suppressor p53 cooperates with SIRT6 to regulate gluconeogenesis by promoting FoxO1 nuclear exclusion","volume":"111","author":"Zhang","year":"2014","journal-title":"Proc. Natl. Academy Sci. U. S. A."},{"issue":"13","key":"10.1016\/j.abb.2017.12.009_bib33","doi-asserted-by":"crossref","first-page":"3372","DOI":"10.1158\/1078-0432.CCR-15-1638","article-title":"SIRT6 overexpression potentiates apoptosis evasion in hepatocellular carcinoma via BCL2-associated X protein-dependent apoptotic pathway","volume":"22","author":"Ran","year":"2016","journal-title":"Clin. Canc. Res."},{"issue":"13","key":"10.1016\/j.abb.2017.12.009_bib34","doi-asserted-by":"crossref","first-page":"2878","DOI":"10.1021\/bi802093g","article-title":"Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD","volume":"48","author":"Du","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.abb.2017.12.009_bib35","first-page":"1","article-title":"Evaluation of enzyme inhibitors in drug discovery. A guide for medicinal chemists and pharmacologists","volume":"46","author":"Copeland","year":"2005","journal-title":"Meth. Biochem. Anal."},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib36","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/0005-2744(69)90420-3","article-title":"Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors","volume":"185","author":"Morrison","year":"1969","journal-title":"Biochim. Biophys. Acta"},{"issue":"16","key":"10.1016\/j.abb.2017.12.009_bib37","doi-asserted-by":"crossref","first-page":"14575","DOI":"10.1074\/jbc.M111.218990","article-title":"Structure and biochemical functions of SIRT6","volume":"286","author":"Pan","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"51","key":"10.1016\/j.abb.2017.12.009_bib38","doi-asserted-by":"crossref","first-page":"15456","DOI":"10.1021\/bi011858j","article-title":"Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions","volume":"40","author":"Sauve","year":"2001","journal-title":"Biochemistry"},{"issue":"15","key":"10.1016\/j.abb.2017.12.009_bib39","doi-asserted-by":"crossref","first-page":"12632","DOI":"10.1074\/jbc.M111830200","article-title":"Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases","volume":"277","author":"Borra","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"21","key":"10.1016\/j.abb.2017.12.009_bib40","doi-asserted-by":"crossref","first-page":"18535","DOI":"10.1074\/jbc.M200671200","article-title":"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","volume":"277","author":"Jackson","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.abb.2017.12.009_bib41","doi-asserted-by":"crossref","first-page":"30","DOI":"10.3390\/cancers7010030","article-title":"p53 acetylation: regulation and consequences","volume":"7","author":"Reed","year":"2014","journal-title":"Cancers"},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib42","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/j.bbrc.2007.06.084","article-title":"Alkylating agent methyl methanesulfonate (MMS) induces a wave of global protein hyperacetylation: implications in cancer cell death","volume":"360","author":"Lee","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"8","key":"10.1016\/j.abb.2017.12.009_bib43","doi-asserted-by":"crossref","first-page":"2259","DOI":"10.1073\/pnas.0308762101","article-title":"Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo","volume":"101","author":"Luo","year":"2004","journal-title":"Proc. Natl. Academy Sci. U. S. A."},{"issue":"52","key":"10.1016\/j.abb.2017.12.009_bib44","doi-asserted-by":"crossref","first-page":"50607","DOI":"10.1074\/jbc.C200578200","article-title":"Acetylation of p53 inhibits its ubiquitination by Mdm2","volume":"277","author":"Li","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"22","key":"10.1016\/j.abb.2017.12.009_bib45","doi-asserted-by":"crossref","first-page":"6236","DOI":"10.1093\/emboj\/cdf616","article-title":"MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation","volume":"21","author":"Ito","year":"2002","journal-title":"EMBO J."},{"issue":"4","key":"10.1016\/j.abb.2017.12.009_bib46","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1002\/ijc.27726","article-title":"Involvement of p53 in the cytotoxic activity of the NAMPT inhibitor FK866 in myeloid leukemic cells","volume":"132","author":"Thakur","year":"2013","journal-title":"Int. J. Canc."},{"issue":"31","key":"10.1016\/j.abb.2017.12.009_bib47","doi-asserted-by":"crossref","first-page":"9249","DOI":"10.1021\/bi034959l","article-title":"Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry","volume":"42","author":"Sauve","year":"2003","journal-title":"Biochemistry"},{"issue":"1","key":"10.1016\/j.abb.2017.12.009_bib48","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1006\/abio.2001.5490","article-title":"Concurrent quantification of quinolinic, picolinic, and nicotinic acids using electron-capture negative-ion gas chromatography-mass spectrometry","volume":"301","author":"Smythe","year":"2002","journal-title":"Anal. Biochem."},{"issue":"31","key":"10.1016\/j.abb.2017.12.009_bib49","doi-asserted-by":"crossref","first-page":"21745","DOI":"10.1074\/jbc.M602909200","article-title":"Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction","volume":"281","author":"Qin","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.abb.2017.12.009_bib50","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0107729","article-title":"Mechanism of inhibition of the human sirtuin enzyme SIRT3 by nicotinamide: computational and experimental studies","volume":"9","author":"Guan","year":"2014","journal-title":"PLoS One"},{"issue":"47","key":"10.1016\/j.abb.2017.12.009_bib51","doi-asserted-by":"crossref","first-page":"45099","DOI":"10.1074\/jbc.M205670200","article-title":"Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1","volume":"277","author":"Bitterman","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"51","key":"10.1016\/j.abb.2017.12.009_bib52","doi-asserted-by":"crossref","first-page":"50985","DOI":"10.1074\/jbc.M306552200","article-title":"Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone\/protein deacetylases","volume":"278","author":"Jackson","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.abb.2017.12.009_bib53","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0045098","article-title":"Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition","volume":"7","author":"Fischer","year":"2012","journal-title":"PLoS One"},{"issue":"38","key":"10.1016\/j.abb.2017.12.009_bib54","doi-asserted-by":"crossref","first-page":"10227","DOI":"10.1021\/bi800767t","article-title":"Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase","volume":"47","author":"French","year":"2008","journal-title":"Biochemistry"},{"issue":"42","key":"10.1016\/j.abb.2017.12.009_bib55","doi-asserted-by":"crossref","first-page":"38837","DOI":"10.1074\/jbc.M106779200","article-title":"Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening","volume":"276","author":"Grozinger","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"5837","key":"10.1016\/j.abb.2017.12.009_bib56","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1126\/science.1143780","article-title":"Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease","volume":"317","author":"Outeiro","year":"2007","journal-title":"Science"},{"issue":"42","key":"10.1016\/j.abb.2017.12.009_bib57","doi-asserted-by":"crossref","first-page":"15064","DOI":"10.1073\/pnas.0404603101","article-title":"Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor","volume":"101","author":"Vannini","year":"2004","journal-title":"Proc. Natl. Academy Sci. U. S. A."},{"issue":"1","key":"10.1016\/j.abb.2017.12.009_bib58","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1073\/pnas.98.1.87","article-title":"Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin","volume":"98","author":"Furumai","year":"2001","journal-title":"Proc. Natl. Academy Sci. U. S. A."},{"issue":"28","key":"10.1016\/j.abb.2017.12.009_bib59","doi-asserted-by":"crossref","first-page":"17174","DOI":"10.1016\/S0021-9258(17)44885-X","article-title":"Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A","volume":"265","author":"Yoshida","year":"1990","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.abb.2017.12.009_bib60","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1039\/b817886k","article-title":"Discovery, biological activity, synthesis and potential therapeutic utility of naturally occurring histone deacetylase inhibitors","volume":"26","author":"Newkirk","year":"2009","journal-title":"Nat. Prod. Rep."},{"issue":"8","key":"10.1016\/j.abb.2017.12.009_bib61","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1016\/j.bbapap.2009.09.009","article-title":"Structural basis for sirtuin function: what we know and what we don't","volume":"1804","author":"Sanders","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"issue":"3","key":"10.1016\/j.abb.2017.12.009_bib62","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.tem.2016.10.002","article-title":"SIRT6: novel mechanisms and links to aging and disease","volume":"28","author":"Tasselli","year":"2017","journal-title":"Trends Endocrinol. Metabol."},{"issue":"10","key":"10.1016\/j.abb.2017.12.009_bib63","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1038\/nrm2502","article-title":"Is there a code embedded in proteins that is based on post-translational modifications?","volume":"9","author":"Sims","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"6810","key":"10.1016\/j.abb.2017.12.009_bib64","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1038\/35042612","article-title":"Deacetylation of p53 modulates its effect on cell growth and apoptosis","volume":"408","author":"Luo","year":"2000","journal-title":"Nature"},{"issue":"9","key":"10.1016\/j.abb.2017.12.009_bib65","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1007\/s00018-003-3090-z","article-title":"Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases","volume":"60","author":"Kyrylenko","year":"2003","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"10.1016\/j.abb.2017.12.009_bib66","first-page":"OL1737","article-title":"Transcription levels of sirtuin family in neural stem cells and brain tissues of adult mice","volume":"Suppl.58","author":"Wang","year":"2012","journal-title":"Cell. Mol. Biol."},{"issue":"13","key":"10.1016\/j.abb.2017.12.009_bib67","doi-asserted-by":"crossref","first-page":"11252","DOI":"10.18632\/oncotarget.3594","article-title":"E2F1 enhances glycolysis through suppressing Sirt6 transcription in cancer cells","volume":"6","author":"Wu","year":"2015","journal-title":"Oncotarget"},{"issue":"2","key":"10.1016\/j.abb.2017.12.009_bib68","doi-asserted-by":"crossref","first-page":"159","DOI":"10.4155\/fmc.14.152","article-title":"Photoaffinity labeling in target- and binding-site identification","volume":"7","author":"Smith","year":"2015","journal-title":"Future Med. Chem."},{"issue":"Pt 1","key":"10.1016\/j.abb.2017.12.009_bib69","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1042\/bj3500199","article-title":"Cloning and characterization of a novel human histone deacetylase, HDAC8","volume":"350","author":"Buggy","year":"2000","journal-title":"Biochem. J."},{"issue":"8","key":"10.1016\/j.abb.2017.12.009_bib70","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0071323","article-title":"A selective HDAC 1\/2 inhibitor modulates chromatin and gene expression in brain and alters mouse behavior in two mood-related tests","volume":"8","author":"Schroeder","year":"2013","journal-title":"PLoS One"},{"issue":"25","key":"10.1016\/j.abb.2017.12.009_bib71","doi-asserted-by":"crossref","first-page":"22211","DOI":"10.1074\/jbc.M110.180224","article-title":"Inhibitors of histone deacetylases: correlation between isoform specificity and reactivation of HIV type 1 (HIV-1) from latently infected cells","volume":"286","author":"Huber","year":"2011","journal-title":"J. Biol. Chem."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986117304423?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986117304423?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T13:00:59Z","timestamp":1762088459000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986117304423"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,1]]},"references-count":71,"alternative-id":["S0003986117304423"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2017.12.009","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2018,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Trichostatin A inhibits deacetylation of histone H3 and p53 by SIRT6","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2017.12.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}