The GroEL/GroES cis cavity as a passive anti‐aggregation device
Open Access
- 3 July 2009
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 583 (16), 2654-2662
- https://doi.org/10.1016/j.febslet.2009.06.049
Abstract
The GroEL/GroES chaperonin folding chamber is an encapsulated space of ∼65 Å diameter with a hydrophilic wall, inside of which many cellular proteins reach the native state. The question of whether t...Keywords
This publication has 48 references indexed in Scilit:
- Chaperonin complex with a newly folded protein encapsulated in the folding chamberNature, 2009
- Chaperonin chamber accelerates protein folding through passive action of preventing aggregationProceedings of the National Academy of Sciences, 2008
- Concerted Release of Substrate Domains from GroEL by ATP Is Demonstrated with FRETJournal of Molecular Biology, 2008
- Essential role of the chaperonin folding compartment in vivoThe EMBO Journal, 2008
- Folding trajectories of human dihydrofolate reductase inside the GroEL–GroES chaperonin cavity and free in solutionProceedings of the National Academy of Sciences, 2007
- Perturbed ATPase activity and not “close confinement” of substrate in the cis cavity affects rates of folding by tail-multiplied GroELProceedings of the National Academy of Sciences, 2007
- Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none mannerProceedings of the National Academy of Sciences of the United States of America, 2007
- Disulfide formation as a probe of folding in GroEL–GroES reveals correct formation of long-range bonds and editing of incorrect short-range onesProceedings of the National Academy of Sciences of the United States of America, 2007
- Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysisProtein Science, 2006
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991