The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
Open accessAbstract
The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like structure. Here we define the contribution of this system to protein folding across the entire E. coli proteome. Approximately 250 different proteins interact with GroEL, but most of these can utilize either GroEL or the upstream chaperones trigger factor (TF) and DnaK for folding. Obligate GroEL-dependence is limited to only approximately 85 substrates, including 13 essential proteins, and occupying more than 75% of GroEL capacity. These proteins appear to populate kinetically trapped intermediates during folding; they are stabilized by TF/DnaK against aggregation but reach native state only upon transfer to GroEL/GroES. Interestingly, substantially enriched among the GroEL substrates are proteins with (betaalpha)8 TIM-barrel domains. We suggest that the chaperonin system may have facilitated the evolution of this fold into a versatile platform for the implementation of numerous enzymatic functions.
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
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Self-citationMolecular 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
Self-citationThe 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
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
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,173
Large-Scale Proteomic Analysis of the Human Spliceosome
Rappsilber, J., Ryder, U., Lamond, A. I., & Mann, M. (2002) · Genome Research · doi:10.1101/gr.473902 · Cited by 943
Self-citationProtein Folding: A Perspective from Theory and Experiment
Dobson, C. M., Šali, A., & Karplus, M. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19980420)37:7<868::aid-anie868>3.0.co;2-h · Cited by 869
Experimental Determination and System Level Analysis of Essential Genes in Escherichia coli MG1655
Gerdes, S. Y., Scholle, M. D., Campbell, J. W., Balázsi, G., Ravasz, E., Daugherty, M. D., Somera, A. L., Kyrpides, N. C., Anderson, I., Gelfand, M. S., et al. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.19.5673-5684.2003 · Cited by 725
Fayet, O., Ziegelhoffer, T., & Georgopoulos, C. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1379-1385.1989 · Cited by 705
Self-citationAnalysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry
Lasonder, E., Ishihama, Y., Andersen, J. S., Vermunt, A. M. W., Pain, A., Sauerwein, R. W., Eling, W. M. C., Hall, N., Waters, A. P., Stunnenberg, H. G., et al. (2002) · Nature · doi:10.1038/nature01111 · Cited by 652
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-citationHSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Stress-Induced Mutagenesis in Bacteria
Foster, P. L. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701648494 · Cited by 536
Yam, A. Y., Xia, Y., Lin, H.-T. J., Burlingame, A., Gerstein, M., & Frydman, J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1515 · Cited by 420
Proteomics in gram‐negative bacterial outer membrane vesicles
Lee, E., Choi, D., Kim, K., & Gho, Y. S. (2008) · Mass Spectrometry Reviews · doi:10.1002/mas.20175 · Cited by 339
Metadata
- Authors
- Kerner, M. J., Naylor, D. J., Ishihama, Y., Maier, T., Chang, H.-C., Stines, A. P., Georgopoulos, C., Frishman, D., Hayer-Hartl, M., Mann, M., & Hartl, F. U.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 122
- Issue
- 2
- Pages
- 209-220
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2147289825
- Cited by
- 659
- References
- 38
- FWCI
- 13.48
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli. https://app.cochat.ai/papers/10.1016/j.cell.2005.05.028
- The paper
- Kerner, M. J., Naylor, D. J., Ishihama, Y., Maier, T., Chang, H.-C., Stines, A. P., Georgopoulos, C., Frishman, D., Hayer-Hartl, M., Mann, M., & Hartl, F. U. (2005). Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli. Cell. https://doi.org/10.1016/j.cell.2005.05.028
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.
