Crystal Structure of the LSD1/CoREST Histone Demethylase Bound to Its Nucleosome Substrate-Reference-Cited by-同舟云学术

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Crystal Structure of the LSD1/CoREST Histone Demethylase Bound to Its Nucleosome Substrate

Published:2020-06 Issue:5 Volume:78 Page:903-914.e4
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Kim Sang-Ah,Zhu Jiang,Yennawar Neela,Eek Priit,Tan Song

Funder

Savannah River Operations Office, U.S. Department of Energy

National Institute of General Medical Sciences

Estonian Research Competency Council

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference52 articles.

1. Development and crystallographic evaluation of histone H3 peptide with N-terminal serine substitution as a potent inhibitor of lysine-specific demethylase 1;Amano;Bioorg. Med. Chem.,2017

2. Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution;Armache;Science,2011

3. Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation;Balasubramanian;J. Biol. Chem.,2002

4. LSD1/CoREST is an allosteric nanoscale clamp regulated by H3-histone-tail molecular recognition;Baron;Proc. Natl. Acad. Sci. USA,2012

5. ERRα protein is stabilized by LSD1 in a demethylation-independent manner;Carnesecchi;PLoS ONE,2017

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