{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T23:06:38Z","timestamp":1792796798155,"version":"4.5.0"},"reference-count":87,"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\/"}],"funder":[{"DOI":"10.13039\/501100003091","name":"Shandong Province","doi-asserted-by":"publisher","award":["2015ZDJS04001"],"award-info":[{"award-number":["2015ZDJS04001"]}],"id":[{"id":"10.13039\/501100003091","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":[[2018,1]]},"DOI":"10.1016\/j.ejmech.2017.10.040","type":"journal-article","created":{"date-parts":[[2017,10,16]],"date-time":"2017-10-16T22:32:57Z","timestamp":1508193177000},"page":"1406-1418","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":140,"special_numbering":"C","title":["Recent advances in the discovery of potent and selective HDAC6 inhibitors"],"prefix":"10.1016","volume":"143","author":[{"given":"Xiu-Xiu","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ren-Zhong","family":"Wan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhao-Peng","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2017.10.040_bib1","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.biochi.2007.06.009","article-title":"Regulation of protein turnover by acetyltransferases and deacetylases","volume":"90","author":"Sadoul","year":"2008","journal-title":"Biochimie"},{"key":"10.1016\/j.ejmech.2017.10.040_bib2","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1016\/j.drudis.2009.06.008","article-title":"Histone acetyl transferases as emerging drug targets","volume":"14","author":"Dekker","year":"2009","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.ejmech.2017.10.040_bib3","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1038\/nrd2133","article-title":"Anticancer activities of histone deacetylase inhibitors","volume":"5","author":"Bolden","year":"2006","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2017.10.040_bib4","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.it.2011.04.001","article-title":"Histone deacetylases as regulators of inflammation and immunity","volume":"32","author":"Shakespear","year":"2011","journal-title":"Trends Immunol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib5","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.tins.2009.06.002","article-title":"Multiple roles of HDAC inhibition in neurodegenerative conditions","volume":"32","author":"Chuang","year":"2009","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.ejmech.2017.10.040_bib6","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S1074-5521(02)00092-3","article-title":"Deacetylase enzymes: biological functions and the use of small-molecule inhibitors","volume":"9","author":"Grozinger","year":"2002","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib7","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/S0168-9525(03)00073-8","article-title":"Class II histone deacetylases: versatile regulators","volume":"19","author":"Verdin","year":"2003","journal-title":"Trends Genet."},{"key":"10.1016\/j.ejmech.2017.10.040_bib8","doi-asserted-by":"crossref","first-page":"25748","DOI":"10.1074\/jbc.M111871200","article-title":"Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family","volume":"277","author":"Gao","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib9","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.cbpa.2009.05.007","article-title":"Creating zinc monkey wrenches in the treatment of epigenetic disorders","volume":"13","author":"Kalin","year":"2009","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib10","doi-asserted-by":"crossref","first-page":"505","DOI":"10.2174\/138161208783885353","article-title":"Chemical origins of isoform selectivity in histone deacetylase inhibitors","volume":"14","author":"Butler","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.ejmech.2017.10.040_bib11","first-page":"302","article-title":"Discovery of selective histone deacetylase 6 inhibitors using the quinazoline as the cap for the treatment of cancer","volume":"59","author":"Yang","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib12","doi-asserted-by":"crossref","first-page":"505","DOI":"10.4155\/fmc.12.3","article-title":"Targeted cancer therapy: giving histone deacetylase inhibitors all they need to succeed","volume":"4","author":"Gryder","year":"2012","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib13","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.lungcan.2004.03.002","article-title":"Phase II trial of the histone deacetylase inhibitor pivaloyloxymethylbutyrate (Pivanex, AN-9) in advanced non-small cell lung cancer","volume":"45","author":"Reid","year":"2004","journal-title":"Lung Cancer"},{"key":"10.1016\/j.ejmech.2017.10.040_bib14","doi-asserted-by":"crossref","first-page":"415","DOI":"10.2174\/1568026615666150813145629","article-title":"Selective histone deacetylase inhibitors with anticancer activity","volume":"16","author":"Ma","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib15","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.2017.10.040_bib16","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/j.ejmech.2016.05.047","article-title":"Inside HDACs with more selective HDAC inhibitors","volume":"121","author":"Roche","year":"2016","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib17","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.2017.10.040_bib18","doi-asserted-by":"crossref","first-page":"22516","DOI":"10.1074\/jbc.M113.489328","article-title":"Inhibition of HDAC6 deacetylase activity increases its binding with microtubules and suppresses microtubule dynamic instability in MCF-7 cells","volume":"288","author":"Asthana","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib19","doi-asserted-by":"crossref","first-page":"2011","DOI":"10.1016\/j.bmc.2007.10.092","article-title":"Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs)","volume":"16","author":"Sch\u00e4fer","year":"2008","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib20","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.2017.10.040_bib21","doi-asserted-by":"crossref","first-page":"6820","DOI":"10.1093\/emboj\/cdf682","article-title":"In\u00a0vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation","volume":"21","author":"Matsuyama","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.ejmech.2017.10.040_bib22","doi-asserted-by":"crossref","first-page":"26729","DOI":"10.1074\/jbc.C500186200","article-title":"Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors","volume":"280","author":"Bali","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib23","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.2017.10.040_bib24","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.2017.10.040_bib25","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1002\/emmm.201201923","article-title":"Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease","volume":"5","author":"Govindarajan","year":"2013","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.ejmech.2017.10.040_bib26","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.bcp.2012.06.014","article-title":"Development and therapeutic impact of HDAC6-selective inhibitors","volume":"84","author":"Dallavalle","year":"2012","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib27","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.2017.10.040_bib28","doi-asserted-by":"crossref","first-page":"10842","DOI":"10.1021\/ja102758v","article-title":"Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, Tubastatin A","volume":"132","author":"Butler","year":"2010","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2017.10.040_bib29","first-page":"383","article-title":"Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays","volume":"10","author":"Haggarty","year":"2003","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib30","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.2017.10.040_bib31","doi-asserted-by":"crossref","first-page":"2898","DOI":"10.1021\/jm7015254","article-title":"Structural origin of selectivity in class II-selective histone deacetylase inhibitors","volume":"51","author":"Estiu","year":"2008","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib32","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1002\/cmdc.200800196","article-title":"Pyridylalanine-containing hydroxamic acids as selective HDAC6 inhibitors","volume":"4","author":"Schafer","year":"2009","journal-title":"Chem. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib33","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1158\/1541-7786.MCR-07-2110","article-title":"Destabilization of ERBB2 transcripts by targeting 3' untranslated region messenger RNA associated HuR and histone deacetylase-6","volume":"6","author":"Scott","year":"2008","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.ejmech.2017.10.040_bib34","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.2017.10.040_bib35","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1021\/jm701606b","article-title":"A\u00a0series of potent and selective, triazolylphenyl-based histone deacetylases inhibitors with activity against pancreatic cancer cells and plasmodium falciparum","volume":"51","author":"Chen","year":"2008","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib36","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\u2014nanomolar-potency inhibitors of pancreatic cancer cell growth","volume":"3","author":"Kozikowski","year":"2008","journal-title":"Chem. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib37","doi-asserted-by":"crossref","first-page":"3033","DOI":"10.1021\/ja809508f","article-title":"Design, synthesis, biological evaluation, and structural characterization of potent histone deacetylase inhibitors based on cyclic \u03b1\/\u03b2-tetrapeptide architectures","volume":"131","author":"Montero","year":"2009","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2017.10.040_bib38","doi-asserted-by":"crossref","first-page":"7836","DOI":"10.1021\/jm900850t","article-title":"Discovery of potent and selective histone deacetylase inhibitors via focused combinatorial libraries of cyclic \u03b13\u03b2-tetrapeptides","volume":"52","author":"Olsen","year":"2009","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib39","doi-asserted-by":"crossref","first-page":"6261","DOI":"10.1016\/j.bmcl.2007.09.014","article-title":"\u03c9-Alkoxy analogues of SAHA (vorinostat) as inhibitors of HDAC: a study of chain-length and stereochemical dependence","volume":"17","author":"Hanessian","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2017.10.040_bib40","doi-asserted-by":"crossref","first-page":"8387","DOI":"10.1021\/jm101092u","article-title":"Non-natural macrocyclic inhibitors of histone deacetylases: design, synthesis, and activity","volume":"53","author":"Auzzas","year":"2010","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib41","doi-asserted-by":"crossref","first-page":"7067","DOI":"10.1016\/j.bmcl.2010.09.100","article-title":"Inhibitors selective for HDAC6 in enzymes and cells","volume":"20","author":"Gupta","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2017.10.040_bib42","doi-asserted-by":"crossref","first-page":"2216","DOI":"10.1016\/j.bmcl.2007.01.117","article-title":"Structural requirements of HDAC inhibitors: SAHA analogs functionalized adjacent to the hydroxamic acid","volume":"17","author":"Bieliauskas","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2017.10.040_bib43","doi-asserted-by":"crossref","first-page":"6139","DOI":"10.1016\/j.bmcl.2011.08.027","article-title":"The structural requirements of histone deacetylase inhibitors: suberoylanilide hydroxamic acid analogs modified at the C3 position display isoform selectivity","volume":"21","author":"Choi","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2017.10.040_bib44","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1158\/1535-7163.MCT-10-0779","article-title":"Histone deacetylase cytoplasmic trapping by a novel fluorescent HDAC inhibitor","volume":"10","author":"Kong","year":"2011","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.ejmech.2017.10.040_bib45","doi-asserted-by":"crossref","first-page":"35042","DOI":"10.1074\/jbc.M105086200","article-title":"The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking","volume":"276","author":"Zhao","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib46","doi-asserted-by":"crossref","first-page":"4325","DOI":"10.1021\/acs.jmedchem.5b00317","article-title":"Design, synthesis and antitumor evaluation of novel histone deacetylase (HDAC) inhibitors equipped with phenylsulfonylfuroxan module as nitric oxide donor","volume":"58","author":"Duan","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib47","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1038\/nature07238","article-title":"S-nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons","volume":"455","author":"Nott","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2017.10.040_bib48","doi-asserted-by":"crossref","first-page":"19183","DOI":"10.1073\/pnas.0805514105","article-title":"HDAC2 blockade by nitric oxide and histone deacetylase inhibitors reveals a common target in Duchenne muscular dystrophy treatment","volume":"105","author":"Colussi","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2017.10.040_bib49","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.2017.10.040_bib50","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1002\/cmdc.201200529","article-title":"Discovery of pyridone-based histone deacetylase inhibitors: approaches for metabolic stability","volume":"8","author":"Cho","year":"2013","journal-title":"Chem. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib51","doi-asserted-by":"crossref","first-page":"6775","DOI":"10.1021\/jm400564j","article-title":"Quinazolin-4-one derivatives as selective histone deacetylase-6 inhibitors for the treatment of Alzheimer's disease","volume":"56","author":"Yu","year":"2013","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib52","doi-asserted-by":"crossref","first-page":"4009","DOI":"10.1021\/jm401899x","article-title":"Azaindolylsulfonamides, with a more selective inhibitory effect on histone deacetylase 6 activity, exhibit antitumor activity in colorectal cancer HCT116 cells","volume":"57","author":"Lee","year":"2014","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib53","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1038\/bjc.2012.576","article-title":"A\u00a0novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth","volume":"108","author":"Kaliszczak","year":"2013","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.ejmech.2017.10.040_bib54","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1021\/jm301355j","article-title":"Potent and selective inhibition of histone deacetylase 6 (HDAC6) does not require a surface-binding motif","volume":"56","author":"Wagner","year":"2013","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib55","doi-asserted-by":"crossref","first-page":"7201","DOI":"10.1021\/jm400385r","article-title":"Potent histone deacetylase inhibitors derived from 4-(aminomethyl)-N-hydroxybenzamide with high selectivity for the HDAC6 isoform","volume":"56","author":"Blackburn","year":"2013","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib56","doi-asserted-by":"crossref","first-page":"5450","DOI":"10.1016\/j.bmcl.2014.10.022","article-title":"Histone deacetylase inhibitors derived from 1,2,3,4-tetrahydropyrrolo[1,2-a]pyrazine and related heterocycles selective for the HDAC6 isoform","volume":"24","author":"Blackburn","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2017.10.040_bib57","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1002\/cmdc.201100007","article-title":"Carbamate prodrug concept for hydroxamate HDAC inhibitors","volume":"6","author":"Schlimme","year":"2011","journal-title":"Chem. Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib58","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1021\/acs.jmedchem.5b01493","article-title":"Synthesis and biological investigation of oxazole hydroxamates as highly selective histone deacetylase 6 (HDAC6) inhibitors","volume":"59","author":"Senger","year":"2016","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib59","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.bmcl.2008.12.045","article-title":"Novel HDAC6 isoform selective chiral small molecule histone deacetylase inhibitors","volume":"19","author":"Smil","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2017.10.040_bib60","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.2017.10.040_bib61","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.intimp.2013.03.016","article-title":"Tubastatin, a selective histone deacetylase 6 inhibitor shows anti-inflammatory and anti-rheumatic effects","volume":"16","author":"Vishwakarma","year":"2013","journal-title":"Int. Immunopharmacol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib62","first-page":"637","article-title":"Selective inhibitor of histone deacetylase 6 (tubastatin A) suppresses proliferation of hepatitis C virus replicon in culture of human hepatocytes","volume":"79","author":"Kozlov","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2017.10.040_bib63","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1021\/jm200773h","article-title":"Second-generation histone deacetylase 6 inhibitors enhance the immunosuppressive effects of Foxp3+ T-regulatory cells","volume":"55","author":"Kalin","year":"2011","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib64","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1021\/acschemneuro.5b00286","article-title":"Bicyclic-capped histone deacetylase 6 inhibitors with improved activity in a model of axonal charcot-marie-tooth disease","volume":"7","author":"Shen","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2017.10.040_bib65","doi-asserted-by":"crossref","first-page":"9891","DOI":"10.1021\/jm301098e","article-title":"Selective histone deacetylase 6 inhibitors bearing substituted urea linkers inhibit melanoma cell growth","volume":"55","author":"Bergman","year":"2012","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib66","doi-asserted-by":"crossref","first-page":"3775","DOI":"10.1039\/c3cc41422a","article-title":"Potent and selective HDAC6 inhibitory activity of N-(4-hydroxycarbamoylbenzyl)-1,2,4,9-tetrahydro-3-thia-9-azafluorenes as novel sulfur analogues of tubastatin A","volume":"49","author":"Vreese","year":"2013","journal-title":"Chem. Commun."},{"key":"10.1016\/j.ejmech.2017.10.040_bib67","doi-asserted-by":"crossref","first-page":"2537","DOI":"10.1039\/C5OB02625C","article-title":"Synthesis and SAR assessment of novel Tubathian analogs in the pursuit of potent and selective HDAC6 inhibitors","volume":"14","author":"Vreese","year":"2016","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib68","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1002\/chem.201604167","article-title":"Synthesis of potent and selective HDAC6 inhibitors bearing a cyclohexane- or cycloheptane-annulated 1,5-benzothiazepine scaffold","volume":"23","author":"Vreese","year":"2017","journal-title":"Chemistry"},{"key":"10.1016\/j.ejmech.2017.10.040_bib69","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1039\/C5CC10301K","article-title":"Rational design and diversity-oriented synthesis of peptoid-based selective HDAC6 inhibitors","volume":"52","author":"Diedrich","year":"2016","journal-title":"Chem. Commun."},{"key":"10.1016\/j.ejmech.2017.10.040_bib70","doi-asserted-by":"crossref","first-page":"15704","DOI":"10.1073\/pnas.1313893110","article-title":"Development of a histone deacetylase 6 inhibitor and its biological effects","volume":"110","author":"Lee","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.ejmech.2017.10.040_bib71","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":"Vreese","year":"2015","journal-title":"Chem. Commun."},{"key":"10.1016\/j.ejmech.2017.10.040_bib72","doi-asserted-by":"crossref","first-page":"8026","DOI":"10.1021\/jm5008962","article-title":"Identification of a novel aminotetralin class of HDAC6 and HDAC8 selective inhibitors","volume":"57","author":"Tang","year":"2014","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib73","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1021\/jm502011f","article-title":"Design and synthesis of orally bioavailable aminopyrrolidinone histone deacetylase 6 inhibitors","volume":"58","author":"Lin","year":"2015","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib74","doi-asserted-by":"crossref","first-page":"10226","DOI":"10.1039\/C5OB01509J","article-title":"Pyrimidinedione-mediated selective histone deacetylase 6 inhibitors with antitumor activity in colorectal cancer HCT116 cells","volume":"13","author":"Liu","year":"2015","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib75","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.2017.10.040_bib76","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.2017.10.040_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.2017.10.040_bib78","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.2017.10.040_bib79","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.expneurol.2012.10.005","article-title":"Mercaptoacetamide-based class II HDAC inhibitor lowers A\u03b2 levels and improves learning and memory in a mouse model of Alzheimer's disease","volume":"239","author":"You","year":"2013","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.ejmech.2017.10.040_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.2017.10.040_bib81","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.2017.10.040_bib82","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.2017.10.040_bib83","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.2017.10.040_bib84","doi-asserted-by":"crossref","first-page":"9969","DOI":"10.1021\/jm401225q","article-title":"Synthesis and structure activity relationship of 3-hydroxypyridin-2-thione based histone deacetylase inhibitors","volume":"56","author":"Sodji","year":"2011","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2017.10.040_bib85","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.2017.10.040_bib86","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1021\/cb200134p","article-title":"A\u00a0novel class of small molecule inhibitors of HDAC6","volume":"7","author":"Inks","year":"2012","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.ejmech.2017.10.040_bib87","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.bcp.2015.11.005","article-title":"4-Hydroxybenzoic acid derivatives as HDAC6-specific inhibitors modulating microtubular structure and HSP90\u03b1 chaperone activity against prostate cancer","volume":"99","author":"Seidel","year":"2016","journal-title":"Biochem. Pharmacol."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523417308401?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523417308401?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,10,24]],"date-time":"2018-10-24T21:30:46Z","timestamp":1540416646000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523417308401"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,1]]},"references-count":87,"alternative-id":["S0223523417308401"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2017.10.040","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2018,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Recent advances in the discovery of potent and selective HDAC6 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.2017.10.040","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}