Quasi-native Chaperonin-bound Intermediates in Facilitated Protein Folding
Open Access
- 1 October 1995
- journal article
- Published by Elsevier BV
- Vol. 270 (41), 23910-23913
- https://doi.org/10.1074/jbc.270.41.23910
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Specificity in chaperonin-mediated protein foldingNature, 1995
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Chaperonin duetNature, 1993
- Folding in vivo of bacterial cytoplasmic proteins: Role of GroELCell, 1993
- Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ionBiochemistry, 1993
- To Fold or Not to Fold . . .Science, 1993
- Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteinsProtein Science, 1992
- 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
- Turnover of tubulin and the N site GTP in chinese hamster ovary cellsCell, 1977