Chaperonins
- 1 April 1998
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 8 (2) , 159-165
- https://doi.org/10.1016/s0959-440x(98)80033-x
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein FoldingJournal of Molecular Biology, 1996
- GroEL Binds to and Unfolds Rhodanese PosttranslationallyPublished by Elsevier ,1996
- Solution structures of GroEL and its complex with rhodanese from small-angle neutron scatteringStructure, 1996
- Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein MisfoldsJournal of Molecular Biology, 1995
- Two Lines of Allosteric Communication in the Oligomeric Chaperonin GroEL are Revealed by the Single Mutation Arg196→AlaJournal of Molecular Biology, 1994
- Molecular Chaperones: Opening and closing the Anfinsen cageCurrent Biology, 1994
- Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperoninCurrent Biology, 1994
- Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein foldingBiochemistry, 1993
- Structure of a molecular chaperone from a thermophilic archaebacteriumNature, 1993
- TCP1 complex is a molecular chaperone in tubulin biogenesisNature, 1992