{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,30]],"date-time":"2026-03-30T20:42:30Z","timestamp":1774903350028,"version":"3.50.1"},"reference-count":53,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,4,6]],"date-time":"2025-04-06T00:00:00Z","timestamp":1743897600000},"content-version":"am","delay-in-days":370,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100005300","name":"American Chemical Society","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005300","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM066706-20"],"award-info":[{"award-number":["GM066706-20"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic &amp; Medicinal Chemistry"],"published-print":{"date-parts":[[2024,4]]},"DOI":"10.1016\/j.bmc.2024.117680","type":"journal-article","created":{"date-parts":[[2024,3,16]],"date-time":"2024-03-16T03:11:24Z","timestamp":1710558684000},"page":"117680","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Histone deacetylase (HDAC) inhibitor specificity determinants are preserved in a class of dual HDAC\/non-covalent proteasome inhibitors"],"prefix":"10.1016","volume":"104","author":[{"given":"Alexandria M.","family":"Chan","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ashley","family":"Mitchell","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lena","family":"Grogan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul","family":"Shapiro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4429-8334","authenticated-orcid":false,"given":"Steven","family":"Fletcher","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bmc.2024.117680_b0005","doi-asserted-by":"crossref","first-page":"12","DOI":"10.2183\/pjab.85.12","article-title":"The proteasome: overview of structure and functions","volume":"85","author":"Tanaka","year":"2009","journal-title":"Proc Jpn Acad Ser B Phys Biol Sci"},{"key":"10.1016\/j.bmc.2024.117680_b0010","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s12079-011-0121-7","article-title":"PIs in cancer therapy","volume":"5","author":"Crawford","year":"2011","journal-title":"J Cell Commun Signal"},{"key":"#cr-split#-10.1016\/j.bmc.2024.117680_b0015.1","doi-asserted-by":"crossref","unstructured":"(a) Manasanch, E. E. and Orlowski, R. Z. Proteasome Inhibitors in Cancer Therapy. Nat. Rev. Clin. Oncol. 2017, 7, 417-433","DOI":"10.1038\/nrclinonc.2016.206"},{"key":"#cr-split#-10.1016\/j.bmc.2024.117680_b0015.2","doi-asserted-by":"crossref","unstructured":"Driessen, C. Proteasome Inhibition in Multiple Myeloma: Head-to-Head Comparison of Currently Available Proteasome Inhibitors. Cell Chem. Biol. 2019, 26, 340-351.","DOI":"10.1016\/j.chembiol.2018.11.007"},{"key":"#cr-split#-10.1016\/j.bmc.2024.117680_b0015.3","doi-asserted-by":"crossref","unstructured":"(a) Manasanch, E. E. and Orlowski, R. Z. Proteasome Inhibitors in Cancer Therapy. Nat. Rev. Clin. Oncol. 2017, 7, 417-433;","DOI":"10.1038\/nrclinonc.2016.206"},{"key":"#cr-split#-10.1016\/j.bmc.2024.117680_b0015.4","doi-asserted-by":"crossref","unstructured":"(3b) Besse, A.; Besse, L.; Kraus, M.; Mendez-Lopez, M.; Bader, J.; Xin, B.-T.; de Bruin, D.; Maurits, E.; Overkleeft, H. S.; Driessen, C. Proteasome Inhibition in Multiple Myeloma: Head-to-Head Comparison of Currently Available Proteasome Inhibitors. Cell Chem. Biol. 2019, 26, 340-351.","DOI":"10.1016\/j.chembiol.2018.11.007"},{"key":"10.1016\/j.bmc.2024.117680_b0020","doi-asserted-by":"crossref","unstructured":"a) Argyriou, A. A.; Iconomou, G.; Kalofonos, H. P. Bortezomib-induced peripheral neuropathy in multiple myeloma: a comprehensive review of the literature. Blood 2008, 112, 1593 - 1599; b) Kaplan, G. S.; Torcun, C. C.; Grune, T.; Ozer, N. K.; Karademir, B. PIs in Cancer Therapy: Treatment Regimen and Peripheral Neuropathy as a Side Effect. Free Radic. Biol. Med. 2017, 103, 1\u201313.","DOI":"10.1182\/blood-2008-04-149385"},{"key":"10.1016\/j.bmc.2024.117680_b0025","article-title":"Carfilzomib induced cardiotoxicity in a multiple myeloma patient","volume":"6","author":"Arnold M\u00e9ndez-Toro","year":"2020","journal-title":"Cardio-Oncology"},{"key":"10.1016\/j.bmc.2024.117680_b0030","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2016.12.007","article-title":"PIs in cancer therapy: treatment regimen and peripheral neuropathy as a side effect","volume":"103","author":"Kaplan","year":"2017","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.bmc.2024.117680_b0035","doi-asserted-by":"crossref","first-page":"11906","DOI":"10.1074\/jbc.M113.533950","article-title":"Discovery of PI-1840, a novel noncovalent and rapidly reversible PI with anti-tumor activity","volume":"289","author":"Kazi","year":"2014","journal-title":"J Biol Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0040","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/2050-7771-1-13","article-title":"The resistance mechanisms of PI bortezomib","volume":"1","author":"L\u00fc","year":"2013","journal-title":"Biomark Res"},{"key":"10.1016\/j.bmc.2024.117680_b0045","doi-asserted-by":"crossref","first-page":"2687","DOI":"10.1182\/blood-2014-03-564534","article-title":"A bim-Targeting strategy overcomes adaptive bortezomib resistance in myeloma through a novel link between autophagy and apoptosis","volume":"124","author":"Chen","year":"2014","journal-title":"Blood"},{"key":"10.1016\/j.bmc.2024.117680_b0050","doi-asserted-by":"crossref","first-page":"2034","DOI":"10.1158\/1535-7163.MCT-11-0433","article-title":"Mechanism of action of PIs and deacetylase inhibitors and the biological basis of synergy in multiple myeloma","volume":"10","author":"Hideshima","year":"2011","journal-title":"Mol Cancer Ther"},{"key":"10.1016\/j.bmc.2024.117680_b0055","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.ctrv.2018.09.001","article-title":"Drug resistance in multiple myeloma","volume":"70","author":"Robak","year":"2018","journal-title":"Cancer Treat Rev"},{"key":"10.1016\/j.bmc.2024.117680_b0060","article-title":"Novel PIs and histone deacetylase inhibitors: Progress in myeloma therapeutics","volume":"10","author":"Chhabra","year":"2017","journal-title":"Pharm Basel Switz"},{"key":"10.1016\/j.bmc.2024.117680_b0065","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.1158\/0008-5472.CAN-07-5989","article-title":"Role of the aggresome pathway in cancer: Targeting histone deacetylase 6\u2013Dependent protein degradation","volume":"68","author":"Rodriguez-Gonzalez","year":"2008","journal-title":"Cancer Res"},{"key":"10.1016\/j.bmc.2024.117680_b0070","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.ymgme.2008.03.012","article-title":"Targeting the aggresome pathway in hematologic malignancies","volume":"94","author":"Simms-Waldrip","year":"2008","journal-title":"Mol Genet Metab"},{"key":"10.1016\/j.bmc.2024.117680_b0075","doi-asserted-by":"crossref","first-page":"4577","DOI":"10.1111\/bcp.14889","article-title":"Recent developments of HDAC inhibitors: Emerging indications and novel molecules","volume":"87","author":"Bondarev","year":"2021","journal-title":"Br J Clin Pharmacol"},{"key":"10.1016\/j.bmc.2024.117680_b0080","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a026831","article-title":"HDACs and HDAC inhibitors in cancer development and therapy","volume":"6","author":"Li","year":"2016","journal-title":"Cold Spring Harb Perspect Med"},{"key":"10.1016\/j.bmc.2024.117680_b0085","doi-asserted-by":"crossref","first-page":"3660","DOI":"10.3390\/ijms23073660","article-title":"Histone deacetylase (HDAC) inhibitors: a promising weapon to tackle therapy resistance in melanoma","volume":"23","author":"Palamaris","year":"2022","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.bmc.2024.117680_b0090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.4068\/cmj.2016.52.1.1","article-title":"HDAC and HDAC inhibitor: from cancer to Cardiovascular diseases","volume":"52","author":"Yoon","year":"2016","journal-title":"Chonnam Med J"},{"key":"10.1016\/j.bmc.2024.117680_b0095","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":"PNAS"},{"key":"10.1016\/j.bmc.2024.117680_b0100","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1002\/cmdc.202000934","article-title":"Strategies to design selective histone deacetylase inhibitors","volume":"16","author":"Melesina","year":"2021","journal-title":"ChemMedChem"},{"key":"10.1016\/j.bmc.2024.117680_b0105","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1002\/ijc.32169","article-title":"Selective Pharmacological inhibitors of HDAC6 reveal biochemical activity but functional tolerance in cancer models","volume":"145","author":"Depetter","year":"2019","journal-title":"Int J Cancer"},{"key":"10.1016\/j.bmc.2024.117680_b0110","doi-asserted-by":"crossref","unstructured":"Chan, A. M.; Fletcher, S. Shifting the Paradigm in Treating Multi-Factorial Diseases: Polypharmacological Co-Inhibitors of HDAC6. RSC Med. Chem. 12 (2), 178\u2013196. https:\/\/doi.org\/10.1039\/d0md00286k.","DOI":"10.1039\/D0MD00286K"},{"key":"10.1016\/j.bmc.2024.117680_b0115","unstructured":"What Is Multiple Myeloma? https:\/\/www.cancer.org\/cancer\/multiple-myeloma\/about\/what-is-multiple-myeloma.html (accessed 2020-01-14)."},{"key":"10.1016\/j.bmc.2024.117680_b0120","unstructured":"Myeloma - Cancer Stat Facts. SEER. https:\/\/seer.cancer.gov\/statfacts\/html\/mulmy.html (accessed 2023-08-13)."},{"key":"10.1016\/j.bmc.2024.117680_b0125","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1111\/jcmm.12279","article-title":"PIs \u2013 Molecular basis and current perspectives in multiple myeloma","volume":"18","author":"Kubiczkova","year":"2014","journal-title":"J Cell Mol Med"},{"key":"10.1016\/j.bmc.2024.117680_b0130","doi-asserted-by":"crossref","first-page":"396","DOI":"10.3324\/haematol.2015.129189","article-title":"Treatment of relapsed and Refractory multiple myeloma","volume":"101","author":"Sonneveld","year":"2016","journal-title":"Haematologica"},{"key":"10.1016\/j.bmc.2024.117680_b0135","unstructured":"Current FDA-Approved Medications. International Myeloma Foundation. https:\/\/www.myeloma.org\/multiple-myeloma-drugs (accessed 2020-05-12)."},{"key":"10.1016\/j.bmc.2024.117680_b0140","doi-asserted-by":"crossref","first-page":"3307","DOI":"10.1158\/1078-0432.CCR-16-2526","article-title":"Ricolinostat, the first selective histone deacetylase 6 inhibitor, in combination with bortezomib and dexamethasone for relapsed or Refractory multiple myeloma","volume":"23","author":"Vogl","year":"2017","journal-title":"Clin Cancer Res off J Am Assoc Cancer Res"},{"key":"10.1016\/j.bmc.2024.117680_b0145","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1016\/S1470-2045(14)70440-1","article-title":"Panobinostat plus bortezomib and dexamethasone versus placebo plus bortezomib and dexamethasone in patients with relapsed or relapsed and Refractory multiple myeloma: a multicentre, randomised, double-blind phase 3 trial","volume":"15","author":"San-Miguel","year":"2014","journal-title":"Lancet Oncol"},{"key":"10.1016\/j.bmc.2024.117680_b0150","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1021\/acs.jmedchem.8b00760","article-title":"Polypharmacology by design: a medicinal chemist\u2019s perspective on Multitargeting compounds","volume":"62","author":"Proschak","year":"2019","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0155","doi-asserted-by":"crossref","first-page":"7874","DOI":"10.1021\/jm5006463","article-title":"Polypharmacology: challenges and opportunities in drug discovery","volume":"57","author":"Anighoro","year":"2014","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0160","doi-asserted-by":"crossref","first-page":"10299","DOI":"10.1021\/acs.jmedchem.8b01487","article-title":"Discovery of the first-in-class dual histone deacetylase-PI","volume":"61","author":"Bhatia","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0165","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1042\/BJ20100383","article-title":"Characterization of a new series of non-covalent PIs with exquisite potency and selectivity for the 20S \u03925-subunit","volume":"430","author":"Blackburn","year":"2010","journal-title":"Biochem J"},{"key":"10.1016\/j.bmc.2024.117680_b0170","doi-asserted-by":"crossref","first-page":"3508","DOI":"10.1021\/acs.jmedchem.0c01808","article-title":"The alpha keto amide moiety as a privileged motif in medicinal chemistry: current insights and Emerging opportunities","volume":"64","author":"Robello","year":"2021","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0175","doi-asserted-by":"crossref","first-page":"e202301077","DOI":"10.1002\/anie.202301077","article-title":"Lipophilicity modulations by fluorination Correlate with membrane Partitioning","volume":"62","author":"Wang","year":"2023","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.bmc.2024.117680_b0180","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1080\/14756360701425014","article-title":"The role of fluorine in medicinal chemistry: review article","volume":"22","author":"Shah","year":"2007","journal-title":"J Enzyme Inhib Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0185","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 Enzyme Inhib Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0190","doi-asserted-by":"crossref","first-page":"7698","DOI":"10.1021\/acs.jmedchem.3c00226","article-title":"The zinc-binding group effect: lessons from non-hydroxamic acid vorinostat analogs","volume":"66","author":"Geurs","year":"2023","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0195","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1021\/cb300549d","article-title":"New 26S PIs with high selectivity for chymotrypsin-like activity and P53-dependent cytotoxicity","volume":"8","author":"Neilsen","year":"2013","journal-title":"ACS Chem Biol"},{"key":"10.1016\/j.bmc.2024.117680_b0200","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.cellsig.2012.10.004","article-title":"Bortezomib\/PI triggers both apoptosis and autophagy-dependent pathways in melanoma cells","volume":"25","author":"Selimovic","year":"2013","journal-title":"Cell Signal"},{"key":"10.1016\/j.bmc.2024.117680_b0205","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1097\/CJI.0000000000000009","article-title":"A phase I trial of bortezomib and interferon alfa-2B in metastatic melanoma","volume":"37","author":"Markowitz","year":"1997","journal-title":"J Immunother Hagerstown Md"},{"key":"10.1016\/j.bmc.2024.117680_b0210","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1111\/exd.13089","article-title":"Inhibition of histone deacetylases in melanoma\u2014a perspective from bench to bedside","volume":"25","author":"Hornig","year":"2016","journal-title":"Exp Dermatol"},{"key":"10.1016\/j.bmc.2024.117680_b0215","doi-asserted-by":"crossref","first-page":"486","DOI":"10.3389\/fcell.2020.00486","article-title":"Histone deacetylase inhibitors to overcome resistance to Targeted and immuno therapy in metastatic melanoma","volume":"8","author":"Yeon","year":"2020","journal-title":"Front Cell Dev Biol"},{"key":"10.1016\/j.bmc.2024.117680_b0220","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.bmc.2024.117680_b0225","doi-asserted-by":"crossref","first-page":"5530","DOI":"10.1021\/jm0503749","article-title":"Structure-based optimization of phenylbutyrate-derived histone deacetylase inhibitors","volume":"48","author":"Lu","year":"2005","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0230","doi-asserted-by":"crossref","first-page":"3138","DOI":"10.1016\/j.bmcl.2010.03.092","article-title":"Benzimidazole and imidazole inhibitors of histone deacetylases: synthesis and biological activity","volume":"20","author":"Bressi","year":"2010","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.bmc.2024.117680_b0235","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.chempr.2021.12.001","article-title":"A \u201cuniversal\u201d catalyst for aerobic oxidations to synthesize (hetero)aromatic aldehydes, ketones, esters, acids, nitriles, and amides","volume":"8","author":"Senthamarai","year":"2022","journal-title":"Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0240","doi-asserted-by":"crossref","first-page":"2265","DOI":"10.1021\/jm800988r","article-title":"Design of Chimeric Histone Deacetylase- and Tyrosine Kinase-Inhibitors: a series of imatinib hybrides as potent inhibitors of wild-type and mutant BCR-ABL, PDGF-R\u03b2, and histone deacetylases","volume":"52","author":"Mahboobi","year":"2009","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2024.117680_b0245","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1021\/acsmedchemlett.7b00487","article-title":"Discovery of novel indoleamine 2,3-dioxygenase 1 (IDO1) and histone deacetylase (HDAC) dual inhibitors","volume":"9","author":"Fang","year":"2018","journal-title":"ACS Med Chem Lett"},{"key":"10.1016\/j.bmc.2024.117680_b9000","doi-asserted-by":"crossref","first-page":"6549","DOI":"10.1039\/C9NJ00885C","article-title":"tert-Butyl (3-cyano-4,6-dimethylpyridin-2-yl)carbonate as a green and chemoselective N-tert-butoxycarbonylation reagent","volume":"43","author":"Du","year":"2019","journal-title":"New J. Chem."}],"container-title":["Bioorganic &amp; Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089624000944?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089624000944?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T16:57:02Z","timestamp":1756745822000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089624000944"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4]]},"references-count":53,"alternative-id":["S0968089624000944"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2024.117680","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2024,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Histone deacetylase (HDAC) inhibitor specificity determinants are preserved in a class of dual HDAC\/non-covalent proteasome inhibitors","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2024.117680","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"117680"}}