The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
The present view of the mechanism of protein folding
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Citations
Cites
Duan, Y., & Kollman, P. A. (1998) · Science · doi:10.1126/science.282.5389.740 · Cited by 1,333
Kim, P. S., & Baldwin, R. L. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002331 · Cited by 1,035
Mechanical and chemical unfolding of a single protein: A comparison
Carrion-Vazquez, M., Oberhauser, A. F., Fowler, S. B., Marszalek, P. E., Broedel, S. E., Clarke, J., & Fernandez, J. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3694 · Cited by 1,027
Ferrin, T. E., Huang, C. C., Jarvis, L. E., & Langridge, R. (1988) · Journal of Molecular Graphics · doi:10.1016/0263-7855(88)80054-7 · Cited by 950
Fersht, A. R., Matouschek, A., & Serrano, L. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90561-w · Cited by 932
Self-citationThe molecular basis for the chemical denaturation of proteins by urea
Bennion, B. J., & Daggett, V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0930122100 · Cited by 896
Self-citationNucleation, Rapid Folding, and Globular Intrachain Regions in Proteins
Wetlaufer, D. B. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.3.697 · Cited by 831
Absolute comparison of simulated and experimental protein-folding dynamics
Snow, C. D., Nguyen, H., Pande, V. S., & Gruebele, M. (2002) · Nature · doi:10.1038/nature01160 · Cited by 701
Karplus, M., & Weaver, D. L. (1976) · Nature · doi:10.1038/260404a0 · Cited by 621
Protein folding: Hypotheses and experiments
Ptitsyn, O. B. (1987) · Journal of Protein Chemistry · doi:10.1007/bf00248050 · Cited by 543
Cited by
Are Biological Systems Poised at Criticality?
Mora, T., & Bialek, W. (2011) · Journal of Statistical Physics · doi:10.1007/s10955-011-0229-4 · Cited by 734
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.037 · Cited by 318
“During the folding process, these short hydrophobic stretches will most likely form the nucleus around which the protein condenses (Daggett and Fersht, 2003).”
BackgroundBiomolecular simulation and modelling: status, progress and prospects
van der Kamp, M. W., Shaw, K. E., Woods, C. J., & Mulholland, A. J. (2008) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0105.focus · Cited by 90
Metadata
- Authors
- Daggett, V., & Fersht, A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2003-06
- Volume
- 4
- Issue
- 6
- Pages
- 497-502
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1588812136
- Cited by
- 398
- References
- 42
- FWCI
- 2.26
- Type
- journal article
- Language
- en
- Open access
- closed
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- Daggett, V., & Fersht, A. (2003). The present view of the mechanism of protein folding. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm1126
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.
