The Roles of the Two Zinc Binding Sites in DnaJ
Open Access
- 1 November 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (45) , 44457-44466
- https://doi.org/10.1074/jbc.m307491200
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Folding of Newly Translated Proteins In Vivo: The Role of Molecular ChaperonesAnnual Review of Biochemistry, 2001
- Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperoneThe EMBO Journal, 2001
- Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteinsCell Stress and Chaperones, 2000
- Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperonesProceedings of the National Academy of Sciences, 1999
- Protein Folding Activity of Hsp70 Is Modified Differentially by the Hsp40 Co-chaperones Sis1 and Ydj1Journal of Biological Chemistry, 1998
- Role of the J-domain in the cooperation of Hsp40 with Hsp70Proceedings of the National Academy of Sciences, 1998
- The Conserved Carboxyl Terminus and Zinc Finger-like Domain of the Co-chaperone Ydj1 Assist Hsp70 in Protein FoldingJournal of Biological Chemistry, 1998
- Nuclear Magnetic Resonance Solution Structure of the Human Hsp40 (HDJ-1) J-domainJournal of Molecular Biology, 1996
- A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK ProteinJournal of Biological Chemistry, 1996
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992