The Hsp110 Molecular Chaperone Stabilizes Apolipoprotein B from Endoplasmic Reticulum-associated Degradation (ERAD)
Open Access
- 1 November 2007
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 282 (45) , 32665-32675
- https://doi.org/10.1074/jbc.m705216200
Abstract
No abstract availableKeywords
This publication has 67 references indexed in Scilit:
- Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationThe Journal of cell biology, 2007
- The Cytoplasmic Hsp70 Chaperone Machinery Subjects Misfolded and Endoplasmic Reticulum Import-incompetent Proteins to Degradation via the Ubiquitin–Proteasome SystemMolecular Biology of the Cell, 2007
- Cdc48 (p97): a ‘molecular gearbox’ in the ubiquitin pathway?Trends in Biochemical Sciences, 2007
- Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factorThe EMBO Journal, 2006
- Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70sThe EMBO Journal, 2006
- A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradationGenes & Development, 2001
- Co-translational Interactions of Apoprotein B with the Ribosome and Translocon during Lipoprotein Assembly or Targeting to the ProteasomePublished by Elsevier ,2001
- Apoprotein B Degradation Is Promoted by the Molecular Chaperones hsp90 and hsp70Published by Elsevier ,2001
- Regulated Co-translational Ubiquitination of Apolipoprotein B100Journal of Biological Chemistry, 1998
- Ubiquitin-Proteasome Pathway Mediates Intracellular Degradation of Apolipoprotein BBiochemistry, 1996