The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System
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Citations
Cites
Guzman, L. M., Belin, D., Carson, M. J., & Beckwith, J. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.14.4121-4130.1995 · Cited by 4,935
Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123
Molecular chaperones in cellular protein folding
Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,568
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
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
Hemmingsen, S. M., Woolford, C., van der Vies, S. M., Tilly, K., Dennis, D. T., Georgopoulos, C. P., Hendrix, R. W., & Ellis, R. J. (1988) · Nature · doi:10.1038/333330a0 · Cited by 1,283
Ellis, R. J., & van der Vies, S. M. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.001541 · Cited by 1,120
Role of the Major Heat Shock Proteins as Molecular Chaperones
Georgopoulos, C., & Welch, W. J. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.003125 · Cited by 1,096
Proteins as molecular chaperones
Ellis, J. (1987) · Nature · doi:10.1038/328378a0 · Cited by 916
Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., & Hartl, F.-U. (1991) · Nature · doi:10.1038/352036a0 · Cited by 854
Self-citationFayet, O., Ziegelhoffer, T., & Georgopoulos, C. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1379-1385.1989 · Cited by 705
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
Self-citationRecombinant protein folding and misfolding in Escherichia coli
Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,445
Muchowski, P. J., Schaffar, G., Sittler, A., Wanker, E. E., Hayer-Hartl, M. K., & Hartl, F. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140202897 · Cited by 667
Self-citationProteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
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., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.028 · Cited by 659
Self-citationNarberhaus, F. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.1.64-93.2002 · Cited by 538
Metadata
- Authors
- Ewalt, K. L., Hendrick, J. P., Houry, W. A., & Hartl, F. U.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-08
- Volume
- 90
- Issue
- 3
- Pages
- 491-500
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2098665638
- Cited by
- 344
- References
- 36
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80509-7
- The paper
- Ewalt, K. L., Hendrick, J. P., Houry, W. A., & Hartl, F. U. (1997). In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System. Cell. https://doi.org/10.1016/s0092-8674(00)80509-7
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.
