The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.
Histone modifying enzymes: Structures, mechanisms, and specificities
Open accessAbstract
Histone modifying enzymes catalyze the addition or removal of an array of covalent modifications in histones and non-histone proteins. Within the context of chromatin, these modifications regulate gene expression as well as other genomic functions and have been implicated in establishing and maintaining a heritable epigenetic code that contributes to defining cell identity and fate. Biochemical and structural characterization of histone modifying enzymes has yielded important insights into their respective catalytic mechanisms, substrate specificities, and regulation. In this review, we summarize recent advances in understanding these enzymes, highlighting studies of the histone acetyltransferases (HATs) p300 (also now known as KAT3B) and Rtt109 (KAT11) and the histone lysine demethylases (HDMs) LSD1 (KDM1) and JMJD2A (KDM4A), present overriding themes that derive from these studies, and pose remaining questions concerning their regulatory roles in mediating DNA transactions.
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Cites
Chromatin modifications and their function
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Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
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“Following the discovery of histone lysine methyltransferases in 2000 [16], there was significant debate concerning the permanence of lysine methyl marks in vivo and whether these modifications are enzymatically reversible by yet unidentified HDMs.”
BackgroundACETYLATION 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
Histone demethylation by a family of JmjC domain-containing proteins
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A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
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The CBP co-activator is a histone acetyltransferase
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LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
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Acetylation and deacetylation of non-histone proteins
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Cited by
Epigenetics: Definition, Mechanisms and Clinical Perspective
Dupont, C., Armant, D., & Brenner, C. (2009) · Seminars in Reproductive Medicine · doi:10.1055/s-0029-1237423 · Cited by 799
Epigenetics: a molecular link between environmental factors and type 2 diabetes
Ling, C., & Groop, L. (2009) · Diabetes · doi:10.2337/db09-1003 · Cited by 617
Nucleosome structure and function
McGinty, R. K., & Tan, S. (2015) · Chemical Reviews · doi:10.1021/cr500373h · Cited by 530
Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B., & Nachury, M. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013728107 · Cited by 472
Developmental origins of health and disease: current knowledge and potential mechanisms
Hoffman, D. J., Reynolds, R. M., & Hardy, D. B. (2017) · Nutrition Reviews · doi:10.1093/nutrit/nux053 · Cited by 355
Metadata
- Authors
- Marmorstein, R., & Trievel, R. C.
- Venue
- Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 1789
- Issue
- 1
- Pages
- 58-68
- ISSN
- 1874-9399 (ISSN-L)
- OpenAlex
- W2048958290
- Cited by
- 326
- References
- 105
- FWCI
- 7.20
- Type
- journal article
- Language
- en
- Open access
- green
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- Marmorstein, R., & Trievel, R. C. (2009). Histone modifying enzymes: Structures, mechanisms, and specificities. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. https://doi.org/10.1016/j.bbagrm.2008.07.009
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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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