Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
Open Access
- 19 December 1994
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 19 (12) , 543-548
- https://doi.org/10.1016/0968-0004(94)90058-2
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative formsCell, 1994
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle.The Journal of cell biology, 1994
- Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperoninCurrent Biology, 1994
- Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulinThe Journal of cell biology, 1993
- Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1Philosophical Transactions Of The Royal Society B-Biological Sciences, 1993
- Structure of a molecular chaperone from a thermophilic archaebacteriumNature, 1993
- TCP1 complex is a molecular chaperone in tubulin biogenesisNature, 1992
- Protein folding in the cellNature, 1992