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Erasers of histone acetylation: the histone deacetylase enzymes.
- Source :
-
Cold Spring Harbor perspectives in biology [Cold Spring Harb Perspect Biol] 2014 Apr 01; Vol. 6 (4), pp. a018713. Date of Electronic Publication: 2014 Apr 01. - Publication Year :
- 2014
-
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.
- Subjects :
- Arginase chemistry
Arginase classification
Arginase physiology
Gene Expression Regulation
Histone Deacetylase Inhibitors chemistry
Histone Deacetylase Inhibitors metabolism
Histone Deacetylases chemistry
Histone Deacetylases classification
Histones chemistry
Histones metabolism
Humans
Models, Biological
Protein Processing, Post-Translational
Protein Structure, Tertiary
Saccharomyces cerevisiae enzymology
Sirtuins antagonists & inhibitors
Sirtuins chemistry
Substrate Specificity
Histone Deacetylases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1943-0264
- Volume :
- 6
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Cold Spring Harbor perspectives in biology
- Publication Type :
- Academic Journal
- Accession number :
- 24691964
- Full Text :
- https://doi.org/10.1101/cshperspect.a018713