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CBP/p300 bromodomains regulate amyloid-like protein aggregation upon aberrant lysine acetylation

Abstract:

Lysine acetylation is becoming increasingly recognized as a general biological principle in cellular homeostasis, and is subject to abnormal control in different human pathologies. Here, we describe a global effect on amyloid-like protein aggregation in human cells that results from aberrant lysine acetylation. Bromodomain reader proteins are involved in the aggregation process and, using chemical biology and gene silencing, we establish that p300/CBP bromodomains are necessary for aggregatio...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.chembiol.2016.11.009

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Department:
Oxford, MSD, Oncology
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Author
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Department:
Oxford, MSD, NDM, Target Discovery Institute
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Author
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Department:
Oxford, MSD, NDM, Target Discovery Institute
Role:
Author
More by this author
Department:
Oxford, MSD, NDM, Target Discovery Institute
Role:
Author
More by this author
Department:
Oxford, MSD, Oncology
Role:
Author
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Funding agency for:
Olzscha, H
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Funding agency for:
Olzscha, H
Eurocan Platform More from this funder
Publisher:
Cell Press Publisher's website
Journal:
Cell Chemical Biology Journal website
Volume:
24
Issue:
1
Pages:
9–23
Publication date:
2016-12-10
Acceptance date:
2016-11-15
DOI:
ISSN:
2451-9456
Pubs id:
pubs:667266
URN:
uri:a7ce66df-21a2-40e1-b97f-28c9c5bfc44e
UUID:
uuid:a7ce66df-21a2-40e1-b97f-28c9c5bfc44e
Local pid:
pubs:667266
Paper number:
1

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