J Proteins Catalytically Activate Hsp70 Molecules to Trap a Wide Range of Peptide Sequences
- 1 November 1998
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 2 (5) , 593-603
- https://doi.org/10.1016/s1097-2765(00)80158-6
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- The Lumenal Domain of Sec63p Stimulates the ATPase Activity of BiP and Mediates BiP Recruitment to the Translocon in Saccharomyces cerevisiaeThe Journal of cell biology, 1997
- Post-translational protein translocation: not all hsc70s are created equalTrends in Biochemical Sciences, 1996
- Real Time Kinetics of the DnaK/DnaJ/GrpE Molecular Chaperone Machine ActionPublished by Elsevier ,1996
- A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome.The Journal of cell biology, 1993
- Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiPCell, 1993
- Peptide-binding specificity of the molecular chaperone BiPNature, 1991
- Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complexNature, 1991
- Ordered Assembly of Nucleoprotein Structures at the Bacteriophage λ Replication Origin during the Initiation of DNA ReplicationJournal of Biological Chemistry, 1989
- Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*Biochemistry, 1967