Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases-Reference-Cited by-同舟云学术

Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases

Published:2020 Issue:20 Volume:56 Page:3039-3042
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Al Temimi Abbas H. K.¹²³⁴^ORCID,White Paul B.¹²³⁴^ORCID,Mulders Marcus J. M.⁵⁶⁴,van der Linden Nicole G. A.¹²³⁴,Blaauw Richard H.⁷⁶⁴,Wegert Anita⁵⁶⁴,Rutjes Floris P. J. T.¹²³⁴^ORCID,Mecinović Jasmin¹²³⁴⁸^ORCID

Affiliation:

1. Institute for Molecules and Materials

2. Radboud University

3. 6525 AJ Nijmegen

4. The Netherlands

5. Mercachem B.V.

6. 6546 BB Nijmegen

7. Chiralix B.V.

8. University of Southern Denmark

Abstract

Histone lysine methyltransferases (KMTs) exhibit substrate specificity for lysine and its geometrically constrained mimics.

Funder

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

H2020 European Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2020/CC/C9CC09098C

Reference22 articles.

1. Chromatin Modifications and Their Function

2. Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact

3. The diverse functions of histone lysine methylation

4. Molecular mechanisms and potential functions of histone demethylases

5. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

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