Protein folding and chaperonins
- 1 July 1992
- journal article
- review article
- Published by Springer Nature in Plant Molecular Biology
- Vol. 19 (4) , 677-687
- https://doi.org/10.1007/bf00026793
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteinsProtein Science, 1992
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeastBiochemistry, 1991
- The role of heat-shock and chaperone proteins in protein folding: possible molecular mechanismsProtein Engineering, Design and Selection, 1991
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Chaperone function: cracking the second half of the genetic codeThe Plant Journal, 1991
- Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.Plant Cell, 1989
- Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunitsEuropean Journal of Biochemistry, 1987
- Assembly in E. coli of a functional multi-subunit ribulose bisphosphate carboxylase from a blue-green algaNature, 1985