Positive cooperativity in the functioning of molecular chaperone GroEL.
Open Access
- 1 April 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (10) , 6796-6800
- https://doi.org/10.1016/s0021-9258(19)50496-3
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- (Mg–ATP)-dependent self-assembly of molecular chaperone GroELNature, 1990
- Protein-catalysed protein foldingTrends in Biotechnology, 1990
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989
- Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisNature, 1989
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- Isolation and characterization of the host protein groE involved in bacteriophage lambda assemblyJournal of Molecular Biology, 1979
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- The quantitative interpretation of maximum in Scatchard plotsFEBS Letters, 1974
- Low-molecular Carbohydrates in Algae. II. Synthesis of 1-D-Mannitol Monoacetate and 1,6-D-Mannitol Diacetate.Acta Chemica Scandinavica, 1953