{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T08:09:15Z","timestamp":1793347755218,"version":"4.5.0"},"reference-count":51,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100002509","name":"Keimyung University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002509","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":[[2025,10]]},"DOI":"10.1016\/j.ejmech.2025.117785","type":"journal-article","created":{"date-parts":[[2025,5,22]],"date-time":"2025-05-22T06:44:29Z","timestamp":1747896269000},"page":"117785","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"special_numbering":"C","title":["Design, synthesis, and biological evaluation of indazole-based histone deacetylase 6 inhibitors"],"prefix":"10.1016","volume":"295","author":[{"given":"Khan Hashim","family":"Ali","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sunil K.","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong Jin","family":"Oh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mosharof","family":"Hossain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ji Hyun","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sun You","family":"Park","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Young Ho","family":"Seo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2025.117785_bib1","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1128\/MMBR.64.2.435-459.2000","article-title":"Acetylation of histones and transcription-related factors","volume":"64","author":"Sterner","year":"2000","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.ejmech.2025.117785_bib2","doi-asserted-by":"crossref","first-page":"3885","DOI":"10.1007\/s00018-014-1656-6","article-title":"Histone deacetylase inhibitors and cell death","volume":"71","author":"Zhang","year":"2014","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ejmech.2025.117785_bib3","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/38664","article-title":"Histone acetylation in chromatin structure and transcription","volume":"389","author":"Grunstein","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2025.117785_bib4","doi-asserted-by":"crossref","first-page":"5097","DOI":"10.1021\/jm0303094","article-title":"Histone deacetylase inhibitors","volume":"46","author":"Miller","year":"2003","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib5","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1126\/science.1175371","article-title":"Lysine acetylation targets protein complexes and co-regulates major cellular functions","volume":"325","author":"Choudhary","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2025.117785_bib6","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a018713","article-title":"Erasers of histone acetylation: the histone deacetylase enzymes","volume":"6","author":"Seto","year":"2014","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.ejmech.2025.117785_bib7","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s40264-018-0773-9","article-title":"Safety and tolerability of histone deacetylase (HDAC) inhibitors in oncology","volume":"42","author":"Shah","year":"2019","journal-title":"Drug Saf."},{"key":"10.1016\/j.ejmech.2025.117785_bib8","doi-asserted-by":"crossref","DOI":"10.1158\/1078-0432.CCR-06-1715","article-title":"HDAC inhibitors and cardiac safety","volume":"13","author":"Molife","year":"2007","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.ejmech.2025.117785_bib9","doi-asserted-by":"crossref","first-page":"5468","DOI":"10.1038\/sj.onc.1210614","article-title":"HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination","volume":"26","author":"Boyault","year":"2007","journal-title":"Oncogene"},{"key":"10.1016\/j.ejmech.2025.117785_bib10","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/j.cell.2009.06.049","article-title":"Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes","volume":"138","author":"Wang","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.ejmech.2025.117785_bib11","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.canlet.2008.08.016","article-title":"HDAC family: what are the cancer relevant targets?","volume":"277","author":"Witt","year":"2009","journal-title":"Cancer Lett."},{"key":"10.1016\/j.ejmech.2025.117785_bib12","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. Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2025.117785_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116447","article-title":"Preferential HDAC6 inhibitors derived from HPOB exhibit synergistic antileukemia activity in combination with decitabine","volume":"272","author":"Tretbar","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116884","article-title":"Tackling triple negative breast cancer with HDAC inhibitors: 6 is the isoform","volume":"279","author":"Guadagni","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib15","doi-asserted-by":"crossref","first-page":"32","DOI":"10.2174\/1574892815666200217125419","article-title":"Novel selective histone deacetylase 6 (HDAC6) inhibitors: a patent review (2016-2019)","volume":"15","author":"He","year":"2020","journal-title":"Recent Pat. Anticancer Drug Discov."},{"key":"10.1016\/j.ejmech.2025.117785_bib16","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1517\/13543784.2010.510514","article-title":"The clinical development of histone deacetylase inhibitors as targeted anticancer drugs","volume":"19","author":"Marks","year":"2010","journal-title":"Expet Opin. Invest. Drugs"},{"key":"10.1016\/j.ejmech.2025.117785_bib17","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. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib18","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.2174\/1871520618666180510113822","article-title":"Indazole derivatives: promising anti-tumor agents","volume":"18","author":"Wan","year":"2018","journal-title":"Anti Cancer Agents Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib19","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1002\/cmdc.201800253","article-title":"Recent advances in the development of indazole-based anticancer agents","volume":"13","author":"Dong","year":"2018","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2025.117785_bib20","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116676","article-title":"Biological and structural investigation of tetrahydro-\u03b2-carboline-based selective HDAC6 inhibitors with improved stability","volume":"276","author":"Scheuerer","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib21","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115776","article-title":"Tetrahydro-\u03b2-carboline derivatives as potent histone deacetylase 6 inhibitors with broad-spectrum antiproliferative activity","volume":"260","author":"Chen","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib22","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1002\/cmdc.202000149","article-title":"Design and synthesis of dihydroxamic acids as HDAC6\/8\/10 inhibitors","volume":"15","author":"Morgen","year":"2020","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2025.117785_bib23","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1007\/s12272-023-01467-w","article-title":"Exploring new histone deacetylase 6 inhibitors and their effects on reversing the \u03b1-tubulin deacetylation and cell morphology changes caused by methamphetamine","volume":"46","author":"Gupta","year":"2023","journal-title":"Arch Pharm. Res. (Seoul)"},{"key":"10.1016\/j.ejmech.2025.117785_bib24","doi-asserted-by":"crossref","first-page":"FDD53","DOI":"10.4155\/fdd-2020-0023","article-title":"Recent advances in small molecular modulators targeting histone deacetylase 6","volume":"2","author":"Xiao","year":"2020","journal-title":"Future Drug Discov."},{"key":"10.1016\/j.ejmech.2025.117785_bib25","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1021\/acsmedchemlett.9b00560","article-title":"Structural and in vivo 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.2025.117785_bib26","article-title":"Design, synthesis and biological evaluation of a series of CNS penetrant HDAC inhibitors structurally derived from amyloid-\u03b2 probes","volume":"9","author":"Choi","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2025.117785_bib27","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.116057","article-title":"Design, synthesis, and biological evaluation of HDAC6 inhibitors targeting L1 loop and serine 531 residue","volume":"265","author":"Jha","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib28","article-title":"Design, synthesis, and biological evaluation of histone deacetylase inhibitor with novel salicylamide zinc binding group","volume":"101","author":"Kim","year":"2022","journal-title":"Medicine (Baltim.)"},{"key":"10.1016\/j.ejmech.2025.117785_bib29","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1007\/s12272-018-1045-z","article-title":"Aspirin-inspired acetyl-donating HDACs inhibitors","volume":"41","author":"Lim","year":"2018","journal-title":"Arch Pharm. Res. (Seoul)"},{"key":"10.1016\/j.ejmech.2025.117785_bib30","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20246213","article-title":"Development of thiazolidinedione-based HDAC6 inhibitors to overcome methamphetamine addiction","volume":"20","author":"Sharma","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2025.117785_bib31","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.ejmech.2018.12.056","article-title":"A novel class of anthraquinone-based HDAC6 inhibitors","volume":"164","author":"Song","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib32","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":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.ejmech.2025.117785_bib33","doi-asserted-by":"crossref","DOI":"10.3390\/molecules26175151","article-title":"Non-hydroxamate zinc-binding groups as warheads for histone deacetylases","volume":"26","author":"Fr\u00fchauf","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2025.117785_bib34","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1021\/acs.jmedchem.1c01472","article-title":"Potent hydrazide-based HDAC inhibitors with a superior pharmacokinetic profile for efficient treatment of acute myeloid leukemia in vivo","volume":"65","author":"Jiang","year":"2022","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib35","doi-asserted-by":"crossref","first-page":"12140","DOI":"10.1021\/acs.jmedchem.2c00853","article-title":"First-in-Class hydrazide-based HDAC6 selective inhibitor with potent oral anti-inflammatory activity by attenuating NLRP3 inflammasome activation","volume":"65","author":"Yue","year":"2022","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib36","doi-asserted-by":"crossref","DOI":"10.1021\/acs.jmedchem.4c02883","article-title":"Development of hydrazide-based HDAC6 selective inhibitors for treating NLRP3 inflammasome-related diseases","author":"Yue","year":"2025","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib37","doi-asserted-by":"crossref","first-page":"4426","DOI":"10.1021\/acs.jmedchem.4c02373","article-title":"Exploring alternative zinc-binding groups in histone deacetylase (HDAC) inhibitors uncovers DS-103 as a potent Ethylhydrazide-Based HDAC inhibitor with chemosensitizing properties","volume":"68","author":"Stopper","year":"2025","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib38","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1021\/acsmedchemlett.5c00033","article-title":"Development of ethyl-hydrazide-based selective histone deacetylase 6 (HDAC6) PROTACs","volume":"16","author":"Stopper","year":"2025","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2025.117785_bib39","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0169-409X(00)00129-0","article-title":"Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings","volume":"46","author":"Lipinski","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ejmech.2025.117785_bib40","doi-asserted-by":"crossref","first-page":"2615","DOI":"10.1021\/jm020017n","article-title":"Molecular properties that influence the oral bioavailability of drug candidates","volume":"45","author":"Veber","year":"2002","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib41","doi-asserted-by":"crossref","DOI":"10.1016\/j.lfs.2022.120946","article-title":"Current trends in development of HDAC-Based chemotherapeutics","volume":"308","author":"Cheshmazar","year":"2022","journal-title":"Life Sci."},{"key":"10.1016\/j.ejmech.2025.117785_bib42","doi-asserted-by":"crossref","first-page":"2751","DOI":"10.3390\/ph3092751","article-title":"Clinical toxicities of histone deacetylase inhibitors","volume":"3","author":"Subramanian","year":"2010","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ejmech.2025.117785_bib43","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2020.105274","article-title":"HDAC6 as privileged target in drug discovery: a perspective","volume":"163","author":"Pulya","year":"2021","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.ejmech.2025.117785_bib44","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.2025.117785_bib45","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1007\/s00280-009-0991-z","article-title":"Hydroxyurea and hydroxamic acid derivatives as antitumor drugs","volume":"64","author":"Saban","year":"2009","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.ejmech.2025.117785_bib46","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.chembiol.2014.12.015","article-title":"Identification of histone deacetylase inhibitors with benzoylhydrazide scaffold that selectively inhibit class I histone deacetylases","volume":"22","author":"Wang","year":"2015","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ejmech.2025.117785_bib47","doi-asserted-by":"crossref","first-page":"9942","DOI":"10.1021\/acs.jmedchem.6b01385","article-title":"Development of allosteric hydrazide-containing class I histone deacetylase inhibitors for use in acute myeloid leukemia","volume":"59","author":"McClure","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib48","doi-asserted-by":"crossref","first-page":"5501","DOI":"10.1021\/acs.jmedchem.0c00442","article-title":"Design of hydrazide-bearing HDACIs based on panobinostat and their p53 and FLT3-ITD dependency in antileukemia activity","volume":"63","author":"Li","year":"2020","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib49","doi-asserted-by":"crossref","first-page":"3584","DOI":"10.1158\/1078-0432.CCR-21-0238","article-title":"Preclinical development and first-in-human study of KA2507, a selective and potent inhibitor of histone deacetylase 6, for patients with refractory solid tumors","volume":"27","author":"Tsimberidou","year":"2021","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.ejmech.2025.117785_bib50","doi-asserted-by":"crossref","first-page":"17796","DOI":"10.1021\/acs.jmedchem.4c01817","article-title":"Hydrazide-based class I selective HDAC inhibitors completely reverse chemoresistance synergistically in platinum-resistant solid cancer cells","volume":"67","author":"Kraft","year":"2024","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2025.117785_bib51","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.ejmech.2018.02.011","article-title":"Design, synthesis, and biological evaluation of novel amide and hydrazide based thioether analogs targeting histone deacteylase (HDAC) enzymes","volume":"148","author":"Farag","year":"2018","journal-title":"Eur. J. Med. Chem."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523425005501?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523425005501?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,6,6]],"date-time":"2025-06-06T20:27:34Z","timestamp":1749241654000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523425005501"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10]]},"references-count":51,"alternative-id":["S0223523425005501"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.117785","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2025,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Design, synthesis, and biological evaluation of indazole-based 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.2025.117785","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Masson SAS. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"117785"}}