Histone deacetylases Journal Article


Authors: Marks, P. A.; Miller, T.; Richon, V. M.
Article Title: Histone deacetylases
Abstract: Post-translational modification of the histones of chromatin has a fundamental role in regulating gene expression. Enzymes involved in these epigenetic events include histone deacetylases (class I and class II), which can be inhibited by a structurally diverse group of small molecules. These histone deacetylase inhibitors induce growth arrest, differentiation and/or apoptosis of cancer cells in vitro and in vivo . Results of clinical trials with several of these agents have indicated that they are well tolerated at doses that have anti-tumour activity.
Keywords: vasculotropin; unclassified drug; histone deacetylase inhibitor; drug tolerability; review; cytotoxic agent; nonhuman; antineoplastic agents; neoplasms; animals; unindexed drug; apoptosis; enzyme inhibition; cell growth; in vivo study; cell differentiation; antineoplastic activity; drug structure; in vitro study; drug design; structure-activity relationship; gene expression regulation; gene expression regulation, neoplastic; protein processing; enzyme inhibitors; histone; chromatin; cancer cell; vorinostat; drug bioavailability; protein p21; histone deacetylases; hydroxamic acid; clinical trials; cyclopeptide; valproic acid; histone deacetylase; arylbutyric acid derivative; n (2 aminophenyl) 4 (3 pyridinylmethoxycarbonylaminomethyl)benzamide; pivaloyloxymethyl butyrate; 4 [n (2 hydroxyethyl) n [2 (3 indolyl)ethyl]aminomethyl]cinnamohydroxamic acid; 4 n acetyldinaline; trichostatin a; cinnamic acid derivative; depsipeptide; growth inhibition; benzamide derivative; ketone derivative; fr 901228; oxamflatin; aliphatic carboxylic acid; apicidin; tetrapeptide; humans; human; priority journal; benzamide; alpha ketoamide; sulfonamide hydroxamic acid; trifluoromethyl ketone
Journal Title: Current Opinion in Pharmacology
Volume: 3
Issue: 4
ISSN: 1471-4892
Publisher: Elsevier Inc.  
Date Published: 2003-08-01
Start Page: 344
End Page: 351
Language: English
DOI: 10.1016/s1471-4892(03)00084-5
PUBMED: 12901942
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 25 September 2014 -- Source: Scopus
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  1. Paul Marks
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