{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T17:34:21Z","timestamp":1786988061173,"version":"build-2736575974"},"reference-count":32,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,2,1]],"date-time":"2019-02-01T00:00:00Z","timestamp":1548979200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,2,1]],"date-time":"2019-02-01T00:00:00Z","timestamp":1548979200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100003668","name":"Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry and Fisheries","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003668","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002701","name":"Ministry of Education","doi-asserted-by":"publisher","award":["2016R1D1A1B01009559"],"award-info":[{"award-number":["2016R1D1A1B01009559"]}],"id":[{"id":"10.13039\/501100002701","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002701","name":"Ministry of Education","doi-asserted-by":"publisher","award":["NRF-2016R1A6A1A03011325"],"award-info":[{"award-number":["NRF-2016R1A6A1A03011325"]}],"id":[{"id":"10.13039\/501100002701","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003624","name":"Ministry of Agriculture, Food and Rural Affairs","doi-asserted-by":"publisher","award":["116102-03"],"award-info":[{"award-number":["116102-03"]}],"id":[{"id":"10.13039\/501100003624","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":[[2019,2]]},"DOI":"10.1016\/j.ejmech.2018.12.056","type":"journal-article","created":{"date-parts":[[2018,12,24]],"date-time":"2018-12-24T11:43:37Z","timestamp":1545651817000},"page":"263-272","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":45,"special_numbering":"C","title":["A novel class of anthraquinone-based HDAC6 inhibitors"],"prefix":"10.1016","volume":"164","author":[{"given":"Yoojin","family":"Song","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiah","family":"Lim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2268-8761","authenticated-orcid":false,"given":"Young Ho","family":"Seo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2018.12.056_bib1","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1016\/j.bbapap.2016.06.007","article-title":"The world of protein acetylation","volume":"1864","author":"Drazic","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2018.12.056_bib2","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/417455a","article-title":"HDAC6 is a microtubule-associated deacetylase","volume":"417","author":"Hubbert","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2018.12.056_bib3","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.2018.12.056_bib4","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.2018.12.056_bib5","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.2018.12.056_bib6","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ncomms1255","article-title":"The acetylation of tau inhibits its function and promotes pathological tau aggregation","volume":"2","author":"Cohen","year":"2011","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2018.12.056_bib7","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/s13024-017-0164-1","article-title":"Increased acetylation of Peroxiredoxin 1 by HDAC6 inhibition leads to recovery of Abeta-induced impaired axonal transport","volume":"12","author":"Choi","year":"2017","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.ejmech.2018.12.056_bib8","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1257037","article-title":"Influenza A virus uses the aggresome processing machinery for host cell entry","volume":"346","author":"Banerjee","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2018.12.056_bib9","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S1074-7613(04)00078-0","article-title":"HDAC6 deacetylase activity links the tubulin cytoskeleton with immune synapse organization","volume":"20","author":"Serrador","year":"2004","journal-title":"Immunity"},{"key":"10.1016\/j.ejmech.2018.12.056_bib10","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0092-8674(03)00939-5","article-title":"The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress","volume":"115","author":"Kawaguchi","year":"2003","journal-title":"Cell"},{"key":"10.1016\/j.ejmech.2018.12.056_bib11","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1021\/acs.orglett.8b01118","article-title":"Multicomponent synthesis and binding mode of imidazo[1,2- a]pyridine-capped selective HDAC6 inhibitors","volume":"20","author":"Mackwitz","year":"2018","journal-title":"Org. Lett."},{"key":"10.1016\/j.ejmech.2018.12.056_bib12","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.2018.12.056_bib13","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.2018.12.056_bib14","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.2018.12.056_bib15","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.2018.12.056_bib16","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.2018.12.056_bib17","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.2018.12.056_bib18","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1089\/dna.2013.2300","article-title":"Interplay between HDAC6 and its interacting partners: essential roles in the aggresome-autophagy pathway and neurodegenerative diseases","volume":"33","author":"Yan","year":"2014","journal-title":"DNA Cell Biol."},{"key":"10.1016\/j.ejmech.2018.12.056_bib19","doi-asserted-by":"crossref","first-page":"e1006799","DOI":"10.1371\/journal.ppat.1006799","article-title":"HDAC6 controls innate immune and autophagy responses to TLR-mediated signalling by the intracellular bacteria Listeria monocytogenes","volume":"13","author":"Moreno-Gonzalo","year":"2017","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ejmech.2018.12.056_bib20","doi-asserted-by":"crossref","first-page":"3454","DOI":"10.1021\/acs.jmedchem.7b01593","article-title":"Marbostat-100 defines a new class of potent and selective antiinflammatory and antirheumatic histone deacetylase 6 inhibitors","volume":"61","author":"Sellmer","year":"2018","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib21","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1038\/nrd2681","article-title":"Therapeutic application of histone deacetylase inhibitors for central nervous system disorders","volume":"7","author":"Kazantsev","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2018.12.056_bib22","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.pharmthera.2016.04.005","article-title":"Diverse roles of HDAC6 in viral infection: implications for antiviral therapy","volume":"164","author":"Zhang","year":"2016","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.ejmech.2018.12.056_bib23","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.ejmech.2017.12.061","article-title":"Development of novel beta-carboline-based hydroxamate derivatives as HDAC inhibitors with antiproliferative and antimetastatic activities in human cancer cells","volume":"144","author":"Ling","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib24","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.ejmech.2017.03.069","article-title":"Selective HDAC inhibitors with potent oral activity against leukemia and colorectal cancer: design, structure-activity relationship and anti-tumor activity study","volume":"134","author":"Li","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib25","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.ejmech.2017.03.079","article-title":"4-Indolyl-N-hydroxyphenylacrylamides as potent HDAC class I and IIB inhibitors in\u00a0vitro and in\u00a0vivo","volume":"134","author":"Mehndiratta","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib26","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1021\/acs.jmedchem.7b01404","article-title":"(N-Hydroxycarbonylbenylamino)Quinolines as selective histone deacetylase 6 inhibitors suppress growth of multiple myeloma in\u00a0vitro and in\u00a0vivo","volume":"61","author":"Lee","year":"2018","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib27","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1080\/14756366.2017.1417274","article-title":"Zinc binding groups for histone deacetylase inhibitors","volume":"33","author":"Zhang","year":"2018","journal-title":"J.\u00a0Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib28","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":"Expert Opin. Investig. Drugs"},{"key":"10.1016\/j.ejmech.2018.12.056_bib29","doi-asserted-by":"crossref","first-page":"2324","DOI":"10.1021\/acs.jcim.5b00559","article-title":"ZINC 15--ligand discovery for everyone","volume":"55","author":"Sterling","year":"2015","journal-title":"J.\u00a0Chem. Inf. Model."},{"key":"10.1016\/j.ejmech.2018.12.056_bib30","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.2018.12.056_bib31","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.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2018.12.056_bib32","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."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523418311024?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523418311024?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T13:49:31Z","timestamp":1759326571000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523418311024"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,2]]},"references-count":32,"alternative-id":["S0223523418311024"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2018.12.056","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2019,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A novel class of anthraquinone-based 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.2018.12.056","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}