{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T03:24:31Z","timestamp":1791948271563,"version":"4.3.4"},"reference-count":98,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2015,7,1]],"date-time":"2015-07-01T00:00:00Z","timestamp":1435708800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,5,12]],"date-time":"2015-05-12T00:00:00Z","timestamp":1431388800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["clinicalkey.jp","clinicalkey.com","cell.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Trends in Pharmacological Sciences"],"published-print":{"date-parts":[[2015,7]]},"DOI":"10.1016\/j.tips.2015.04.013","type":"journal-article","created":{"date-parts":[[2015,5,23]],"date-time":"2015-05-23T08:48:23Z","timestamp":1432370903000},"page":"481-492","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":278,"title":["HDAC8: a multifaceted target for therapeutic interventions"],"prefix":"10.1016","volume":"36","author":[{"given":"Alokta","family":"Chakrabarti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ina","family":"Oehme","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olaf","family":"Witt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guilherme","family":"Oliveira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang","family":"Sippl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Romier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raymond J.","family":"Pierce","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manfred","family":"Jung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tips.2015.04.013_bib0495","doi-asserted-by":"crossref","first-page":"a018713","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 Harb. Perspect. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0500","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/nrg2485","article-title":"The many roles of histone deacetylases in development and physiology: implications for disease and therapy","volume":"10","author":"Haberland","year":"2009","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.tips.2015.04.013_bib0505","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1042\/CS20120504","article-title":"Histone deacetylases as targets for treatment of multiple diseases","volume":"124","author":"Tang","year":"2013","journal-title":"Clin. Sci."},{"key":"10.1016\/j.tips.2015.04.013_bib0510","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrd4360","article-title":"Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders","volume":"13","author":"Falkenberg","year":"2014","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.tips.2015.04.013_bib0515","doi-asserted-by":"crossref","first-page":"3898","DOI":"10.3390\/molecules20033898","article-title":"Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents","volume":"20","author":"Mottamal","year":"2015","journal-title":"Molecules"},{"key":"10.1016\/j.tips.2015.04.013_bib0520","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1042\/bj3500199","article-title":"Cloning and characterization of a novel human histone deacetylase, HDAC8","volume":"350","author":"Buggy","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.tips.2015.04.013_bib0525","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0014-5793(00)01813-5","article-title":"Cloning and characterization of human histone deacetylase 8","volume":"478","author":"Van den Wyngaert","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.tips.2015.04.013_bib0530","doi-asserted-by":"crossref","first-page":"15254","DOI":"10.1074\/jbc.M908988199","article-title":"Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor","volume":"275","author":"Hu","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tips.2015.04.013_bib0535","doi-asserted-by":"crossref","first-page":"C288","DOI":"10.1152\/ajpcell.00102.2014","article-title":"Histone deacetylase 8 regulates cortactin deacetylation and contraction in smooth muscle tissues","volume":"307","author":"Li","year":"2014","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.tips.2015.04.013_bib0540","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.jmb.2004.02.006","article-title":"Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis","volume":"338","author":"Gregoretti","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0545","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1016\/j.str.2004.04.012","article-title":"Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases","volume":"12","author":"Somoza","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.tips.2015.04.013_bib0550","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1128\/MCB.24.2.765-773.2004","article-title":"Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A","volume":"24","author":"Lee","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0555","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1210\/me.2009-0441","article-title":"An acetylation switch modulates the transcriptional activity of estrogen-related receptor alpha","volume":"24","author":"Wilson","year":"2010","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.tips.2015.04.013_bib0560","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nature11316","article-title":"HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle","volume":"489","author":"Deardorff","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.tips.2015.04.013_bib0565","doi-asserted-by":"crossref","first-page":"2210","DOI":"10.1021\/cb500492r","article-title":"An unbiased approach to identify endogenous substrates of \u2018histone\u2019 deacetylase 8","volume":"9","author":"Olson","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0570","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1093\/hmg\/ddu002","article-title":"Loss-of-function HDAC8 mutations cause a phenotypic spectrum of Cornelia de Lange syndrome-like features, ocular hypertelorism, large fontanelle and X-linked inheritance","volume":"23","author":"Kaiser","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.tips.2015.04.013_bib0575","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1186\/s13046-014-0059-8","article-title":"Histone deacetylase 8 is deregulated in urothelial cancer but not a target for efficient treatment","volume":"33","author":"Lehmann","year":"2014","journal-title":"J. Exp. Clin. Cancer Res."},{"key":"10.1016\/j.tips.2015.04.013_bib0580","first-page":"1677","article-title":"Histone deacetylases 1, 6 and 8 are critical for invasion in breast cancer","volume":"25","author":"Park","year":"2011","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.tips.2015.04.013_bib0585","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1038\/onc.2012.81","article-title":"Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8","volume":"32","author":"Yan","year":"2013","journal-title":"Oncogene"},{"key":"10.1016\/j.tips.2015.04.013_bib0590","doi-asserted-by":"crossref","first-page":"e84015","DOI":"10.1371\/journal.pone.0084015","article-title":"DEC1 coordinates with HDAC8 to differentially regulate TAp73 and DeltaNp73 expression","volume":"9","author":"Qian","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1016\/j.tips.2015.04.013_bib0595","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1517\/14728220903241658","article-title":"Targeting of HDAC8 and investigational inhibitors in neuroblastoma","volume":"18","author":"Oehme","year":"2009","journal-title":"Expert Opin. Investig. Drugs"},{"key":"10.1016\/j.tips.2015.04.013_bib0600","doi-asserted-by":"crossref","first-page":"359","DOI":"10.2217\/cns.13.24","article-title":"Targeting of histone deacetylases in brain tumors","volume":"2","author":"Ecker","year":"2013","journal-title":"CNS Oncol."},{"key":"10.1016\/j.tips.2015.04.013_bib0605","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1038\/leu.2008.9","article-title":"A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas","volume":"22","author":"Balasubramanian","year":"2008","journal-title":"Leukemia"},{"key":"10.1016\/j.tips.2015.04.013_bib0610","doi-asserted-by":"crossref","first-page":"e1003645","DOI":"10.1371\/journal.ppat.1003645","article-title":"Structural basis for the inhibition of histone deacetylase 8 (HDAC8), a key epigenetic player in the blood fluke Schistosoma mansoni","volume":"9","author":"Marek","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.tips.2015.04.013_bib0615","doi-asserted-by":"crossref","first-page":"e1002316","DOI":"10.1371\/journal.ppat.1002316","article-title":"Histone deacetylase 8 is required for centrosome cohesion and influenza A virus entry","volume":"7","author":"Yamauchi","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.tips.2015.04.013_bib0620","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1021\/cb1003866","article-title":"NMR profiling of histone deacetylase and acetyl-transferase activities in real time","volume":"6","author":"Dose","year":"2011","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0625","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/nbt.3130","article-title":"Acetylation site specificities of lysine deacetylase inhibitors in human cells","volume":"33","author":"Scholz","year":"2015","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.tips.2015.04.013_bib0630","doi-asserted-by":"crossref","first-page":"4201","DOI":"10.1016\/j.bmc.2013.05.002","article-title":"Synthesis and biological evaluation of a targeted DNA-binding transcriptional activator with HDAC8 inhibitory activity","volume":"21","author":"Saha","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.tips.2015.04.013_bib0635","doi-asserted-by":"crossref","first-page":"10915","DOI":"10.1073\/pnas.89.22.10915","article-title":"Amino acid substitution matrices from protein blocks","volume":"89","author":"Henikoff","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tips.2015.04.013_bib0640","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1002\/bip.22135","article-title":"HDAC8 substrates: histones and beyond","volume":"99","author":"Wolfson","year":"2013","journal-title":"Biopolymers"},{"key":"10.1016\/j.tips.2015.04.013_bib0645","doi-asserted-by":"crossref","first-page":"3545","DOI":"10.1007\/s10620-013-2867-7","article-title":"The up-regulation of histone deacetylase 8 promotes proliferation and inhibits apoptosis in hepatocellular carcinoma","volume":"58","author":"Wu","year":"2013","journal-title":"Dig. Dis. Sci."},{"key":"10.1016\/j.tips.2015.04.013_bib0650","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1128\/MCB.23.2.607-619.2003","article-title":"The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain","volume":"23","author":"Durst","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0655","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbrc.2008.11.135","article-title":"Inactivation of CREB mediated gene transcription by HDAC8 bound protein phosphatase","volume":"379","author":"Gao","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.tips.2015.04.013_bib0660","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1101\/gad.1809209","article-title":"Epigenetic control of skull morphogenesis by histone deacetylase 8","volume":"23","author":"Haberland","year":"2009","journal-title":"Genes Dev."},{"key":"10.1016\/j.tips.2015.04.013_bib0665","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1002\/cbic.200900417","article-title":"Combining mass spectrometry and peptide arrays to profile the specificities of histone deacetylases","volume":"10","author":"Gurard-Levin","year":"2009","journal-title":"ChemBioChem"},{"key":"10.1016\/j.tips.2015.04.013_bib0670","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.tips.2015.04.013_bib0675","doi-asserted-by":"crossref","first-page":"6242","DOI":"10.1021\/bi800053v","article-title":"The activity of HDAC8 depends on local and distal sequences of its peptide substrates","volume":"47","author":"Gurard-Levin","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.tips.2015.04.013_bib0680","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1021\/cb100088g","article-title":"Peptide arrays identify isoform-selective substrates for profiling endogenous lysine deacetylase activity","volume":"5","author":"Gurard-Levin","year":"2010","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0685","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1038\/sj.embor.7401047","article-title":"Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex","volume":"8","author":"Vannini","year":"2007","journal-title":"EMBO Rep."},{"key":"10.1016\/j.tips.2015.04.013_bib0690","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.bbrc.2007.03.158","article-title":"Factors affecting the substrate specificity of histone deacetylases","volume":"357","author":"Riester","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.tips.2015.04.013_bib0695","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1016\/j.bbrc.2004.09.155","article-title":"Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates","volume":"324","author":"Riester","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.tips.2015.04.013_bib0700","doi-asserted-by":"crossref","first-page":"3005","DOI":"10.1021\/ci5004653","article-title":"Discovery of inhibitors of Schistosoma mansoni HDAC8 by combining homology modeling, virtual screening and in vitro validation","volume":"54","author":"Kannan","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.tips.2015.04.013_bib0705","first-page":"769","article-title":"Expression profile of class I histone deacetylases in human cancer tissues","volume":"18","author":"Nakagawa","year":"2007","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.tips.2015.04.013_bib0710","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1158\/1078-0432.CCR-08-0684","article-title":"Histone deacetylase 8 in neuroblastoma tumorigenesis","volume":"15","author":"Oehme","year":"2009","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.tips.2015.04.013_bib0715","doi-asserted-by":"crossref","first-page":"15064","DOI":"10.1073\/pnas.0404603101","article-title":"Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor","volume":"101","author":"Vannini","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tips.2015.04.013_bib0720","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/380711a0","article-title":"Defects in cardiac outflow tract formation and pro-B-lymphocyte expansion in mice lacking Sox-4","volume":"380","author":"Schilham","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.tips.2015.04.013_bib0725","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1242\/dev.042101","article-title":"Sequential requirement of Sox4 and Sox11 during development of the sympathetic nervous system","volume":"137","author":"Potzner","year":"2010","journal-title":"Development"},{"key":"10.1016\/j.tips.2015.04.013_bib0730","doi-asserted-by":"crossref","first-page":"3475","DOI":"10.1101\/gad.403406","article-title":"The establishment of neuronal properties is controlled by Sox4 and Sox11","volume":"20","author":"Bergsland","year":"2006","journal-title":"Genes Dev."},{"key":"10.1016\/j.tips.2015.04.013_bib0735","doi-asserted-by":"crossref","first-page":"3640","DOI":"10.1182\/blood-2012-07-441022","article-title":"SOX4 is a direct target gene of FRA-2 and induces expression of HDAC8 in adult T-cell leukemia\/lymphoma","volume":"121","author":"Higuchi","year":"2013","journal-title":"Blood"},{"key":"10.1016\/j.tips.2015.04.013_bib0740","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.tips.2015.04.013_bib0745","doi-asserted-by":"crossref","first-page":"e1657","DOI":"10.1038\/cddis.2015.24","article-title":"Selective inhibition of HDAC8 decreases neuroblastoma growth in vitro and in vivo and enhances retinoic acid-mediated differentiation","volume":"6","author":"Rettig","year":"2015","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.tips.2015.04.013_bib0750","doi-asserted-by":"crossref","first-page":"6018","DOI":"10.1093\/nar\/gkt346","article-title":"MYCN and HDAC2 cooperate to repress miR-183 signaling in neuroblastoma","volume":"41","author":"Lodrini","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.tips.2015.04.013_bib0755","doi-asserted-by":"crossref","first-page":"E2592","DOI":"10.1073\/pnas.1300113110","article-title":"Histone deacetylase 10 promotes autophagy-mediated cell survival","volume":"110","author":"Oehme","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tips.2015.04.013_bib0760","doi-asserted-by":"crossref","first-page":"436","DOI":"10.2174\/138161209787315774","article-title":"Targeting histone deacetylases in neuroblastoma","volume":"15","author":"Witt","year":"2009","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.tips.2015.04.013_bib0765","doi-asserted-by":"crossref","first-page":"5259","DOI":"10.1128\/MCB.01971-05","article-title":"Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation","volume":"26","author":"Lee","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0770","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0378-1119(00)00014-7","article-title":"Role of the transcription factor AML-1 in acute leukemia and hematopoietic differentiation","volume":"245","author":"Lutterbach","year":"2000","journal-title":"Gene"},{"key":"10.1016\/j.tips.2015.04.013_bib0775","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1093\/carcin\/bgt070","article-title":"Pure curcumin increases the expression of SOCS1 and SOCS3 in myeloproliferative neoplasms through suppressing class I histone deacetylases","volume":"34","author":"Chen","year":"2013","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.tips.2015.04.013_bib0780","doi-asserted-by":"crossref","DOI":"10.1016\/j.exphem.2012.10.012","article-title":"Histone deacetylases inhibitor sodium butyrate inhibits JAK2\/STAT signaling through upregulation of SOCS1 and SOCS3 mediated by HDAC8 inhibition in myeloproliferative neoplasms","volume":"41","author":"Gao","year":"2013","journal-title":"Exp. Hematol."},{"key":"10.1016\/j.tips.2015.04.013_bib0785","doi-asserted-by":"crossref","first-page":"e1476","DOI":"10.1038\/cddis.2014.422","article-title":"HDAC8 and STAT3 repress BMF gene activity in colon cancer cells","volume":"5","author":"Kang","year":"2014","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.tips.2015.04.013_bib0790","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1093\/carcin\/bgp147","article-title":"Alpha-keto acid metabolites of organoselenium compounds inhibit histone deacetylase activity in human colon cancer cells","volume":"30","author":"Nian","year":"2009","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.tips.2015.04.013_bib0795","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/S0140-6736(06)69440-3","article-title":"Human schistosomiasis","volume":"368","author":"Gryseels","year":"2006","journal-title":"Lancet"},{"key":"10.1016\/j.tips.2015.04.013_bib0800","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1086\/338574","article-title":"Triggering of innate immune responses by schistosome egg glycolipids and their carbohydrate epitope GalNAc beta 1-4(Fuc alpha 1-2Fuc alpha 1-3)GlcNAc","volume":"185","author":"Van der Kleij","year":"2002","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.tips.2015.04.013_bib0805","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1017\/S0031182009990400","article-title":"The Schistosomiasis Control Initiative (SCI): rationale, development and implementation from 2002\u20132008","volume":"136","author":"Fenwick","year":"2009","journal-title":"Parasitology"},{"key":"10.1016\/j.tips.2015.04.013_bib0810","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1097\/QCO.0b013e328318978f","article-title":"Praziquantel: mechanisms of action, resistance and new derivatives for schistosomiasis","volume":"21","author":"Doenhoff","year":"2008","journal-title":"Curr. Opin. Infect. Dis."},{"key":"10.1016\/j.tips.2015.04.013_bib0815","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1038\/nrd4091","article-title":"The epigenetics pipeline","volume":"12","author":"DeWoskin","year":"2013","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.tips.2015.04.013_bib0820","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.pt.2010.09.001","article-title":"Piggy-backing the concept of cancer drugs for schistosomiasis treatment: a tangible perspective?","volume":"27","author":"Dissous","year":"2011","journal-title":"Trends Parasitol."},{"key":"10.1016\/j.tips.2015.04.013_bib0825","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.molbiopara.2009.06.001","article-title":"Histone deacetylase inhibitors induce apoptosis, histone hyperacetylation and up-regulation of gene transcription in Schistosoma mansoni","volume":"168","author":"Dubois","year":"2009","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.tips.2015.04.013_bib0830","first-page":"3567","article-title":"Targeting schistosome histone modifying enzymes for drug development","volume":"18","author":"Pierce","year":"2012","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.tips.2015.04.013_bib0835","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1016\/j.bbrc.2008.10.090","article-title":"The class I histone deacetylases of the platyhelminth parasite Schistosoma mansoni","volume":"377","author":"Oger","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.tips.2015.04.013_bib0840","doi-asserted-by":"crossref","first-page":"e1001329","DOI":"10.1371\/journal.ppat.1001329","article-title":"Dissection of the influenza A virus endocytic routes reveals macropinocytosis as an alternative entry pathway","volume":"7","author":"de Vries","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.tips.2015.04.013_bib0845","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1002\/ajmg.1320470703","article-title":"de Lange syndrome: a clinical review of 310 individuals","volume":"47","author":"Jackson","year":"1993","journal-title":"Am. J. Med. Genet."},{"key":"10.1016\/j.tips.2015.04.013_bib0850","article-title":"Cornelia de Lange syndrome","author":"Boyle","year":"2014","journal-title":"Clin. Genet."},{"key":"10.1016\/j.tips.2015.04.013_bib0855","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1126\/science.1256917","article-title":"Closing the cohesin ring: structure and function of its Smc3-kleisin interface","volume":"346","author":"Gligoris","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.tips.2015.04.013_bib0860","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1021\/cb5003762","article-title":"Compromised structure and function of HDAC8 mutants identified in Cornelia de Lange Syndrome spectrum disorders","volume":"9","author":"Decroos","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0865","doi-asserted-by":"crossref","first-page":"2874","DOI":"10.1016\/j.bmcl.2007.02.064","article-title":"Design and evaluation of \u2018Linkerless\u2019 hydroxamic acids as selective HDAC8 inhibitors","volume":"17","author":"Krennhrubec","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tips.2015.04.013_bib0870","doi-asserted-by":"crossref","first-page":"4816","DOI":"10.1021\/jm400390r","article-title":"Discovery of the first histone deacetylase 6\/8 dual inhibitors","volume":"56","author":"Olson","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.tips.2015.04.013_bib0875","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.1016\/j.bmcl.2011.01.134","article-title":"Discovery of histone deacetylase 8 selective inhibitors","volume":"21","author":"Tang","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tips.2015.04.013_bib0880","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1002\/cmdc.201300414","article-title":"Design, synthesis, and biological activity of NCC149 derivatives as histone deacetylase 8-selective inhibitors","volume":"9","author":"Suzuki","year":"2014","journal-title":"ChemMedChem"},{"key":"10.1016\/j.tips.2015.04.013_bib0885","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1002\/cmdc.201200300","article-title":"Synthesis and biological evaluation of ortho-aryl N-hydroxycinnamides as potent histone deacetylase (HDAC) 8 isoform-selective inhibitors","volume":"7","author":"Huang","year":"2012","journal-title":"ChemMedChem"},{"key":"10.1016\/j.tips.2015.04.013_bib0890","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1002\/cmdc.200900309","article-title":"Azetidinones as zinc-binding groups to design selective HDAC8 inhibitors","volume":"4","author":"Galletti","year":"2009","journal-title":"ChemMedChem"},{"key":"10.1016\/j.tips.2015.04.013_bib0895","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1124\/jpet.103.055541","article-title":"Identification of novel isoform-selective inhibitors within class I histone deacetylases","volume":"307","author":"Hu","year":"2003","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.tips.2015.04.013_bib0900","doi-asserted-by":"crossref","first-page":"4626","DOI":"10.1016\/j.bmc.2011.06.030","article-title":"Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors","volume":"19","author":"Whitehead","year":"2011","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.tips.2015.04.013_bib0905","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/nbt.1759","article-title":"Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes","volume":"29","author":"Bantscheff","year":"2011","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.tips.2015.04.013_bib0910","doi-asserted-by":"crossref","DOI":"10.1016\/j.drudis.2015.01.004","article-title":"How the flexibility of human histone deacetylases influences ligand binding: an overview","author":"Deschamps","year":"2015","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.tips.2015.04.013_bib0915","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/978-3-642-21631-2_10","article-title":"Structural biology of human metal-dependent histone deacetylases","volume":"206","author":"Schapira","year":"2011","journal-title":"Handb. Exp. Pharmacol."},{"key":"10.1016\/j.tips.2015.04.013_bib0920","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1038\/icb.2011.97","article-title":"HDAC inhibitors in parasitic diseases","volume":"90","author":"Andrews","year":"2012","journal-title":"Immunol. Cell Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0925","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. Mol. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0930","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1038\/msb.2013.26","article-title":"The functional interactome landscape of the human histone deacetylase family","volume":"9","author":"Joshi","year":"2013","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0935","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/S0002-9440(10)63320-2","article-title":"Expression of histone deacetylase 8, a class I histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues","volume":"165","author":"Waltregny","year":"2004","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.tips.2015.04.013_bib0940","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1084\/jem.20082826","article-title":"Drug inhibition of HDAC3 and epigenetic control of differentiation in Apicomplexa parasites","volume":"206","author":"Bougdour","year":"2009","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.tips.2015.04.013_bib0945","doi-asserted-by":"crossref","first-page":"3666","DOI":"10.1128\/AAC.02721-13","article-title":"Lysine acetylation in sexual stage malaria parasites is a target for antimalarial small molecules","volume":"58","author":"Trenholme","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.tips.2015.04.013_bib0950","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2014.12.066","article-title":"Evaluation of histone deacetylase inhibitors (HDACi) as therapeutic leads for human African trypanosomiasis (HAT)","author":"Carrillo","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.tips.2015.04.013_bib0955","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/j.bmcl.2006.12.028","article-title":"Discovery of uracil-based histone deacetylase inhibitors able to reduce acquired antifungal resistance and trailing growth in Candida albicans","volume":"17","author":"Mai","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.tips.2015.04.013_bib0960","doi-asserted-by":"crossref","first-page":"3106","DOI":"10.1128\/MCB.26.8.3106-3113.2006","article-title":"Positive and negative regulation of the innate antiviral response and beta interferon gene expression by deacetylation","volume":"26","author":"Nusinzon","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.tips.2015.04.013_bib0965","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.4049\/jimmunol.1400420","article-title":"HDAC8-mediated epigenetic reprogramming plays a key role in resistance to anthrax lethal toxin-induced pyroptosis in macrophages","volume":"193","author":"Ha","year":"2014","journal-title":"J. Immunol."},{"key":"10.1016\/j.tips.2015.04.013_bib0970","doi-asserted-by":"crossref","first-page":"13554","DOI":"10.1021\/bi801610c","article-title":"Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors","volume":"47","author":"Dowling","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.tips.2015.04.013_bib0975","doi-asserted-by":"crossref","first-page":"5048","DOI":"10.1021\/bi1005046","article-title":"Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function","volume":"49","author":"Dowling","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.tips.2015.04.013_bib0980","doi-asserted-by":"crossref","first-page":"12474","DOI":"10.1021\/ja205972n","article-title":"Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases","volume":"133","author":"Cole","year":"2011","journal-title":"J. Am. Chem. Soc."}],"container-title":["Trends in Pharmacological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0165614715000899?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0165614715000899?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,22]],"date-time":"2018-09-22T06:27:28Z","timestamp":1537597648000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0165614715000899"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,7]]},"references-count":98,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2015,7]]}},"alternative-id":["S0165614715000899"],"URL":"https:\/\/doi.org\/10.1016\/j.tips.2015.04.013","relation":{},"ISSN":["0165-6147"],"issn-type":[{"value":"0165-6147","type":"print"}],"subject":[],"published":{"date-parts":[[2015,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"HDAC8: a multifaceted target for therapeutic interventions","name":"articletitle","label":"Article Title"},{"value":"Trends in Pharmacological Sciences","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.tips.2015.04.013","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}