Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling-Reference-Cited by-同舟云学术

Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling

Published:2019-01-09 Issue:1 Volume:10 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Longbotham James E.,Chio Cynthia M.,Dharmarajan Venkatasubramanian,Trnka Michael J.,Torres Idelisse Ortiz,Goswami Devrishi,Ruiz Karen,Burlingame Alma L.,Griffin Patrick R.^ORCID,Fujimori Danica Galonić

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-07829-z.pdf

Reference69 articles.

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3. Martin, C. & Zhang, Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838–849 (2005).

4. Mosammaparast, N. & Shi, Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu. Rev. Biochem. 79, 155–179 (2010).

5. Shi, Y. et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941–953 (2004).

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