Literature DB >> 24691964

Erasers of histone acetylation: the histone deacetylase enzymes.

Edward Seto1, Minoru Yoshida.   

Abstract

Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD(+)-dependent mechanisms to deacetylate acetyl lysine substrates. Although removal of histone acetyl epigenetic modification by HDACs regulates chromatin structure and transcription, deacetylation of nonhistones controls diverse cellular processes. HDAC inhibitors are already known potential anticancer agents and show promise for the treatment of many diseases.

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Year:  2014        PMID: 24691964      PMCID: PMC3970420          DOI: 10.1101/cshperspect.a018713

Source DB:  PubMed          Journal:  Cold Spring Harb Perspect Biol        ISSN: 1943-0264            Impact factor:   10.005


  121 in total

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Journal:  BMC Med Genomics       Date:  2009-11-30       Impact factor: 3.063

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  483 in total

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Journal:  Plant Cell       Date:  2017-08-04       Impact factor: 11.277

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6.  Inhibition of histone deacetylase 7 reverses concentrative nucleoside transporter 2 repression in colorectal cancer by up-regulating histone acetylation state.

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9.  HDAC8 inhibition ameliorates pulmonary fibrosis.

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