CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2010.07737.x/fullpdf
Reference74 articles.
1. Chaperoned ubiquitylation - crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex;Zhang;Mol Cell,2005
2. Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity;Nikolay;J Biol Chem,2004
3. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold;Cyr;Trends Biochem Sci,2002
4. From the cradle to the grave: molecular chaperones that may choose between folding and degradation;Höhfeld;EMBO Rep,2001
5. Protein turnover: a CHIP programmed for proteolysis;Wiederkehr;Curr Biol,2002
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