The DOI matches its Crossref record; 186 of the 186 references it cites were found in a registry or an index.
Nonhistone protein acetylation as cancer therapy targets
Open accessAbstract
Acetylation and deacetylation are counteracting, post-translational modifications that affect a large number of histone and nonhistone proteins. The significance of histone acetylation in the modification of chromatin structure and dynamics, and thereby gene transcription regulation, has been well recognized. A steadily growing number of nonhistone proteins have been identified as acetylation targets and reversible lysine acetylation in these proteins plays an important role(s) in the regulation of mRNA stability, protein localization and degradation, and protein-protein and protein-DNA interactions. The recruitment of histone acetyltransferases (HATs) and histone deacetylases (HDACs) to the transcriptional machinery is a key element in the dynamic regulation of genes controlling cellular proliferation, differentiation and apoptosis. Many nonhistone proteins targeted by acetylation are the products of oncogenes or tumor-suppressor genes and are directly involved in tumorigenesis, tumor progression and metastasis. Aberrant activity of HDACs has been documented in several types of cancers and HDAC inhibitors (HDACi) have been employed for therapeutic purposes. Here we review the published literature in this field and provide updated information on the regulation and function of nonhistone protein acetylation. While concentrating on the molecular mechanism and pathways involved in the addition and removal of the acetyl moiety, therapeutic modalities of HDACi are also discussed.
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1 retracted
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RetractedLysine acetylation targets protein complexes and co-regulates major cellular functions
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Histone deacetylases (HDACs): characterization of the classical HDAC family
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Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
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ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,639
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
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HDAC6 is a microtubule-associated deacetylase
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Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
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Singh, B. N., Shankar, S., & Srivastava, R. K. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.093 · Cited by 1,602
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Critical roles of non-histone protein lysine methylation in human tumorigenesis
Hamamoto, R., Saloura, V., & Nakamura, Y. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3884 · Cited by 376
Use of Epigenetic Drugs in Disease: An Overview
Heerboth, S., Lapinska, K., Snyder, N., Leary, M., Rollinson, S., & Sarkar, S. (2014) · Genetics & Epigenetics · doi:10.4137/geg.s12270 · Cited by 326
Cracking the Estrogen Receptor's Posttranslational Code in Breast Tumors
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Metadata
- Authors
- Singh, B. N., Zhang, G., Hwa, Y. L., Li, J., Dowdy, S. C., & Jiang, S.-W.
- Venue
- Expert Review of Anticancer Therapy
- Publisher
- Informa UK Limited
- Published
- 2010-06
- Volume
- 10
- Issue
- 6
- Pages
- 935-954
- ISSN
- 1473-7140 (ISSN-L)
- 1744-8328
- OpenAlex
- W2164453551
- Cited by
- 300
- References
- 186
- FWCI
- 5.20
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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