ArticleProceedings of the National Academy of Sciences of the United States of America1997
Protein folding: how the mechanism of GroEL action is defined by kinetics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL.Journal of chemical biology · 2013Article
- Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding.Protein engineering, design & selection : PEDS · 2011Article
- Protein refolding by pH-triggered chaperone binding and release.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- GroEL/S substrate specificity based on substrate unfolding propensity.Cell stress & chaperones · 2007Article
- Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL.Protein science : a publication of the Protein Society · 1999Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We propose a mechanism for the role of the bacterial chaperonin GroEL in folding proteins. The principal assumptions of the mechanism are (i) that many unfolded proteins bind to GroEL because GroEL preferentially binds small unstructured regions of the substrate protein, (ii) that substrate protein within the cavity of GroEL folds by the same kinetic mechanism and rate processes as in bulk solution, (iii) that stable or transient complexes with GroEL during the folding process are defined by a kinetic partitioning between formation and dissociation of the complex and the rate of folding and unfolding of the protein, and (iv) that dissociation from the complex in early stages of folding may lead to aggregation but dissociation at a late stage leads to correct folding. The experimental conditions for refolding may play a role in defining the function of GroEL in the folding pathway. We propose that the role of GroES and MgATP, either binding or hydrolysis, is to regulate the association and dissociation processes rather than affecting the rate of folding.
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Registered trials
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