The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Chaperonin Function: Folding by Forced Unfolding
Open accessAbstract
The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding.
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Cites
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AAA+ superfamily ATPases: common structure–diverse function
Ogura, T., & Wilkinson, A. J. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00447.x · Cited by 956
Vale, R. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.1.f13 · Cited by 506
The mechanical stability of ubiquitin is linkage dependent
Carrion-Vazquez, M., Li, H., Lu, H., Marszalek, P. E., Oberhauser, A. F., & Fernandez, J. M. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb965 · Cited by 481
Measuring the Forces that Control Protein Interactions
Leckband, D. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.1 · Cited by 444
Metadata
- Authors
- Shtilerman, M., Lorimer, G. H., & Walter Englander, S.
- Venue
- Science
- Published
- 1999-04-30
- Volume
- 284
- Issue
- 5415
- Pages
- 822-825
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2053514414
- Cited by
- 290
- References
- 52
- FWCI
- 12.40
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
