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Molecular basis of USP7 inhibition by selective small-molecule inhibitors.

Abstract:

Ubiquitination controls the stability of most cellular proteins, and its deregulation contributes to human diseases including cancer. Deubiquitinases remove ubiquitin from proteins, and their inhibition can induce the degradation of selected proteins, potentially including otherwise 'undruggable' targets. For example, the inhibition of ubiquitin-specific protease 7 (USP7) results in the degradation of the oncogenic E3 ligase MDM2, and leads to re-activation of the tumour suppressor p53 in var...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted manuscript

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Publisher copy:
10.1038/nature24451

Authors


Turnbull, AP More by this author
Ioannidis, S More by this author
Krajewski, WW More by this author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM; Target Discovery Institute
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Lister Institute for Preventive Medicine More from this funder
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Journal website
Volume:
550
Pages:
481–486
Publication date:
2017-10-18
Acceptance date:
2017-09-25
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
Pubs id:
pubs:737157
URN:
uri:785217ad-82b1-44c7-bac7-a7c17a6ba790
UUID:
uuid:785217ad-82b1-44c7-bac7-a7c17a6ba790
Local pid:
pubs:737157
Language:
English
Keywords:

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