HEDJ, an Hsp40 Co-chaperone Localized to the Endoplasmic Reticulum of Human Cells
Open Access
- 1 August 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (32), 24984-24992
- https://doi.org/10.1074/jbc.m000739200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- DnaJ Dramatically Stimulates ATP Hydrolysis by DnaK: Insight into Targeting of Hsp70 Proteins to Polypeptide SubstratesBiochemistry, 1999
- Protein Transport by Purified Yeast Sec Complex and Kar2p Without MembranesScience, 1997
- ER Quality Control: The Cytoplasmic ConnectionCell, 1997
- Molecular chaperones in cellular protein foldingNature, 1996
- Can Hsp70 proteins act as force-generating motors?Cell, 1995
- DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70Trends in Biochemical Sciences, 1994
- Eukaryotic DnaJ homologs and the specificity of Hsp70 activityCell, 1993
- Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein.The Journal of cell biology, 1991
- Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast.The Journal of cell biology, 1990
- A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.The Journal of cell biology, 1989