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Chaperoned ubiquitylation - Crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
Minghao Zhang
, Mark Windheim
, S. Mark Roe
, Mark Peggie
,
Philip Cohen
, Chrisostomos Prodromou
, Laurence H. Pearl
Research output
:
Contribution to journal
›
Article
›
peer-review
367
Citations (Scopus)
Overview
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Dive into the research topics of 'Chaperoned ubiquitylation - Crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex'. Together they form a unique fingerprint.
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Keyphrases
Chaperone
100%
Ubiquitylation
100%
Ubc13
100%
U-box E3 Ubiquitin Ligase
100%
Uev1A
100%
Heat Shock Protein 90 (Hsp90)
66%
TPR Domain
66%
Binding Site
33%
Heat Shock Protein 70 (HSP70)
33%
Protomers
33%
Ubiquitin
33%
Deubiquitinating Enzyme
33%
K63-linked Polyubiquitination
33%
Client Proteins
33%
Asymmetric Pattern
33%
Site Activity
33%
Chain Extension
33%
U-box Domain
33%
Functional Partners
33%
Selective Cooperation
33%
Decapeptide
33%
Asymmetric Homodimer
33%
Biochemistry, Genetics and Molecular Biology
Crystal Structure
100%
Ubiquitination
100%
Ubiquitin-Conjugating Enzyme
100%
Hsp90
66%
TPR Domain
66%
C-Terminus
33%
Cooperation
33%
Binding Site
33%
Hsp70
33%
Protomer
33%
Conformation
33%
Ubiquitin
33%