The Hsp70 and Hsp60 Chaperone Machines
Open Access
- 1 February 1998
- Vol. 92 (3) , 351-366
- https://doi.org/10.1016/s0092-8674(00)80928-9
Abstract
No abstract availableThis publication has 108 references indexed in Scilit:
- Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70Journal of Molecular Biology, 1997
- Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reactionJournal of Molecular Biology, 1997
- Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiaeJournal of Molecular Biology, 1997
- Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein MisfoldsJournal of Molecular Biology, 1995
- Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulatorsFEBS Letters, 1995
- The Role of ATP in the Functional Cycle of the DnaK Chaperone SystemJournal of Molecular Biology, 1995
- The Origins and Consequences of Asymmetry in the Chaperonin Reaction CycleJournal of Molecular Biology, 1995
- Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperoninFEBS Letters, 1995
- Cooperativity in ATP hydrolysis by GroEL is increased by GroESFEBS Letters, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991