{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T14:00:08Z","timestamp":1793887208260,"version":"4.8.0"},"reference-count":136,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100013076","name":"National Major Science and Technology Projects of China","doi-asserted-by":"publisher","award":["2018ZX09711002-002-009"],"award-info":[{"award-number":["2018ZX09711002-002-009"]}],"id":[{"id":"10.13039\/501100013076","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81703358"],"award-info":[{"award-number":["81703358"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003399","name":"Science and Technology Commission of Shanghai Municipality","doi-asserted-by":"publisher","award":["17431903900"],"award-info":[{"award-number":["17431903900"]}],"id":[{"id":"10.13039\/501100003399","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003399","name":"Science and Technology Commission of Shanghai Municipality","doi-asserted-by":"publisher","award":["21S11908000"],"award-info":[{"award-number":["21S11908000"]}],"id":[{"id":"10.13039\/501100003399","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003399","name":"Science and Technology Commission of Shanghai Municipality","doi-asserted-by":"publisher","award":["18QB1404200"],"award-info":[{"award-number":["18QB1404200"]}],"id":[{"id":"10.13039\/501100003399","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003399","name":"Science and Technology Commission of Shanghai Municipality","doi-asserted-by":"publisher","award":["22ZR1460300"],"award-info":[{"award-number":["22ZR1460300"]}],"id":[{"id":"10.13039\/501100003399","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":[[2023,10]]},"DOI":"10.1016\/j.ejmech.2023.115613","type":"journal-article","created":{"date-parts":[[2023,6,29]],"date-time":"2023-06-29T11:52:58Z","timestamp":1688039578000},"page":"115613","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":32,"special_numbering":"C","title":["Perspectives and new aspects of histone deacetylase inhibitors in the therapy of CNS diseases"],"prefix":"10.1016","volume":"258","author":[{"given":"Bo","family":"Han","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mengfei","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiayi","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiushi","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Niubing","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuezhi","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2008-1755","authenticated-orcid":false,"given":"Qingwei","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2023.115613_bib1","doi-asserted-by":"crossref","DOI":"10.1016\/j.biomaterials.2020.120492","article-title":"Advances in nanomedicines for diagnosis of central nervous system disorders","volume":"269","author":"Zhang","year":"2021","journal-title":"Biomaterials"},{"issue":"6","key":"10.1016\/j.ejmech.2023.115613_bib2","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1038\/nrn.2017.46","article-title":"The emerging field of epigenetics in neurodegeneration and neuroprotection","volume":"18","author":"Hwang","year":"2017","journal-title":"Nat. Rev. Neurosci."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib3","doi-asserted-by":"crossref","first-page":"181","DOI":"10.2217\/nmt-2018-0004","article-title":"Role of epigenetics in Alzheimer's disease pathogenesis","volume":"8","author":"Stoccoro","year":"2018","journal-title":"Neurodegener. Dis. Manag."},{"issue":"10","key":"10.1016\/j.ejmech.2023.115613_bib4","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1038\/s41594-019-0309-8","article-title":"Bromodomain biology and drug discovery","volume":"26","author":"Zaware","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib5","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/nrg.2017.80","article-title":"The DNA methyltransferase family: a versatile toolkit for epigenetic regulation","volume":"19","author":"Lyko","year":"2018","journal-title":"Nat. Rev. Genet."},{"issue":"6","key":"10.1016\/j.ejmech.2023.115613_bib6","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1111\/odi.12569","article-title":"Epigenetic gene regulation by histone demethylases: emerging role in oncogenesis and inflammation","volume":"23","author":"Kang","year":"2017","journal-title":"Oral Dis."},{"key":"10.1016\/j.ejmech.2023.115613_bib7","doi-asserted-by":"crossref","DOI":"10.1016\/j.pharmthera.2022.108190","article-title":"HDACs and the epigenetic plasticity of cancer cells: target the complexity","volume":"238","author":"Brancolini","year":"2022","journal-title":"Pharmacol. Ther."},{"issue":"12","key":"10.1016\/j.ejmech.2023.115613_bib8","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1080\/15592294.2019.1640546","article-title":"Epidrugs: targeting epigenetic marks in cancer treatment","volume":"14","author":"Miranda Furtado","year":"2019","journal-title":"Epigenetics"},{"issue":"13","key":"10.1016\/j.ejmech.2023.115613_bib9","doi-asserted-by":"crossref","first-page":"4878","DOI":"10.3390\/ijerph17134878","article-title":"Epigenetic basis of lead-induced neurological disorders","volume":"17","author":"Wang","year":"2020","journal-title":"Int. J. Environ. Res. Publ. Health"},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib10","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1007\/s12016-022-08956-8","article-title":"Epigenetic dysregulation in autoimmune and inflammatory skin diseases","volume":"63","author":"Gibson","year":"2022","journal-title":"Clin. Rev. Allergy Immunol."},{"issue":"7","key":"10.1016\/j.ejmech.2023.115613_bib11","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1161\/CIRCRESAHA.118.312497","article-title":"Epigenetic modifications in cardiovascular aging and diseases","volume":"123","author":"Zhang","year":"2018","journal-title":"Circ. Res."},{"issue":"12","key":"10.1016\/j.ejmech.2023.115613_bib12","doi-asserted-by":"crossref","first-page":"1789","DOI":"10.1039\/C4MD00350K","article-title":"Discovery of an orally active subtype-selective HDAC inhibitor, chidamide, as an epigenetic modulator for cancer treatment","volume":"5","author":"Pan","year":"2014","journal-title":"MedChemComm"},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib13","doi-asserted-by":"crossref","first-page":"12","DOI":"10.3390\/cells10010012","article-title":"HDAC6 in diseases of cognition and of neurons","volume":"10","author":"Lopresti","year":"2020","journal-title":"Cells"},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib14","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1186\/s13045-018-0654-9","article-title":"Histone deacetylase 6 in cancer","volume":"11","author":"Li","year":"2018","journal-title":"J. Hematol. Oncol."},{"key":"10.1016\/j.ejmech.2023.115613_bib15","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.mcn.2017.11.007","article-title":"Epigenetic crosstalk: pharmacological inhibition of HDACs can rescue defective synaptic morphology and neurotransmission phenotypes associated with loss of the chromatin reader Kismet","volume":"87","author":"Latcheva","year":"2018","journal-title":"Mol. Cell. Neurosci."},{"key":"10.1016\/j.ejmech.2023.115613_bib16","doi-asserted-by":"crossref","DOI":"10.1155\/2011\/143269","article-title":"Targeting HDACs: a promising therapy for Alzheimer's disease","volume":"2011","author":"Xu","year":"2011","journal-title":"Oxid. Med. Cell. Longev."},{"issue":"8","key":"10.1016\/j.ejmech.2023.115613_bib17","doi-asserted-by":"crossref","first-page":"2873","DOI":"10.1128\/MCB.25.8.2873-2884.2005","article-title":"Class II histone deacetylases: from sequence to function, regulation, and clinical implication","volume":"25","author":"Yang","year":"2005","journal-title":"Mol. Cell Biol."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib18","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.neulet.2009.10.037","article-title":"HDAC inhibitor trichostatin A-inhibited survival of dopaminergic neuronal cells","volume":"467","author":"Wang","year":"2009","journal-title":"Neurosci. Lett."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib19","doi-asserted-by":"crossref","first-page":"6082","DOI":"10.1038\/s41598-017-05125-2","article-title":"A selective inhibitor of histone deacetylase 3 prevents cognitive deficits and suppresses striatal CAG repeat expansions in Huntington's disease mice","volume":"7","author":"Suelves","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2023.115613_bib20","article-title":"Tubastatin A, an HDAC6 inhibitor, alleviates stroke-induced brain infarction and functional deficits: potential roles of alpha-tubulin acetylation and FGF-21 up-regulation","volume":"6","author":"Wang","year":"2016","journal-title":"Sci. Rep."},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib21","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/sj.cdd.4401769","article-title":"HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis","volume":"13","author":"Saha","year":"2006","journal-title":"Cell Death Differ."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib22","first-page":"41","article-title":"Remodeling chromatin and stress resistance in the central nervous system: histone deacetylase inhibitors as novel and broadly effective neuroprotective agents","volume":"4","author":"Langley","year":"2005","journal-title":"Curr. Drug Targets: CNS Neurol. Disord."},{"issue":"Pt 3","key":"10.1016\/j.ejmech.2023.115613_bib23","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1042\/bj20021321","article-title":"Histone deacetylases (HDACs): characterization of the classical HDAC family","volume":"370","author":"De Ruijter","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2023.115613_bib24","doi-asserted-by":"crossref","first-page":"63","DOI":"10.4103\/abr.abr_142_19","article-title":"Histone deacetylases and histone deacetylase inhibitors: molecular mechanisms of action in various cancers","volume":"8","author":"Sanaei","year":"2019","journal-title":"Adv. Biomed. Res."},{"key":"10.1016\/j.ejmech.2023.115613_bib25","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2021.779177","article-title":"SIRT1: a potential therapeutic target in autoimmune diseases","volume":"12","author":"Shen","year":"2021","journal-title":"Front. Immunol."},{"issue":"13","key":"10.1016\/j.ejmech.2023.115613_bib26","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.2174\/1389557516666160620095103","article-title":"Small molecules as SIRT modulators","volume":"18","author":"Bai","year":"2018","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib27","doi-asserted-by":"crossref","DOI":"10.1155\/2020\/6782872","article-title":"The beneficial roles of SIRT1 in neuroinflammation-related diseases","volume":"2020","author":"Jiao","year":"2020","journal-title":"Oxid. Med. Cell. Longev."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib28","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/BF02686117","article-title":"Distribution of histone deacetylases 1-11 in the rat brain","volume":"31","author":"Broide","year":"2007","journal-title":"J. Mol. Neurosci."},{"issue":"13","key":"10.1016\/j.ejmech.2023.115613_bib29","doi-asserted-by":"crossref","first-page":"3153","DOI":"10.3390\/ijms20133153","article-title":"The role of SIRT1 on DNA damage response and epigenetic alterations in cancer","volume":"20","author":"Alves-Fernandes","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"21","key":"10.1016\/j.ejmech.2023.115613_bib30","doi-asserted-by":"crossref","first-page":"2051","DOI":"10.1161\/CIRCULATIONAHA.117.028728","article-title":"SIRT2 acts as a cardioprotective deacetylase in pathological cardiac hypertrophy","volume":"136","author":"Tang","year":"2017","journal-title":"Circulation"},{"issue":"6265","key":"10.1016\/j.ejmech.2023.115613_bib31","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.aac4854","article-title":"NAD(+) in aging, metabolism, and neurodegeneration","volume":"350","author":"Verdin","year":"2015","journal-title":"Science"},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib32","doi-asserted-by":"crossref","first-page":"158","DOI":"10.2174\/1570159X19666210609160017","article-title":"Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective","volume":"20","author":"Kumar","year":"2022","journal-title":"Curr. Neuropharmacol."},{"issue":"19","key":"10.1016\/j.ejmech.2023.115613_bib33","doi-asserted-by":"crossref","first-page":"7751","DOI":"10.1073\/pnas.0903139106","article-title":"Genetic dissection of histone deacetylase requirement in tumor cells","volume":"106","author":"Haberland","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"7243","key":"10.1016\/j.ejmech.2023.115613_bib34","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/nature07925","article-title":"HDAC2 negatively regulates memory formation and synaptic plasticity","volume":"459","author":"Guan","year":"2009","journal-title":"Nature"},{"issue":"7","key":"10.1016\/j.ejmech.2023.115613_bib35","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.tips.2015.04.013","article-title":"HDAC8: a multifaceted target for therapeutic interventions","volume":"36","author":"Chakrabarti","year":"2015","journal-title":"Trends Pharmacol. Sci."},{"issue":"6","key":"10.1016\/j.ejmech.2023.115613_bib36","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/j.neuron.2004.06.002","article-title":"CBP histone acetyltransferase activity is a critical component of memory consolidation","volume":"42","author":"Korzus","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.ejmech.2023.115613_bib37","doi-asserted-by":"crossref","first-page":"42","DOI":"10.3389\/fncel.2015.00042","article-title":"HDAC4 as a potential therapeutic target in neurodegenerative diseases: a summary of recent achievements","volume":"9","author":"Mielcarek","year":"2015","journal-title":"Front. Cell. Neurosci."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib38","doi-asserted-by":"crossref","first-page":"35","DOI":"10.3233\/JAD-2012-121009","article-title":"Loss of HDAC5 impairs memory function: implications for Alzheimer's disease","volume":"33","author":"Agis-Balboa","year":"2013","journal-title":"J Alzheimers Dis"},{"issue":"10","key":"10.1016\/j.ejmech.2023.115613_bib39","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1128\/MCB.01516-07","article-title":"Histone deacetylase inhibitor depsipeptide activates silenced genes through decreasing both CpG and H3K9 methylation on the promoter","volume":"28","author":"Wu","year":"2008","journal-title":"Mol. Cell Biol."},{"issue":"19","key":"10.1016\/j.ejmech.2023.115613_bib40","doi-asserted-by":"crossref","first-page":"10572","DOI":"10.1073\/pnas.191375098","article-title":"Cloning and characterization of a histone deacetylase, HDAC9","volume":"98","author":"Zhou","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"5","key":"10.1016\/j.ejmech.2023.115613_bib41","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1093\/nar\/30.5.1114","article-title":"Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain","volume":"30","author":"Tong","year":"2002","journal-title":"Nucleic Acids Res."},{"issue":"12","key":"10.1016\/j.ejmech.2023.115613_bib42","doi-asserted-by":"crossref","first-page":"2369","DOI":"10.1038\/sj.emboj.7600244","article-title":"Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase","volume":"23","author":"Yeung","year":"2004","journal-title":"EMBO J."},{"issue":"1\u20133","key":"10.1016\/j.ejmech.2023.115613_bib43","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/S0014-5793(03)01444-3","article-title":"Predominant expression of Sir2alpha, an NAD-dependent histone deacetylase, in the embryonic mouse heart and brain","volume":"556","author":"Sakamoto","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ejmech.2023.115613_bib44","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.expneurol.2013.01.024","article-title":"Modeling dyskinesia in animal models of Parkinson disease","volume":"256","author":"Morin","year":"2014","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.ejmech.2023.115613_bib45","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.neuint.2017.04.012","article-title":"SIRT3 and mitochondrial metabolism in neurodegenerative diseases","volume":"109","author":"Salvatori","year":"2017","journal-title":"Neurochem. Int."},{"issue":"5","key":"10.1016\/j.ejmech.2023.115613_bib46","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1111\/jnc.12942","article-title":"Loss of SIRT4 decreases GLT-1-dependent glutamate uptake and increases sensitivity to kainic acid","volume":"131","author":"Shih","year":"2014","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ejmech.2023.115613_bib47","doi-asserted-by":"crossref","first-page":"171","DOI":"10.3389\/fncel.2016.00171","article-title":"SIRT5 deficiency enhances susceptibility to kainate-induced seizures and exacerbates hippocampal neurodegeneration not through mitochondrial antioxidant enzyme SOD2","volume":"10","author":"Li","year":"2016","journal-title":"Front. Cell. Neurosci."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib48","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1016\/j.jmb.2008.07.048","article-title":"Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5","volume":"382","author":"Schlicker","year":"2008","journal-title":"J. Mol. Biol."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib49","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.tibs.2010.07.009","article-title":"Chromatin regulation and genome maintenance by mammalian SIRT6","volume":"36","author":"Tennen","year":"2011","journal-title":"Trends Biochem. Sci."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib50","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1074\/mcp.M113.031682","article-title":"A human proteome microarray identifies that the heterogeneous nuclear ribonucleoprotein K (hnRNP K) recognizes the 5' terminal sequence of the hepatitis C virus RNA","volume":"13","author":"Fan","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.ejmech.2023.115613_bib51","series-title":"Regulation of Immune Responses by Histone Deacetylase Inhibitors","author":"Licciardi","year":"2012"},{"key":"10.1016\/j.ejmech.2023.115613_bib52","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113383","article-title":"Design, synthesis and biological evaluation of brain penetrant benzazepine-based histone deacetylase 6 inhibitors for alleviating stroke-induced brain infarction","volume":"218","author":"Guo","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib53","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.bioorg.2016.05.005","article-title":"Inhibitors of histone deacetylase as antitumor agents: a critical review","volume":"67","author":"Manal","year":"2016","journal-title":"Bioorg. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib54","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/35106079","article-title":"Histone deacetylases and cancer: causes and therapies","volume":"1","author":"Marks","year":"2001","journal-title":"Nat. Rev. Cancer"},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib55","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.ccr.2012.09.003","article-title":"Coordinated silencing of MYC-mediated miR-29 by HDAC3 and EZH2 as a therapeutic target of histone modification in aggressive B-Cell lymphomas","volume":"22","author":"Zhang","year":"2012","journal-title":"Cancer Cell"},{"issue":"13","key":"10.1016\/j.ejmech.2023.115613_bib56","doi-asserted-by":"crossref","first-page":"2630","DOI":"10.1182\/blood-2009-09-243147","article-title":"microRNA expression profile and identification of miR-29 as a prognostic marker and pathogenetic factor by targeting CDK6 in mantle cell lymphoma","volume":"115","author":"Zhao","year":"2010","journal-title":"Blood"},{"issue":"10","key":"10.1016\/j.ejmech.2023.115613_bib57","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1093\/neuonc\/noaa103","article-title":"Increased activation of HDAC1\/2\/6 and Sp1 underlies therapeutic resistance and tumor growth in glioblastoma","volume":"22","author":"Yang","year":"2020","journal-title":"Neuro Oncol."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib58","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/s13046-022-02257-w","article-title":"HDAC6 involves in regulating the lncRNA-microRNA-mRNA network to promote the proliferation of glioblastoma cells","volume":"41","author":"Wu","year":"2022","journal-title":"J. Exp. Clin. Cancer Res."},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib59","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/jnc.14849","article-title":"Histone deacetylase 6 promotes growth of glioblastoma through the MKK7\/JNK\/c-Jun signaling pathway","volume":"152","author":"Huang","year":"2020","journal-title":"J. Neurochem."},{"issue":"12","key":"10.1016\/j.ejmech.2023.115613_bib60","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1517\/13543784.2011.629604","article-title":"Belinostat: clinical applications in solid tumors and lymphoma","volume":"20","author":"Molife","year":"2011","journal-title":"Expet Opin. Invest. Drugs"},{"key":"10.1016\/j.ejmech.2023.115613_bib61","doi-asserted-by":"crossref","first-page":"347","DOI":"10.2147\/OTT.S93528","article-title":"Chidamide in the treatment of peripheral T-cell lymphoma","volume":"10","author":"Chan","year":"2017","journal-title":"OncoTargets Ther."},{"issue":"8","key":"10.1016\/j.ejmech.2023.115613_bib62","first-page":"859","article-title":"The discovery and development of romidepsin for the treatment of T-cell lymphoma","volume":"12","author":"Smolewski","year":"2017","journal-title":"Expet Opin. Drug Discov."},{"issue":"6","key":"10.1016\/j.ejmech.2023.115613_bib63","doi-asserted-by":"crossref","first-page":"477","DOI":"10.2217\/fon-2016-0329","article-title":"Panobinostat for the management of multiple myeloma","volume":"13","author":"Sivaraj","year":"2017","journal-title":"Future Oncol."},{"issue":"13","key":"10.1016\/j.ejmech.2023.115613_bib64","first-page":"7412","article-title":"Vorinostat as potential antiparasitic drug","volume":"24","author":"Herrera-Martinez","year":"2020","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib65","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1111\/cbdd.12554","article-title":"Synthesis, biological evaluation, and computer-aided drug designing of new derivatives of hyperactive suberoylanilide hydroxamic acid histone deacetylase inhibitors","volume":"86","author":"Zhang","year":"2015","journal-title":"Chem. Biol. Drug Des."},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib66","doi-asserted-by":"crossref","first-page":"123","DOI":"10.2174\/1381612823666171114165051","article-title":"Curcumin: a natural pan-HDAC inhibitor in cancer","volume":"24","author":"Soflaei","year":"2018","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.ejmech.2023.115613_bib67","first-page":"448","article-title":"In vitro and in vivo anticancer studies of 2'-hydroxy chalcone derivatives exhibit apoptosis in colon cancer cells by HDAC inhibition and cell cycle arrest","volume":"16","author":"Pande","year":"2017","journal-title":"EXCLI J"},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib68","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.bbamcr.2014.11.004","article-title":"Resveratrol regulates PTEN\/Akt pathway through inhibition of MTA1\/HDAC unit of the NuRD complex in prostate cancer","volume":"1853","author":"Dhar","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2023.115613_bib69","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1186\/1471-2407-11-144","article-title":"Curcumin-induced HDAC inhibition and attenuation of medulloblastoma growth in vitro and in vivo","volume":"11","author":"Lee","year":"2011","journal-title":"BMC Cancer"},{"key":"10.1016\/j.ejmech.2023.115613_bib70","article-title":"A novel hydroxamic acid-based curcumin derivative as potent histone deacetylase inhibitor for the treatment of glioblastoma","volume":"11","author":"Wang","year":"2021","journal-title":"Front. Oncol."},{"issue":"11","key":"10.1016\/j.ejmech.2023.115613_bib71","doi-asserted-by":"crossref","first-page":"18577","DOI":"10.18632\/oncotarget.14612","article-title":"Advances in epigenetic glioblastoma therapy","volume":"8","author":"Lee","year":"2017","journal-title":"Oncotarget"},{"issue":"7","key":"10.1016\/j.ejmech.2023.115613_bib72","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1039\/C8MD00454D","article-title":"Design, synthesis and biological evaluation of beta-peptoid-capped HDAC inhibitors with anti-neuroblastoma and anti-glioblastoma activity","volume":"10","author":"Ressing","year":"2019","journal-title":"Medchemcomm"},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib73","doi-asserted-by":"crossref","first-page":"3193","DOI":"10.1021\/acs.jmedchem.1c01585","article-title":"Discovery of HDAC6-selective inhibitor NN-390 with in vitro efficacy in group 3 medulloblastoma","volume":"65","author":"Nawar","year":"2022","journal-title":"J. Med. Chem."},{"issue":"5","key":"10.1016\/j.ejmech.2023.115613_bib74","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1242\/dmm.030205","article-title":"Neurodegenerative disease: models, mechanisms, and a new hope","volume":"10","author":"Gitler","year":"2017","journal-title":"Dis Model Mech"},{"key":"10.1016\/j.ejmech.2023.115613_bib75","doi-asserted-by":"crossref","DOI":"10.1016\/j.brainres.2020.146692","article-title":"HDAC6 inhibitors: translating genetic and molecular insights into a therapy for axonal CMT","volume":"1733","author":"Rossaert","year":"2020","journal-title":"Brain Res."},{"issue":"7000","key":"10.1016\/j.ejmech.2023.115613_bib76","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/nature02621","article-title":"Pathways towards and away from Alzheimer's disease","volume":"430","author":"Mattson","year":"2004","journal-title":"Nature"},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib77","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1111\/nan.12518","article-title":"HDAC2 dysregulation in the nucleus basalis of Meynert during the progression of Alzheimer's disease","volume":"45","author":"Mahady","year":"2019","journal-title":"Neuropathol. Appl. Neurobiol."},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib78","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3233\/JAD-2012-120727","article-title":"The role of HDAC6 in Alzheimer's disease","volume":"33","author":"Zhang","year":"2013","journal-title":"J Alzheimers Dis"},{"issue":"17","key":"10.1016\/j.ejmech.2023.115613_bib79","doi-asserted-by":"crossref","first-page":"6775","DOI":"10.1021\/jm400564j","article-title":"Quinazolin-4-one derivatives as selective histone deacetylase-6 inhibitors for the treatment of Alzheimer's disease","volume":"56","author":"Yu","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib80","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113419","article-title":"Synthesis and biological evaluation of phenothiazine derivative-containing hydroxamic acids as potent class II histone deacetylase inhibitors","volume":"219","author":"Hsu","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib81","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112329","article-title":"Corrigendum to \"Design, synthesis, and evaluation of N-phenyl-4-(2-phenylsulfonamido)-benzamides as microtubule-targeting agents in drug-resistant cancer cells, displaying HDAC inhibitory response\"","volume":"196","author":"Wu","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib82","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.111950","article-title":"Novel 2, 5-diketopiperazine derivatives as potent selective histone deacetylase 6 inhibitors: rational design, synthesis and antiproliferative activity","volume":"187","author":"Chen","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib83","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2023.129148","article-title":"Discovery of indole-piperazine derivatives as selective histone deacetylase 6 inhibitors with neurite outgrowth-promoting activities and neuroprotective activities","volume":"81","author":"Liang","year":"2023","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"9996","key":"10.1016\/j.ejmech.2023.115613_bib84","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S0140-6736(14)61393-3","article-title":"Parkinson's disease","volume":"386","author":"Kalia","year":"2015","journal-title":"Lancet"},{"issue":"7","key":"10.1016\/j.ejmech.2023.115613_bib85","doi-asserted-by":"crossref","first-page":"3531","DOI":"10.1074\/jbc.M115.675488","article-title":"Regulation of histone acetylation by autophagy in Parkinson disease","volume":"291","author":"Park","year":"2016","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.ejmech.2023.115613_bib86","doi-asserted-by":"crossref","first-page":"6970","DOI":"10.1007\/s12035-016-0199-2","article-title":"Nuclear accumulation of histone deacetylase 4 (HDAC4) exerts neurotoxicity in models of Parkinson's disease","volume":"54","author":"Wu","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ejmech.2023.115613_bib87","article-title":"SIRT1 and SIRT2 activity control in neurodegenerative diseases","volume":"11","author":"Manjula","year":"2020","journal-title":"Front. Pharmacol."},{"issue":"5","key":"10.1016\/j.ejmech.2023.115613_bib88","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1016\/j.bmcl.2012.01.053","article-title":"Anti-tumor activity of new orally bioavailable 2-amino-5-(thiophen-2-yl)benzamide-series histone deacetylase inhibitors, possessing an aqueous soluble functional group as a surface recognition domain","volume":"22","author":"Hirata","year":"2012","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2023.115613_bib89","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.neurobiolaging.2015.10.001","article-title":"A novel histone deacetylase 1 and 2 isoform-specific inhibitor alleviates experimental Parkinson's disease","volume":"37","author":"Choong","year":"2016","journal-title":"Neurobiol. Aging"},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib90","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.102302","article-title":"Acetylation of NDUFV1 induced by a newly synthesized HDAC6 inhibitor HGC rescues dopaminergic neuron loss in Parkinson models","volume":"24","author":"Li","year":"2021","journal-title":"iScience"},{"issue":"18","key":"10.1016\/j.ejmech.2023.115613_bib91","doi-asserted-by":"crossref","first-page":"12445","DOI":"10.1021\/acs.jmedchem.2c01149","article-title":"Developing HDAC4-selective protein degraders to investigate the role of HDAC4 in huntington's disease pathology","volume":"65","author":"Macabuag","year":"2022","journal-title":"J. Med. Chem."},{"issue":"23","key":"10.1016\/j.ejmech.2023.115613_bib92","doi-asserted-by":"crossref","first-page":"3767","DOI":"10.1093\/hmg\/ddn273","article-title":"Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease","volume":"17","author":"Pallos","year":"2008","journal-title":"Hum. Mol. Genet."},{"issue":"43","key":"10.1016\/j.ejmech.2023.115613_bib93","doi-asserted-by":"crossref","first-page":"11174","DOI":"10.1523\/JNEUROSCI.3004-06.2006","article-title":"Mitochondrial-dependent Ca2+ handling in Huntington's disease striatal cells: effect of histone deacetylase inhibitors","volume":"26","author":"Oliveira","year":"2006","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ejmech.2023.115613_bib94","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.phrs.2015.08.002","article-title":"Transcriptional dysregulation in Huntington's disease: the role of histone deacetylases","volume":"100","author":"Sharma","year":"2015","journal-title":"Pharmacol. Res."},{"issue":"42","key":"10.1016\/j.ejmech.2023.115613_bib95","doi-asserted-by":"crossref","first-page":"35444","DOI":"10.1074\/jbc.M112.394544","article-title":"Histone deacetylase-1 (HDAC1) is a molecular switch between neuronal survival and death","volume":"287","author":"Bardai","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.ejmech.2023.115613_bib96","doi-asserted-by":"crossref","first-page":"839","DOI":"10.18632\/aging.100818","article-title":"Blocking the association of HDAC4 with MAP1S accelerates autophagy clearance of mutant Huntingtin","volume":"7","author":"Yue","year":"2015","journal-title":"Aging (Albany NY)"},{"issue":"24","key":"10.1016\/j.ejmech.2023.115613_bib97","doi-asserted-by":"crossref","first-page":"9934","DOI":"10.1021\/jm4011884","article-title":"Design, synthesis, and biological evaluation of potent and selective class IIa histone deacetylase (HDAC) inhibitors as a potential therapy for Huntington's disease","volume":"56","author":"Burli","year":"2013","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib98","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1021\/acsmedchemlett.0c00532","article-title":"Evaluation of 5-(Trifluoromethyl)-1,2,4-oxadiazole-Based class IIa HDAC inhibitors for huntington's disease","volume":"12","author":"Stott","year":"2021","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib99","first-page":"e2","article-title":"Heart disease and stroke statistics--2012 update: a report from the American Heart Association","volume":"125","author":"Roger","year":"2012","journal-title":"Circulation"},{"issue":"46","key":"10.1016\/j.ejmech.2023.115613_bib100","doi-asserted-by":"crossref","first-page":"19599","DOI":"10.1073\/pnas.0907935106","article-title":"HDAC6 is a target for protection and regeneration following injury in the nervous system","volume":"106","author":"Rivieccio","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"10.1016\/j.ejmech.2023.115613_bib101","doi-asserted-by":"crossref","first-page":"9188","DOI":"10.1007\/s12035-018-1058-0","article-title":"SIRT2 inhibition confers neuroprotection by downregulation of FOXO3a and MAPK signaling pathways in ischemic stroke","volume":"55","author":"She","year":"2018","journal-title":"Mol. Neurobiol."},{"issue":"31","key":"10.1016\/j.ejmech.2023.115613_bib102","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."},{"issue":"10","key":"10.1016\/j.ejmech.2023.115613_bib103","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."},{"issue":"10","key":"10.1016\/j.ejmech.2023.115613_bib104","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.tig.2017.07.008","article-title":"Multifarious functions of the fragile X mental retardation protein","volume":"33","author":"Davis","year":"2017","journal-title":"Trends Genet."},{"issue":"14","key":"10.1016\/j.ejmech.2023.115613_bib105","doi-asserted-by":"crossref","first-page":"3278","DOI":"10.1093\/nar\/gkf434","article-title":"Quantitative analysis of DNA demethylation and transcriptional reactivation of the FMR1 gene in fragile X cells treated with 5-azadeoxycytidine","volume":"30","author":"Pietrobono","year":"2002","journal-title":"Nucleic Acids Res."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib106","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1021\/acschemneuro.8b00600","article-title":"Brain penetrable histone deacetylase 6 inhibitor SW-100 ameliorates memory and learning impairments in a mouse model of fragile X syndrome","volume":"10","author":"Kozikowski","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2023.115613_bib107","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104109","article-title":"Design, synthesis and biological evaluation of dual-function inhibitors targeting NMDAR and HDAC for Alzheimer's disease","volume":"103","author":"He","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib108","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.ejmech.2018.03.005","article-title":"Design, synthesis, biological evaluation and in vivo testing of dual phosphodiesterase 5 (PDE5) and histone deacetylase 6 (HDAC6)-selective inhibitors for the treatment of Alzheimer's disease","volume":"150","author":"Rabal","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115613_bib109","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.114090","article-title":"Histone deacetylase 6 inhibitors with blood-brain barrier penetration as a potential strategy for CNS-Disorders therapy","volume":"229","author":"Gu","year":"2022","journal-title":"Eur. J. Med. Chem."},{"issue":"18","key":"10.1016\/j.ejmech.2023.115613_bib110","doi-asserted-by":"crossref","first-page":"13152","DOI":"10.1021\/acs.jmedchem.1c00910","article-title":"Strategies for structural modification of small molecules to improve blood-brain barrier penetration: a recent perspective","volume":"64","author":"Xiong","year":"2021","journal-title":"J. Med. Chem."},{"issue":"9","key":"10.1016\/j.ejmech.2023.115613_bib111","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1021\/jm301769u","article-title":"3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition","volume":"56","author":"Patil","year":"2013","journal-title":"J. Med. Chem."},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib112","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. Therapeut."},{"issue":"7","key":"10.1016\/j.ejmech.2023.115613_bib113","doi-asserted-by":"crossref","first-page":"1844","DOI":"10.1021\/acschembio.6b00012","article-title":"Inhibition of zinc-dependent histone deacetylases with a chemically triggered electrophile","volume":"11","author":"Boskovic","year":"2016","journal-title":"ACS Chem. Biol."},{"issue":"5","key":"10.1016\/j.ejmech.2023.115613_bib114","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nchembio.1223","article-title":"Selective class IIa histone deacetylase inhibition via a nonchelating zinc-binding group","volume":"9","author":"Lobera","year":"2013","journal-title":"Nat. Chem. Biol."},{"issue":"8","key":"10.1016\/j.ejmech.2023.115613_bib115","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1021\/ml400158k","article-title":"Tropolones as lead-like natural products: the development of potent and selective histone deacetylase inhibitors","volume":"4","author":"Ononye","year":"2013","journal-title":"ACS Med. Chem. Lett."},{"issue":"5","key":"10.1016\/j.ejmech.2023.115613_bib116","doi-asserted-by":"crossref","first-page":"408","DOI":"10.2174\/1568026621666211015092047","article-title":"Advances in the design and development of PROTAC-mediated HDAC degradation","volume":"22","author":"Rodrigues","year":"2022","journal-title":"Curr. Top. Med. Chem."},{"issue":"12","key":"10.1016\/j.ejmech.2023.115613_bib117","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1039\/D2MD00199C","article-title":"A 'click' chemistry approach to novel entinostat (MS-275) based class I histone deacetylase proteolysis targeting chimeras","volume":"13","author":"Cross","year":"2022","journal-title":"RSC Med Chem"},{"issue":"23","key":"10.1016\/j.ejmech.2023.115613_bib118","doi-asserted-by":"crossref","first-page":"7241","DOI":"10.3390\/molecules26237241","article-title":"Design, synthesis, and biological evaluation of HDAC degraders with CRBN E3 ligase ligands","volume":"26","author":"Lu","year":"2021","journal-title":"Molecules"},{"issue":"21","key":"10.1016\/j.ejmech.2023.115613_bib119","doi-asserted-by":"crossref","first-page":"4991","DOI":"10.3390\/molecules25214991","article-title":"Development of a bestatin-SAHA hybrid with dual inhibitory activity against APN and HDAC","volume":"25","author":"Cao","year":"2020","journal-title":"Molecules"},{"issue":"79","key":"10.1016\/j.ejmech.2023.115613_bib120","doi-asserted-by":"crossref","first-page":"11087","DOI":"10.1039\/D2CC03712B","article-title":"Development of the first non-hydroxamate selective HDAC6 degraders","volume":"58","author":"Keuler","year":"2022","journal-title":"Chem. Commun."},{"issue":"68","key":"10.1016\/j.ejmech.2023.115613_bib121","doi-asserted-by":"crossref","first-page":"9866","DOI":"10.1039\/D0CC03243C","article-title":"Discovery of histone deacetylase 3 (HDAC3)-specific PROTACs","volume":"56","author":"Xiao","year":"2020","journal-title":"Chem. Commun."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib122","doi-asserted-by":"crossref","DOI":"10.1016\/j.drudis.2022.103387","article-title":"Drug delivery challenges and formulation aspects of proteolysis targeting chimera (PROTACs)","volume":"28","author":"Saraswat","year":"2023","journal-title":"Drug Discov. Today"},{"issue":"7","key":"10.1016\/j.ejmech.2023.115613_bib123","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1016\/j.chembiol.2020.04.008","article-title":"A cell-based target engagement assay for the identification of cereblon E3 ubiquitin ligase ligands and their application in HDAC6 degraders","volume":"27","author":"Yang","year":"2020","journal-title":"Cell Chem. Biol."},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib124","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1021\/acsmedchemlett.0c00046","article-title":"Development of selective histone deacetylase 6 (HDAC6) degraders recruiting von hippel-lindau (VHL) E3 ubiquitin ligase","volume":"11","author":"Yang","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115613_bib125","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.ejmech.2018.01.063","article-title":"Discovery of a Keap1-dependent peptide PROTAC to knockdown Tau by ubiquitination-proteasome degradation pathway","volume":"146","author":"Lu","year":"2018","journal-title":"Eur. J. Med. Chem."},{"issue":"38","key":"10.1016\/j.ejmech.2023.115613_bib126","doi-asserted-by":"crossref","first-page":"11530","DOI":"10.1002\/anie.201706529","article-title":"Discovery of small molecules that induce the degradation of huntingtin","volume":"56","author":"Tomoshige","year":"2017","journal-title":"Angew Chem. Int. Ed. Engl."},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib127","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.nbd.2006.09.017","article-title":"Dorfin-CHIP chimeric proteins potently ubiquitylate and degrade familial ALS-related mutant SOD1 proteins and reduce their cellular toxicity","volume":"25","author":"Ishigaki","year":"2007","journal-title":"Neurobiol. Dis."},{"issue":"6","key":"10.1016\/j.ejmech.2023.115613_bib128","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/j.chembiol.2020.03.010","article-title":"Specific knockdown of alpha-synuclein by peptide-directed proteasome degradation rescued its associated neurotoxicity","volume":"27","author":"Qu","year":"2020","journal-title":"Cell Chem. Biol."},{"issue":"3","key":"10.1016\/j.ejmech.2023.115613_bib129","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1021\/acsmedchemlett.1c00500","article-title":"Conversion of a PROTAC mutant huntingtin degrader into small-molecule hydrophobic tags focusing on drug-like properties","volume":"13","author":"Hirai","year":"2022","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib130","first-page":"24","article-title":"PROTACs technology for treatment of Alzheimer's disease: advances and perspectives","volume":"1","author":"Inuzuka","year":"2022","journal-title":"Acta Mater Med"},{"issue":"2","key":"10.1016\/j.ejmech.2023.115613_bib131","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1038\/s41418-020-00696-6","article-title":"The role of E3 ubiquitin ligases in the development and progression of glioblastoma","volume":"28","author":"Humphreys","year":"2021","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.ejmech.2023.115613_bib132","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.jconrel.2017.08.033","article-title":"Advances in the design of solid lipid nanoparticles and nanostructured lipid carriers for targeting brain diseases","volume":"264","author":"Tapeinos","year":"2017","journal-title":"J. Contr. Release"},{"issue":"1","key":"10.1016\/j.ejmech.2023.115613_bib133","doi-asserted-by":"crossref","first-page":"22","DOI":"10.2174\/1381612823666170828133059","article-title":"Alzheimer's disease and Parkinson's disease: a review of current treatment adopting a nanotechnology approach","volume":"24","author":"Trompetero","year":"2018","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.ejmech.2023.115613_bib134","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.jconrel.2017.12.015","article-title":"Crossing the blood-brain barrier with nanoparticles","volume":"270","author":"Zhou","year":"2018","journal-title":"J. Contr. Release"},{"key":"10.1016\/j.ejmech.2023.115613_bib135","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.brainresbull.2018.10.009","article-title":"Evaluation of intranasal delivery route of drug administration for brain targeting","volume":"143","author":"Erdo","year":"2018","journal-title":"Brain Res. Bull."},{"issue":"4","key":"10.1016\/j.ejmech.2023.115613_bib136","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/nrd.2015.21","article-title":"From blood-brain barrier to blood-brain interface: new opportunities for CNS drug delivery","volume":"15","author":"Banks","year":"2016","journal-title":"Nat. Rev. Drug Discov."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423005792?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423005792?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T06:06:01Z","timestamp":1777529161000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523423005792"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10]]},"references-count":136,"alternative-id":["S0223523423005792"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115613","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2023,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Perspectives and new aspects of histone deacetylase inhibitors in the therapy of CNS diseases","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115613","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115613"}}