Unfolding protein folding
- 1 July 1991
- journal article
- Published by Springer Nature in Nature
- Vol. 352 (6330) , 17-18
- https://doi.org/10.1038/352017a0
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- GroE facilitates refolding of citrate synthase by suppressing aggregationBiochemistry, 1991
- Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependentBiochemistry, 1990
- Evidence for a molten globule state as a general intermediate in protein foldingFEBS Letters, 1990
- Protein Sorting to Mitochondria: Evolutionary Conservations of Folding and AssemblyScience, 1990
- Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteriaTrends in Biotechnology, 1990
- Molecular chaperones: proteins essential for the biogenesis of some macromolecular structuresTrends in Biochemical Sciences, 1989
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988
- Asymmetry of tyrosyl-tRNA synthetase in solutionBiochemistry, 1988
- Two configurations of a channel-forming membrane proteinNature, 1984