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Small molecules as tools to study the chemical epigenetics of lysine acetylation

Abstract:

Lysine acetylation has emerged as a key post-translational modification found at many sites throughout the cell. It plays an important role in epigenetic processes, and more generally in the regulation of protein stability and interactions. Acetyl groups are installed by lysine acetyltransferases and removed by lysine deacetylases. Acetylated lysine residues function as binding sites for bromodomains, which are epigenetic reader protein modules that mediate protein–protein interactions. Progr...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.cbpa.2018.06.015

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Organic Chemistry
Role:
Author
ORCID:
0000-0001-7365-3617
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Oxford college:
St Hugh's College
Role:
Author
ORCID:
0000-0002-5148-117X
More from this funder
Funding agency for:
Schiedel, M
Grant:
SCHI 1408/1-1
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Funding agency for:
Conway, S
Publisher:
Elsevier Publisher's website
Journal:
Current Opinion in Chemical Biology Journal website
Volume:
45
Pages:
166-178
Publication date:
2018-06-27
Acceptance date:
2018-06-11
DOI:
EISSN:
1879-0402
ISSN:
1367-5931
Pmid:
29958150
Source identifiers:
864625
Language:
English
Pubs id:
pubs:864625
UUID:
uuid:3613bc7a-f1dc-4bd7-95b7-18b165cdf7ad
Local pid:
pubs:864625
Deposit date:
2018-09-03

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