CHIP: a quality-control E3 ligase collaborating with molecular chaperones
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry
Reference32 articles.
1. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome;Alberti;Journal of Biological Chemistry,2002
2. The U box is a modified RING finger—A common domain in ubiquitination;Aravind;Current Biology,2000
3. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions;Ballinger;Molecular Cell Biology,1999
4. Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70;Bercovich;Journal of Biological Chemistry,1997
5. Hsp90 & Co.—A holding for folding;Buchner;Trends in Biochemical Sciences,1999
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