The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
Abstract
Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)–mediated protein folding, the final step in the accurate expression of genetic information. Major, asymmetric conformational changes in the GroEL double toroid accompany binding of ATP and the cochaperonin GroES. When a nonnative polypeptide, bound to one of the GroEL rings, is encapsulated by GroES to form a cis ternary complex, these changes drive the polypeptide into the sequestered cavity and initiate its folding. ATP hydrolysis in the cis ring primes release of the products, and ATP binding in the trans ring then disrupts the cis complex. This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Molecular chaperones in cellular protein folding
Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,568
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
MATRIX PROTEOGLYCANS: From Molecular Design to Cellular Function
Iozzo, R. V. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.609 · Cited by 1,637
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., & Sigler, P. B. (1994) · Nature · doi:10.1038/371578a0 · Cited by 1,321
Self-citationStructural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,258
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Xu, Z., Horwich, A. L., & Sigler, P. B. (1997) · Nature · doi:10.1038/41944 · Cited by 1,239
Self-citationMartin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., & Hartl, F.-U. (1991) · Nature · doi:10.1038/352036a0 · Cited by 854
Self-citationRudiger, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1501 · Cited by 815
Lee, G. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.659 · Cited by 779
Ehrnsperger, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.221 · Cited by 754
Cited by
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
Synthesis of Native Proteins by Chemical Ligation
Dawson, P. E., & Kent, S. B. H. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.923 · Cited by 1,082
Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
Yasuda, R., Noji, H., Yoshida, M., Kinosita, K., & Itoh, H. (2001) · Nature · doi:10.1038/35073513 · Cited by 819
Heat Shock Proteins and Cancer
Wu, J., Liu, T., Rios, Z., Mei, Q., Lin, X., & Cao, S. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.11.009 · Cited by 696
Metadata
- Authors
- Sigler, P. B., Xu, Z., Rye, H. S., Burston, S. G., Fenton, W. A., & Horwich, A. L.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1998-06
- Volume
- 67
- Issue
- 1
- Pages
- 581-608
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2144263933
- Cited by
- 572
- References
- 52
- FWCI
- 2.90
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. https://app.cochat.ai/papers/10.1146/annurev.biochem.67.1.581
- The paper
- Sigler, P. B., Xu, Z., Rye, H. S., Burston, S. G., Fenton, W. A., & Horwich, A. L. (1998). STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.67.1.581
Data sources
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.
