Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control-Reference-Cited by-同舟云学术

Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control

Published:2020 Issue:36 Volume:11 Page:9950-9961
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Ramanan Rajeev¹²³⁴^ORCID,Chaturvedi Shobhit S.¹²³⁴^ORCID,Lehnert Nicolai¹⁵⁶⁴^ORCID,Schofield Christopher J.⁷⁸⁹^ORCID,Karabencheva-Christova Tatyana G.¹²³⁴^ORCID,Christov Christo Z.¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. Michigan Technological University

3. Houghton

4. USA

5. University of Michigan

6. Ann Arbor

7. The Chemistry Research Laboratory

8. University of Oxford

9. UK

Abstract

The second sphere residues and regions of the protein in histone demethylase enzymes that makes correlated motion with the active site contribute to efficient catalysis.

Funder

Michigan Technological University

Wellcome Trust

Cancer Research UK

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/SC/D0SC03713C

Reference74 articles.

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3. Targeting Histone Demethylases: A New Avenue for the Fight against Cancer

4. Histone Demethylation Mediated by the Nuclear Amine Oxidase Homolog LSD1

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