The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Regulation of histone deacetylase activities
Abstract
Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl groups from lysine residues in both histone and non‐histone proteins. They play a key role in the regulation of gene transcription and many other biological processes involving chromatin. Significantly, recent studies suggest that HDACs are critically involved in cell‐cycle regulation, cell proliferation, differentiation, and in the development of human cancer. HDAC inhibitors currently are being exploited as potential anti‐cancer agents. As expected for vital regulators of many cellular processes, the activities of HDACs are tightly controlled and precisely regulated by multiple mechanisms. The activities of most if not all HDACs are regulated by protein–protein interactions. In addition, many HDACs are regulated by post‐translational modifications as well as by subcellular localization. Less studied, but perhaps equally important, is the regulation of some HDACs by control of expression, availability of cofactors, and by proteolytic processing. A complete understanding of how HDACs are regulated will contribute not only to our overall knowledge of chromatin structure and gene control, but will offer tremendous insight into approaches for developing therapeutic HDAC inhibitors with improved specificity. © 2004 Wiley‐Liss, Inc.
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Cites
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · cited 1×
“It is important to note that the primary physiological substrate of HDAC6 and SIRT2 are the cytoplasmic a-tubulin protein and not histones [Hubbert et al., 2002; Matsuyama et al., 2002; North et al., 2003; Zhang et al., 2003].”
BackgroundHistone deacetylases and cancer: causes and therapies
Marks, P. A., Rifkind, R. A., Richon, V. M., Breslow, R., Miller, T., & Kelly, W. K. (2001) · Nature reviews. Cancer · doi:10.1038/35106079 · Cited by 1,866
Histone-deacetylase inhibitors: novel drugs for the treatment of cancer
Johnstone, R. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd772 · Cited by 1,515
Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y.-Z., Greenwald, M., et al. (2001) · Nature · doi:10.1038/35099568 · Cited by 1,228 · cited 1×
“Additionally, drugs that target HDACs potentially may be useful against malaria and toxoplasmosis, and for treatment of Huntington’s disease [Darkin-Rattray et al., 1996; Steffan et al., 2001].”
BackgroundZhang, Y., Ng, H.-H., Erdjument-Bromage, H., Tempst, P., Bird, A., & Reinberg, D. (1999) · Genes & Development · doi:10.1101/gad.13.15.1924 · Cited by 1,103
Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740 · cited 1×
“It is important to note that the primary physiological substrate of HDAC6 and SIRT2 are the cytoplasmic a-tubulin protein and not histones [Hubbert et al., 2002; Matsuyama et al., 2002; North et al., 2003; Zhang et al., 2003].”
BackgroundNicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736
In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation
Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf682 · Cited by 720
Cited by
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Yang, X.-J., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,230
Self-citationHDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C. (2007) · Cell Research · doi:10.1038/sj.cr.7310149 · Cited by 678
Sirtuins in aging and age-related disease
Longo, V. D., & Kennedy, B. K. (2006) · Cell · doi:10.1016/j.cell.2006.07.002 · Cited by 628
Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication
Yang, X.-J., & Grégoire, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.2873-2884.2005 · Cited by 419
Chemical mechanisms of histone lysine and arginine modifications
Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390
Metadata
- Authors
- Sengupta, N., & Seto, E.
- Venue
- Journal of Cellular Biochemistry
- Publisher
- Wiley
- Published
- 2004-07-20
- Volume
- 93
- Issue
- 1
- Pages
- 57-67
- ISSN
- 0730-2312 (ISSN-L)
- 1097-4644
- OpenAlex
- W2114063466
- Cited by
- 346
- References
- 24
- FWCI
- 7.33
- Type
- journal article
- Language
- en
- Open access
- closed
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