Histone Acetyltransferases

Article Properties
  • Language
    English
  • Publication Date
    2001/06/01
  • Indian UGC (Journal)
  • Refrences
    277
  • Citations
    1,339
  • Sharon Y. Roth Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, Texas 77030;Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201;Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908;
  • John M. Denu Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, Texas 77030;Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201;Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908;
  • C. David Allis Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, Texas 77030;Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201;Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908;
Abstract
Cite
Roth, Sharon Y., et al. “Histone Acetyltransferases”. Annual Review of Biochemistry, vol. 70, no. 1, 2001, pp. 81-120, https://doi.org/10.1146/annurev.biochem.70.1.81.
Roth, S. Y., Denu, J. M., & Allis, C. D. (2001). Histone Acetyltransferases. Annual Review of Biochemistry, 70(1), 81-120. https://doi.org/10.1146/annurev.biochem.70.1.81
Roth SY, Denu JM, Allis CD. Histone Acetyltransferases. Annual Review of Biochemistry. 2001;70(1):81-120.
Journal Categories
Science
Biology (General)
Science
Chemistry
Organic chemistry
Biochemistry
Description

How is gene expression regulated within the complex packaging of DNA? This review delves into the crucial role of histone acetyltransferases (HATs) in transcriptional regulation, exploring their mechanisms, regulation, and links to cellular processes. HATs are essential enzymes that modify histones, influencing gene accessibility and expression. The review discusses the discovery, substrate specificity, catalytic mechanism, and regulation of HATs. These enzymes are part of large, multisubunit complexes that target histones and other factors for acetylation, a modification positively linked to transcriptional activation. The involvement of HATs in cellular regulatory processes underlying normal development and differentiation, as well as abnormal processes leading to oncogenesis, are explored. While the functions and regulation of HATs are only beginning to be understood, this review underscores their far-reaching implications for human biology and disease. This provides a framework to better understand the connections to both cellular regulatory processes underlying normal development and differentiation, as well as abnormal processes that lead to oncogenesis.

Published in Annual Review of Biochemistry, this review on histone acetyltransferases aligns perfectly with the journal's focus on comprehensive overviews of key topics in biochemistry. By discussing the structure, function, and regulation of HATs, the paper contributes directly to the journal's existing body of research on chromatin modification, gene expression, and cellular regulation. Its scope and depth are consistent with the journal's mission.

Refrences
Citations
Citations Analysis
The first research to cite this article was titled The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4 and was published in 2001. The most recent citation comes from a 2024 study titled The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4 . This article reached its peak citation in 2007 , with 81 citations.It has been cited in 584 different journals, 18% of which are open access. Among related journals, the Journal of Biological Chemistry cited this research the most, with 72 citations. The chart below illustrates the annual citation trends for this article.
Citations used this article by year