Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction
Open Access
- 1 March 1997
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 266 (4) , 656-664
- https://doi.org/10.1006/jmbi.1996.0815
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Release of both native and non-native proteins from a cis-only GroEL ternary complexNature, 1996
- Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.Proceedings of the National Academy of Sciences, 1996
- The Origins and Consequences of Asymmetry in the Chaperonin Reaction CycleJournal of Molecular Biology, 1995
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopyNature, 1994
- Refolding of Barnase in the Presence of GroEJournal of Molecular Biology, 1993
- A polypeptide bound by the chaperonin groEL is localized within a central cavity.Proceedings of the National Academy of Sciences, 1993
- Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATPBiochemistry, 1992
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989