Hydroxamic Acid-Modified Peptide Library Provides Insights into the Molecular Basis for the Substrate Selectivity of HDAC Corepressor Complexes-Reference-Cited by-同舟云学术

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Hydroxamic Acid-Modified Peptide Library Provides Insights into the Molecular Basis for the Substrate Selectivity of HDAC Corepressor Complexes

Published:2022-08-16 Issue:9 Volume:17 Page:2572-2582
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Archibald Lewis J.¹,Brown Edward A.²,Millard Christopher J.²,Watson Peter J.²,Robertson Naomi S.³,Wang Siyu²,Schwabe John W. R.²,Jamieson Andrew G.¹^ORCID

Affiliation:

1. School of Chemistry, Advanced Research Centre, University of Glasgow, Glasgow G11 6EW, U.K.

2. The Leicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, U.K.

3. Department of Chemistry, University of Cambridge, Cambridge CB2 1GA, U.K.

Funder

Engineering and Physical Sciences Research Council

Wellcome Trust

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.2c00510

Reference29 articles.

1. REREa/Atrophin-2 interacts with histone deacetylase and Fgf8 signaling to regulate multiple processes of zebrafish development

2. Differential HDAC1 and 2 Recruitment by Members of the MIER Family

3. Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3

4. NURD, a Novel Complex with Both ATP-Dependent Chromatin-Remodeling and Histone Deacetylase Activities

5. The MiDAC histone deacetylase complex is essential for embryonic development and has a unique multivalent structure

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