Abstract
Histone deacetylases are able to catalyze the hydrolysis of N-acetyl lysine residues of histones which package chromosomal DNA. Therefore they play an important role in mediating gene expression and cell proliferation. HDAC inhibitors have not only shown promise as antiparasitic, antineurodegenerative, antirheumatologic agents and immunosuppressant, but as potent anticancer agents by inducing cell cycle arrest, differentiation and apoptosis. This review highlights recent development in design, synthesis and biological evaluation of HDAC inhibitors for cancer therapy.
Keywords: Antitumor drugs, cancer therapy, cyclic peptide, drug discovery, epigenetic regulation, histone deacetylase, hdac isoforms, histone deacetylase inhibitors, hybrid compounds, multi-targeted inhibitor.
Current Medicinal Chemistry
Title:Histone Deacetylase Inhibitors: An Attractive Strategy for Cancer Therapy
Volume: 20 Issue: 14
Author(s): Jiyang Li, Guangqiang Li and Wenqing Xu
Affiliation:
Keywords: Antitumor drugs, cancer therapy, cyclic peptide, drug discovery, epigenetic regulation, histone deacetylase, hdac isoforms, histone deacetylase inhibitors, hybrid compounds, multi-targeted inhibitor.
Abstract: Histone deacetylases are able to catalyze the hydrolysis of N-acetyl lysine residues of histones which package chromosomal DNA. Therefore they play an important role in mediating gene expression and cell proliferation. HDAC inhibitors have not only shown promise as antiparasitic, antineurodegenerative, antirheumatologic agents and immunosuppressant, but as potent anticancer agents by inducing cell cycle arrest, differentiation and apoptosis. This review highlights recent development in design, synthesis and biological evaluation of HDAC inhibitors for cancer therapy.
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Cite this article as:
Li Jiyang, Li Guangqiang and Xu Wenqing, Histone Deacetylase Inhibitors: An Attractive Strategy for Cancer Therapy, Current Medicinal Chemistry 2013; 20 (14) . https://dx.doi.org/10.2174/0929867311320140005
DOI https://dx.doi.org/10.2174/0929867311320140005 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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