{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T16:23:59Z","timestamp":1785774239410,"version":"3.56.0"},"reference-count":105,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01NS079183"],"award-info":[{"award-number":["R01NS079183"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R41AG058283"],"award-info":[{"award-number":["R41AG058283"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R43HD093464"],"award-info":[{"award-number":["R43HD093464"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2021,1]]},"DOI":"10.1016\/j.ejmech.2020.112887","type":"journal-article","created":{"date-parts":[[2020,9,29]],"date-time":"2020-09-29T18:46:49Z","timestamp":1601405209000},"page":"112887","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":45,"special_numbering":"C","title":["Mercaptoacetamide: A promising zinc-binding group for the discovery of selective histone deacetylase 6 inhibitors"],"prefix":"10.1016","volume":"209","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4400-7787","authenticated-orcid":false,"given":"Maur\u00edcio T.","family":"Tavares","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4795-5368","authenticated-orcid":false,"given":"Alan P.","family":"Kozikowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0295-2545","authenticated-orcid":false,"given":"Sida","family":"Shen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2020.112887_bib1","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.canlet.2008.03.037","article-title":"Histone deacetylase inhibitors: mechanisms of cell death and promise in combination cancer therapy","volume":"269","author":"Carew","year":"2008","journal-title":"Canc. Lett."},{"key":"10.1016\/j.ejmech.2020.112887_bib2","doi-asserted-by":"crossref","first-page":"32288","DOI":"10.1074\/jbc.M109.045856","article-title":"Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells","volume":"284","author":"Liu","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib3","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.02999","article-title":"Identification of \u2019erasers\u2019 for lysine crotonylated histone marks using a chemical proteomics approach","volume":"3","author":"Bao","year":"2014","journal-title":"Elife"},{"key":"10.1016\/j.ejmech.2020.112887_bib4","doi-asserted-by":"crossref","first-page":"103","DOI":"10.2217\/epi.14.69","article-title":"Histone deacetylase 6 in health and disease","volume":"7","author":"Seidel","year":"2015","journal-title":"Epigenomics"},{"key":"10.1016\/j.ejmech.2020.112887_bib5","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1002\/cmdc.201500486","article-title":"Why hydroxamates may not be the best histone deacetylase inhibitors--What some may have forgotten or would rather forget?","volume":"11","author":"Shen","year":"2016","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2020.112887_bib7","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1007\/s00280-011-1766-x","article-title":"Chidamide (CS055\/HBI-8000): a new histone deacetylase inhibitor of the benzamide class with antitumor activity and the ability to enhance immune cell-mediated tumor cell cytotoxicity","volume":"69","author":"Ning","year":"2012","journal-title":"Canc. Chemother. Pharmacol."},{"key":"10.1016\/j.ejmech.2020.112887_bib8","doi-asserted-by":"crossref","first-page":"7672","DOI":"10.1021\/acs.jmedchem.5b01044","article-title":"Discovery of novel class I histone deacetylase inhibitors with promising in\u00a0vitro and in\u00a0vivo antitumor activities","volume":"58","author":"Yao","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib9","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1007\/s00228-015-1846-7","article-title":"Population pharmacokinetics of intravenous and oral panobinostat in patients with hematologic and solid tumors","volume":"71","author":"Savelieva","year":"2015","journal-title":"Eur. J. Clin. Pharmacol."},{"key":"10.1016\/j.ejmech.2020.112887_bib10","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.bone.2013.08.024","article-title":"Vorinostat-induced bone loss might be related to drug toxicity","volume":"57","author":"Xu","year":"2013","journal-title":"Bone"},{"key":"10.1016\/j.ejmech.2020.112887_bib11","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1007\/s00280-007-0622-5","article-title":"Plasma and cerebrospinal fluid pharmacokinetics of the histone deacetylase inhibitor, belinostat (PXD101), in non-human primates","volume":"62","author":"Warren","year":"2008","journal-title":"Canc. Chemother. Pharmacol."},{"key":"10.1016\/j.ejmech.2020.112887_bib12","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s10147-011-0348-6","article-title":"Evaluation of safety, pharmacokinetics, and efficacy of vorinostat, a histone deacetylase inhibitor, in the treatment of gastrointestinal (GI) cancer in a phase I clinical trial","volume":"18","author":"Doi","year":"2013","journal-title":"Int. J. Clin. Oncol."},{"key":"10.1016\/j.ejmech.2020.112887_bib13","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1080\/13543776.2020.1725470","article-title":"Histone deacetylase (HDAC) inhibitors in cancer: a patent review (2017-present)","volume":"30","author":"Zhao","year":"2020","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2020.112887_bib14","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1074\/jbc.C500241200","article-title":"Two catalytic domains are required for protein deacetylation","volume":"281","author":"Zhang","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib15","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.bbrc.2005.12.144","article-title":"Characterization of the two catalytic domains in histone deacetylase 6","volume":"341","author":"Zou","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ejmech.2020.112887_bib16","doi-asserted-by":"crossref","first-page":"4389","DOI":"10.1073\/pnas.0430973100","article-title":"Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation","volume":"100","author":"Haggarty","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.ejmech.2020.112887_bib17","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/glia.22624","article-title":"HDAC6 inhibition results in tau acetylation and modulates tau phosphorylation and degradation in oligodendrocytes","volume":"62","author":"Noack","year":"2014","journal-title":"Glia"},{"key":"10.1016\/j.ejmech.2020.112887_bib18","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.molcel.2014.04.028","article-title":"HDAC6 deacetylates and ubiquitinates MSH2 to maintain proper levels of MutSalpha","volume":"55","author":"Zhang","year":"2014","journal-title":"Mol. Cell."},{"key":"10.1016\/j.ejmech.2020.112887_bib19","doi-asserted-by":"crossref","first-page":"4035","DOI":"10.1096\/fj.201801680R","article-title":"The unraveling of substrate specificity of histone deacetylase 6 domains using acetylome peptide microarrays and peptide libraries","volume":"33","author":"Kutil","year":"2019","journal-title":"Faseb. J."},{"key":"10.1016\/j.ejmech.2020.112887_bib20","doi-asserted-by":"crossref","first-page":"4912","DOI":"10.1021\/acs.biochem.9b00934","article-title":"Structural basis of catalysis and inhibition of HDAC6 CD1, the enigmatic catalytic domain of histone deacetylase 6","volume":"58","author":"Osko","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2020.112887_bib21","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1038\/nchembio.2140","article-title":"Structural insights into HDAC6 tubulin deacetylation and its selective inhibition","volume":"12","author":"Miyake","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ejmech.2020.112887_bib22","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/s41589-018-0180-7","article-title":"Acetylation of intrinsically disordered regions regulates phase separation","volume":"15","author":"Saito","year":"2019","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ejmech.2020.112887_bib23","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1107\/S2053230X20010250","article-title":"Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6","volume":"76","author":"Osko","year":"2020","journal-title":"Acta Crystallogr. F Struct. Biol. Commun."},{"key":"10.1016\/j.ejmech.2020.112887_bib24","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.molcel.2007.05.033","article-title":"HDAC6 modulates cell motility by altering the acetylation level of cortactin","volume":"27","author":"Zhang","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1016\/j.ejmech.2020.112887_bib25","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.molcel.2005.04.021","article-title":"HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor","volume":"18","author":"Kovacs","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1016\/j.ejmech.2020.112887_bib26","doi-asserted-by":"crossref","first-page":"12487","DOI":"10.1074\/jbc.M114.607580","article-title":"Histone deacetylase 6 (HDAC6) promotes the pro-survival activity of 14-3-3zeta via deacetylation of lysines within the 14-3-3zeta binding pocket","volume":"290","author":"Mortenson","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib27","doi-asserted-by":"crossref","first-page":"9633","DOI":"10.1073\/pnas.0803749105","article-title":"HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation","volume":"105","author":"Parmigiani","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.ejmech.2020.112887_bib28","first-page":"170","article-title":"Pharmocologic treatment with histone deacetylase 6 inhibitor (ACY-738) recovers Alzheimer\u2019s disease phenotype in amyloid precursor protein\/presenilin 1 (APP\/PS1) mice","volume":"1","author":"Majid","year":"2015","journal-title":"Alzheimers Dement"},{"key":"10.1016\/j.ejmech.2020.112887_bib29","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1038\/nm.2396","article-title":"HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease","volume":"17","author":"d\u2019Ydewalle","year":"2011","journal-title":"Nat. Med."},{"key":"10.1016\/j.ejmech.2020.112887_bib30","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1038\/s41467-018-03461-z","article-title":"Aberrant GlyRS-HDAC6 interaction linked to axonal transport deficits in Charcot-Marie-Tooth neuropathy","volume":"9","author":"Mo","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2020.112887_bib31","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1093\/brain\/awx375","article-title":"HDAC6 is a therapeutic target in mutant GARS-induced Charcot-Marie-Tooth disease","volume":"141","author":"Benoy","year":"2018","journal-title":"Brain"},{"key":"10.1016\/j.ejmech.2020.112887_bib32","doi-asserted-by":"crossref","first-page":"113281","DOI":"10.1016\/j.expneurol.2020.113281","article-title":"HDAC6 inhibition promotes alpha-tubulin acetylation and ameliorates CMT2A peripheral neuropathy in mice","volume":"328","author":"Picci","year":"2020","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.ejmech.2020.112887_bib33","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1038\/s41467-017-00911-y","article-title":"HDAC6 inhibition reverses axonal transport defects in motor neurons derived from FUS-ALS patients","volume":"8","author":"Guo","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2020.112887_bib34","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1186\/s40478-019-0750-2","article-title":"Restoration of histone acetylation ameliorates disease and metabolic abnormalities in a FUS mouse model","volume":"7","author":"Rossaert","year":"2019","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.ejmech.2020.112887_bib35","doi-asserted-by":"crossref","first-page":"68","DOI":"10.3389\/fncel.2014.00068","article-title":"A\u00a0selective histone deacetylase-6 inhibitor improves BDNF trafficking in hippocampal neurons from Mecp2 knockout mice: implications for Rett syndrome","volume":"8","author":"Xu","year":"2014","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112887_bib36","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s00109-014-1202-x","article-title":"MeCP2 deficiency is associated with reduced levels of tubulin acetylation and can be restored using HDAC6 inhibitors","volume":"93","author":"Gold","year":"2015","journal-title":"J.\u00a0Mol. Med."},{"key":"10.1016\/j.ejmech.2020.112887_bib37","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1080\/13543776.2019.1708901","article-title":"A\u00a0patent review of histone deacetylase 6 inhibitors in neurodegenerative diseases (2014-2019)","volume":"30","author":"Shen","year":"2020","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2020.112887_bib38","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1021\/acs.jmedchem.9b00924","article-title":"Old but gold: tracking the new guise of histone deacetylase 6 (HDAC6) enzyme as a biomarker and therapeutic target in rare diseases","volume":"63","author":"Brindisi","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib39","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/s00280-018-3721-6","article-title":"Role of the HDAC6\/STAT3 pathway in regulating PD-L1 expression in osteosarcoma cell lines","volume":"83","author":"Keremu","year":"2019","journal-title":"Canc. Chemother. Pharmacol."},{"key":"10.1016\/j.ejmech.2020.112887_bib40","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/j.molonc.2015.12.012","article-title":"Essential role of HDAC6 in the regulation of PD-L1 in melanoma","volume":"10","author":"Lienlaf","year":"2016","journal-title":"Mol. Oncol."},{"key":"10.1016\/j.ejmech.2020.112887_bib41","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1016\/j.molonc.2015.04.002","article-title":"Targeting histone deacetylase 6 mediates a dual anti-melanoma effect: enhanced antitumor immunity and impaired cell proliferation","volume":"9","author":"Woan","year":"2015","journal-title":"Mol. Oncol."},{"key":"10.1016\/j.ejmech.2020.112887_bib42","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1021\/acsmedchemlett.7b00223","article-title":"Synthesis and pharmacological evaluation of selective histone deacetylase 6 inhibitors in melanoma models","volume":"8","author":"Tavares","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112887_bib43","doi-asserted-by":"crossref","first-page":"8557","DOI":"10.1021\/acs.jmedchem.9b00946","article-title":"Discovery of a new isoxazole-3-hydroxamate-based histone deacetylase 6 inhibitor SS-208 with antitumor activity in syngeneic melanoma mouse models","volume":"62","author":"Shen","year":"2019","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib44","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1016\/j.jaci.2014.10.002","article-title":"Histone deacetylase 6 inhibition impairs effector CD8 T-cell functions during skin inflammation","volume":"135","author":"Tsuji","year":"2015","journal-title":"J.\u00a0Allergy Clin. Immunol."},{"key":"10.1016\/j.ejmech.2020.112887_bib45","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1093\/carcin\/bgx121","article-title":"A\u00a0potent hydroxamic acid-based, small-molecule inhibitor A452 preferentially inhibits HDAC6 activity and induces cytotoxicity toward cancer cells irrespective of p53 status","volume":"39","author":"Ryu","year":"2018","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.ejmech.2020.112887_bib46","doi-asserted-by":"crossref","first-page":"6136","DOI":"10.1038\/s41598-019-42237-3","article-title":"Selective HDAC6 inhibitors improve anti-PD-1 immune checkpoint blockade therapy by decreasing the anti-inflammatory phenotype of macrophages and down-regulation of immunosuppressive proteins in tumor cells","volume":"9","author":"Knox","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2020.112887_bib47","first-page":"307","article-title":"The role of epigenetic mechanisms and processes in autoimmune disorders","volume":"6","author":"Greer","year":"2012","journal-title":"Biologics"},{"key":"10.1016\/j.ejmech.2020.112887_bib48","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1186\/s13045-018-0654-9","article-title":"Histone deacetylase 6 in cancer","volume":"11","author":"Li","year":"2018","journal-title":"J.\u00a0Hematol. Oncol."},{"key":"10.1016\/j.ejmech.2020.112887_bib49","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1080\/14728222.2018.1541235","article-title":"HDAC6 as a potential therapeutic target for peripheral nerve disorders","volume":"22","author":"Prior","year":"2018","journal-title":"Expert Opin. Ther. Targets"},{"key":"10.1016\/j.ejmech.2020.112887_bib50","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1021\/acschemneuro.0c00074","article-title":"Translation of HDAC6 PET imaging using [(18)F]EKZ-001-cGMP production and measurement of HDAC6 target occupancy in nonhuman primates","volume":"11","author":"Celen","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112887_bib51","article-title":"Clinical validation of the novel HDAC6 radiotracer [(18)F]EKZ-001 in the human brain","author":"Koole","year":"2020","journal-title":"Eur. J. Nucl. Med. Mol. Imag."},{"key":"10.1016\/j.ejmech.2020.112887_bib52","unstructured":"Clinical Trials for Ricolinostat. https:\/\/clinicaltrials.gov\/ct2\/results?term=ACY-1215&amp;Search=Search (accessed Mar 27, 2020)."},{"key":"10.1016\/j.ejmech.2020.112887_bib54","doi-asserted-by":"crossref","first-page":"2579","DOI":"10.1182\/blood-2011-10-387365","article-title":"Preclinical activity, pharmacodynamic, and pharmacokinetic properties of a selective HDAC6 inhibitor, ACY-1215, in combination with bortezomib in multiple myeloma","volume":"119","author":"Santo","year":"2012","journal-title":"Blood"},{"key":"10.1016\/j.ejmech.2020.112887_bib55","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.18632\/oncotarget.13738","article-title":"Selective HDAC inhibition by ACY-241 enhances the activity of paclitaxel in solid tumor models","volume":"8","author":"Huang","year":"2017","journal-title":"Oncotarget"},{"key":"10.1016\/j.ejmech.2020.112887_bib56","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1016\/j.ejmech.2017.10.040","article-title":"Recent advances in the discovery of potent and selective HDAC6 inhibitors","volume":"143","author":"Wang","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib57","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1080\/13543776.2018.1459568","article-title":"HDAC inhibitors: a 2013-2017 patent survey","volume":"28","author":"Faria Freitas","year":"2018","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2020.112887_bib58","doi-asserted-by":"crossref","first-page":"9868","DOI":"10.1039\/C5CC03295D","article-title":"Synthesis of benzothiophene-based hydroxamic acids as potent and selective HDAC6 inhibitors","volume":"51","author":"De Vreese","year":"2015","journal-title":"Chem. Commun."},{"key":"10.1016\/j.ejmech.2020.112887_bib59","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1021\/acschemneuro.8b00600","article-title":"Brain penetrable histone deacetylase 6 inhibitor SW-100 ameliorates memory and learning impairments in a mouse model of Fragile X syndrome","volume":"10","author":"Kozikowski","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112887_bib60","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1038\/ja.2011.35","article-title":"Romidepsin (Istodax, NSC 630176, FR901228, FK228, depsipeptide): a natural product recently approved for cutaneous T-cell lymphoma","volume":"64","author":"VanderMolen","year":"2011","journal-title":"J.\u00a0Antibiot."},{"key":"10.1016\/j.ejmech.2020.112887_bib61","doi-asserted-by":"crossref","first-page":"5425","DOI":"10.1021\/jm7009217","article-title":"Design, synthesis, structure--selectivity relationship, and effect on human cancer cells of a novel series of histone deacetylase 6-selective inhibitors","volume":"50","author":"Itoh","year":"2007","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib62","doi-asserted-by":"crossref","first-page":"4809","DOI":"10.1021\/jm060554y","article-title":"Highly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate","volume":"49","author":"Suzuki","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib63","doi-asserted-by":"crossref","first-page":"8358","DOI":"10.1021\/jm5008209","article-title":"ST7612AA1, a thioacetate-omega(gamma-lactam carboxamide) derivative selected from a novel generation of oral HDAC inhibitors","volume":"57","author":"Giannini","year":"2014","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib64","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.bmcl.2008.11.081","article-title":"Sulfamides as novel histone deacetylase inhibitors","volume":"19","author":"Wahhab","year":"2009","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib65","doi-asserted-by":"crossref","first-page":"4320","DOI":"10.1016\/j.bmcl.2015.07.065","article-title":"Discovery of 1-hydroxypyridine-2-thiones as selective histone deacetylase inhibitors and their potential application for treating leukemia","volume":"25","author":"Muthyala","year":"2015","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib66","doi-asserted-by":"crossref","first-page":"3985","DOI":"10.1021\/jm800093c","article-title":"Trithiocarbonates as a novel class of HDAC inhibitors: SAR studies, isoenzyme selectivity, and pharmacological profiles","volume":"51","author":"Dehmel","year":"2008","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib67","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1007\/s00044-011-9623-3","article-title":"Design, synthesis, and biological evaluation of novel 2,4-thiazolidinedione derivatives as histone deacetylase inhibitors targeting liver cancer cell line","volume":"21","author":"Mohan","year":"2012","journal-title":"Med. Chem. Res."},{"key":"10.1016\/j.ejmech.2020.112887_bib68","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1021\/jm301769u","article-title":"3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition","volume":"56","author":"Patil","year":"2013","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib69","doi-asserted-by":"crossref","first-page":"9969","DOI":"10.1021\/jm401225q","article-title":"Synthesis and structure-activity relationship of 3-hydroxypyridine-2-thione-based histone deacetylase inhibitors","volume":"56","author":"Sodji","year":"2013","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib70","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.bmcl.2004.10.074","article-title":"Identification of a potent non-hydroxamate histone deacetylase inhibitor by mechanism-based drug design","volume":"15","author":"Suzuki","year":"2005","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib71","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/j.bmcl.2005.01.006","article-title":"Chemistry and biology of mercaptoacetamides as novel histone deacetylase inhibitors","volume":"15","author":"Chen","year":"2005","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib72","doi-asserted-by":"crossref","first-page":"3320","DOI":"10.1016\/j.bmc.2005.12.047","article-title":"Carbonyl- and sulfur-containing analogs of suberoylanilide hydroxamic acid: potent inhibition of histone deacetylases","volume":"14","author":"Gu","year":"2006","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib73","doi-asserted-by":"crossref","first-page":"3054","DOI":"10.1021\/jm070178x","article-title":"Functional differences in epigenetic modulators-superiority of mercaptoacetamide-based histone deacetylase inhibitors relative to hydroxamates in cortical neuron neuroprotection studies","volume":"50","author":"Kozikowski","year":"2007","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib74","doi-asserted-by":"crossref","first-page":"3442","DOI":"10.1016\/j.jmb.2014.03.007","article-title":"Molecular basis for the antiparasitic activity of a mercaptoacetamide derivative that inhibits histone deacetylase 8 (HDAC8) from the human pathogen schistosoma mansoni","volume":"426","author":"Stolfa","year":"2014","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2020.112887_bib75","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1021\/ci800366f","article-title":"Novel inhibitors of human histone deacetylase (HDAC) identified by QSAR modeling of known inhibitors, virtual screening, and experimental validation","volume":"49","author":"Tang","year":"2009","journal-title":"J.\u00a0Chem. Inf. Model."},{"key":"10.1016\/j.ejmech.2020.112887_bib76","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1002\/cmdc.200700314","article-title":"Chemistry, biology, and QSAR studies of substituted biaryl hydroxamates and mercaptoacetamides as HDAC inhibitors-nanomolar-potency inhibitors of pancreatic cancer cell growth","volume":"3","author":"Kozikowski","year":"2008","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2020.112887_bib77","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1002\/cmdc.201100522","article-title":"Chiral mercaptoacetamides display enantioselective inhibition of histone deacetylase 6 and exhibit neuroprotection in cortical neuron models of oxidative stress","volume":"7","author":"Kalin","year":"2012","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2020.112887_bib78","doi-asserted-by":"crossref","first-page":"4370","DOI":"10.1021\/jm8002894","article-title":"Use of the nitrile oxide cycloaddition (NOC) reaction for molecular probe generation: a new class of enzyme selective histone deacetylase inhibitors (HDACIs) showing picomolar activity at HDAC6","volume":"51","author":"Kozikowski","year":"2008","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib79","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.bmcl.2015.12.007","article-title":"Novel thiol-based histone deacetylase inhibitors bearing 3-phenyl-1H-pyrazole-5-carboxamide scaffold as surface recognition motif: design, synthesis and SAR study","volume":"26","author":"Wen","year":"2016","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib80","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1021\/acsmedchemlett.5b00303","article-title":"Thiol-based potent and selective HDAC6 inhibitors promote tubulin acetylation and T-regulatory cell suppressive function","volume":"6","author":"Segretti","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112887_bib81","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1021\/acsmedchemlett.7b00012","article-title":"Design and synthesis of mercaptoacetamides as potent, selective, and brain permeable histone deacetylase 6 inhibitors","volume":"8","author":"Lv","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112887_bib82","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1016\/j.bmcl.2005.02.075","article-title":"Mercaptoamide-based non-hydroxamic acid type histone deacetylase inhibitors","volume":"15","author":"Anandan","year":"2005","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib83","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.expneurol.2012.10.005","article-title":"Mercaptoacetamide-based class II HDAC inhibitor lowers Abeta levels and improves learning and memory in a mouse model of Alzheimer\u2019s disease","volume":"239","author":"Sung","year":"2013","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.ejmech.2020.112887_bib84","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1021\/jm049207j","article-title":"Novel inhibitors of human histone deacetylases: design, synthesis, enzyme inhibition, and cancer cell growth inhibition of SAHA-based non-hydroxamates","volume":"48","author":"Suzuki","year":"2005","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib85","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/j.sbi.2011.08.004","article-title":"Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes","volume":"21","author":"Lombardi","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ejmech.2020.112887_bib86","first-page":"4916","article-title":"FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases","volume":"62","author":"Furumai","year":"2002","journal-title":"Canc. Res."},{"key":"10.1016\/j.ejmech.2020.112887_bib87","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1021\/acsmedchemlett.8b00487","article-title":"Molecular basis for the selective inhibition of histone deacetylase 6 by a mercaptoacetamide inhibitor","volume":"9","author":"Porter","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112887_bib88","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1038\/nchembio.2134","article-title":"Histone deacetylase 6 structure and molecular basis of catalysis and inhibition","volume":"12","author":"Hai","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ejmech.2020.112887_bib89","doi-asserted-by":"crossref","first-page":"127023","DOI":"10.1016\/j.bmcl.2020.127023","article-title":"Structural determinants of affinity and selectivity in the binding of inhibitors to histone deacetylase 6","volume":"30","author":"Osko","year":"2020","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2020.112887_bib90","doi-asserted-by":"crossref","first-page":"1138","DOI":"10.1021\/acs.jmedchem.8b01090","article-title":"Synthesis and biological investigation of phenothiazine-based benzhydroxamic acids as selective histone deacetylase 6 inhibitors","volume":"62","author":"Vogerl","year":"2019","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib91","doi-asserted-by":"crossref","first-page":"8054","DOI":"10.1021\/acs.jmedchem.8b01013","article-title":"Histone deacetylase 6-selective inhibitors and the influence of capping groups on hydroxamate-zinc denticity","volume":"61","author":"Porter","year":"2018","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib92","doi-asserted-by":"crossref","first-page":"13459","DOI":"10.1073\/pnas.1718823114","article-title":"Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors","volume":"114","author":"Porter","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.ejmech.2020.112887_bib93","doi-asserted-by":"crossref","first-page":"1517","DOI":"10.1002\/cmdc.201800238","article-title":"Synthesis, crystallization studies, and in\u00a0vitro characterization of cinnamic acid derivatives as smHDAC8 inhibitors for the treatment of schistosomiasis","volume":"13","author":"Bayer","year":"2018","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2020.112887_bib94","doi-asserted-by":"crossref","first-page":"3916","DOI":"10.1021\/acs.biochem.8b00367","article-title":"Entropy as a driver of selectivity for inhibitor binding to histone deacetylase 6","volume":"57","author":"Porter","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2020.112887_bib95","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.ejmech.2017.04.013","article-title":"Synthesis and applications of benzohydroxamic acid-based histone deacetylase inhibitors","volume":"135","author":"De Vreese","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib96","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1021\/acs.jmedchem.9b01540","article-title":"Exploring structural determinants of inhibitor affinity and selectivity in complexes with histone deacetylase 6","volume":"63","author":"Osko","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112887_bib97","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1021\/acsmedchemlett.9b00560","article-title":"Structural and in\u00a0vivo characterization of Tubastatin A, a widely used histone deacetylase 6 inhibitor","volume":"11","author":"Shen","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2020.112887_bib98","doi-asserted-by":"crossref","first-page":"6081","DOI":"10.1021\/bi00440a052","article-title":"Geometry of interaction of metal ions with sulfur-containing ligands in protein structures","volume":"28","author":"Chakrabarti","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2020.112887_bib99","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.ijpharm.2008.05.001","article-title":"In\u00a0vitro plasma stability, permeability and solubility of mercaptoacetamide histone deacetylase inhibitors","volume":"361","author":"Konsoula","year":"2008","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.ejmech.2020.112887_bib100","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1248\/bpb.32.74","article-title":"Involvement of P-glycoprotein and multidrug resistance associated protein 1 on the transepithelial transport of a mercaptoacetamide-based histone-deacetylase inhibitor in Caco-2 cells","volume":"32","author":"Konsoula","year":"2009","journal-title":"Biol. Pharm. Bull."},{"key":"10.1016\/j.ejmech.2020.112887_bib101","doi-asserted-by":"crossref","first-page":"2844","DOI":"10.1158\/1535-7163.MCT-09-0629","article-title":"Pharmacokinetics-pharmacodynamics and antitumor activity of mercaptoacetamide-based histone deacetylase inhibitors","volume":"8","author":"Konsoula","year":"2009","journal-title":"Mol. Canc. Therapeut."},{"key":"10.1016\/j.ejmech.2020.112887_bib102","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1021\/cn200100h","article-title":"Knowledge-based, central nervous system (CNS) lead selection and lead optimization for CNS drug discovery","volume":"3","author":"Ghose","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112887_bib103","doi-asserted-by":"crossref","first-page":"4672","DOI":"10.1002\/jcb.26133","article-title":"A\u00a0Mercaptoacetamide-based class II histone deacetylase inhibitor suppresses cell migration and invasion in monomorphic malignant human glioma cells by inhibiting FAK\/STAT3 signaling","volume":"118","author":"Nam","year":"2017","journal-title":"J.\u00a0Cell. Biochem."},{"key":"10.1016\/j.ejmech.2020.112887_bib104","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/7854_2012_220","article-title":"All about running: synaptic plasticity, growth factors and adult hippocampal neurogenesis","volume":"15","author":"Vivar","year":"2013","journal-title":"Curr. Top Behav. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112887_bib105","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0057808","article-title":"Rapamycin reverses status epilepticus-induced memory deficits and dendritic damage","volume":"8","author":"Brewster","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2020.112887_bib106","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1016\/j.neurobiolaging.2012.06.027","article-title":"Effects of different amyloid beta-protein analogues on synaptic function","volume":"34","author":"Ripoli","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.ejmech.2020.112887_bib107","doi-asserted-by":"crossref","first-page":"591","DOI":"10.3233\/JAD-150717","article-title":"A\u00a0Mercaptoacetamide-based class II histone deacetylase inhibitor increases dendritic spine density via RasGRF1\/ERK pathway","volume":"51","author":"Song","year":"2016","journal-title":"J.\u00a0Alzheimers Dis."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S022352342030859X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S022352342030859X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T14:16:45Z","timestamp":1759328205000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S022352342030859X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1]]},"references-count":105,"alternative-id":["S022352342030859X"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2020.112887","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2021,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mercaptoacetamide: A promising zinc-binding group for the discovery of selective histone deacetylase 6 inhibitors","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2020.112887","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"112887"}}