Journal article
A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin
- Abstract:
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Ubiquitylation, the posttranslational linkage of ubiquitin moieties to lysines in target proteins, helps regulate a myriad of biological processes. Ubiquitin, and sometimes ubiquitin-homology domains, are recognized by ubiquitin-binding domains, including CUE domains. CUE domains are thus generally thought to function by mediating interactions with ubiquitylated proteins. The chromatin remodeler, SMARCAD1, interacts with KAP1, a transcriptional corepressor. The SMARCAD1-KAP1 interaction is di...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 4.7MB)
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- Publisher copy:
- 10.1016/j.str.2019.05.003
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Authors
Funding
Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 27
- Issue:
- 8
- Pages:
- 1316-1325.e6
- Publication date:
- 2019-06-13
- Acceptance date:
- 2019-05-13
- DOI:
- ISSN:
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1878-4186 and 0969-2126
- Pmid:
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31204252
- Source identifiers:
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1022843
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:1022843
- UUID:
-
uuid:245828bb-1421-45a7-ad70-8f9c80230945
- Local pid:
- pubs:1022843
- Deposit date:
- 2019-09-09
Terms of use
- Copyright holder:
- Francis Crick Institute
- Copyright date:
- 2019
- Notes:
-
© 2019 Francis Crick Institute. Published by Elsevier Ltd.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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