The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein
Open accessAbstract
GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (approximately 30 kDa) folded more rapidly as the size of the cage was gradually reduced to a point where restriction in space slowed folding dramatically. For larger proteins (approximately 40-50 kDa), either expanding or reducing cage volume decelerated folding. Additionally, interactions with the C-terminal, mildly hydrophobic Gly-Gly-Met repeat sequences of GroEL protruding into the cavity, and repulsion effects from the negatively charged cavity wall were required for rapid folding of some proteins. We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways.
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
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Macromolecular crowding: an important but neglected aspect of the intracellular environment
Ellis, R. J. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00172-x · Cited by 1,153
Polypeptide Flux through Bacterial Hsp70
Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., & Hartl, F. U. (1999) · Cell · doi:10.1016/s0092-8674(00)80787-4 · Cited by 424
Self-citation
Cited by
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Self-citationIn vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,439
Self-citationHsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., Gurkan, C., Kellner, W., Matteson, J., Plutner, H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.043 · Cited by 601
Beck, J. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i1.48 · Cited by 494
Protein Folding in the Cytoplasm and the Heat Shock Response
Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M., & Hartl, F. U. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004390 · Cited by 428
Self-citation
Metadata
- Authors
- Tang, Y.-C., Chang, H.-C., Roeben, A., Wischnewski, D., Wischnewski, N., Kerner, M. J., Hartl, F. U., & Hayer-Hartl, M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-06
- Volume
- 125
- Issue
- 5
- Pages
- 903-914
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2107370157
- Cited by
- 311
- References
- 4
- FWCI
- 9.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
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.
