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Histone acetylation in chromatin structure and transcription

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  • Michael Grunstein

    (UCLA School of Medicine and the Molecular Biology Institute, University of California)

Abstract

The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle. These acetylation patterns may direct histone assembly and help regulate the unfolding and activity of genes.

Suggested Citation

  • Michael Grunstein, 1997. "Histone acetylation in chromatin structure and transcription," Nature, Nature, vol. 389(6649), pages 349-352, September.
  • Handle: RePEc:nat:nature:v:389:y:1997:i:6649:d:10.1038_38664
    DOI: 10.1038/38664
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    Cited by:

    1. Thomas B. Kepler & Timothy C. Elston, 2001. "Stochasticity in Transcriptional Regulation: Origins, Consequences and Mathematical Representations," Working Papers 01-06-033, Santa Fe Institute.
    2. Sung-Yeon Hwang & Hyewon Kim & Danielle Denisko & Boxun Zhao & Dohoon Lee & Jiseok Jeong & Jinuk Kim & Kiwon Park & Junhyun Park & Dongjoon Jeong & Sehong Park & Hee-Jung Choi & Sun Kim & Eunjung Alic, 2024. "Human cytomegalovirus harnesses host L1 retrotransposon for efficient replication," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Dustin C. Becht & Brianna J. Klein & Akinori Kanai & Suk Min Jang & Khan L. Cox & Bing-Rui Zhou & Sabrina K. Phanor & Yi Zhang & Ruo-Wen Chen & Christopher C. Ebmeier & Catherine Lachance & Maxime Gal, 2023. "MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix domain," Nature Communications, Nature, vol. 14(1), pages 1-20, December.
    4. Avinash B. Patel & Jinkang Qing & Kelly H. Tam & Sara Zaman & Maria Luiso & Ishwar Radhakrishnan & Yuan He, 2023. "Cryo-EM structure of the Saccharomyces cerevisiae Rpd3L histone deacetylase complex," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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