The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Three key residues form a critical contact network in a protein folding transition state
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Citations
Cites
Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding
Fersht, A. (2017) · Series in Structural Biology · doi:10.1142/10574 · Cited by 2,039
Structure and Mechanism in Protein Science. A guide to Enzyme Catalysis and Protein Folding
Howland, J. L. (2001) · Biochemistry and Molecular Biology Education · Cited by 1,823
Protein denaturation. C. Theoretical models for the mechanism of denaturation.
Tanford, C. (1970) · PubMed · Cited by 1,546
Plaxco, K. W., Simons, K. T., & Baker, D. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1645 · Cited by 1,518
Tanford, C. (1970) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60241-7 · Cited by 1,277
Mapping the transition state and pathway of protein folding by protein engineering
Matouschek, A., Kellis, J. T., Serrano, L., & Fersht, A. R. (1989) · Nature · doi:10.1038/340122a0 · Cited by 703
A simple model for calculating the kinetics of protein folding from three-dimensional structures
Muñoz, V., & Eaton, W. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11311 · Cited by 636
"New View" of Protein Folding Reconciled with the Old Through Multiple Unfolding Simulations
Lazaridis, T., & Karplus, M. (1997) · Science · doi:10.1126/science.278.5345.1928 · Cited by 505
Self-citationThe molten globule state of α‐lactalbumin
Kuwajima, K. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.1.8566530 · Cited by 458
Protein Structure Determination in Solution by Nuclear Magnetic Resonance Spectroscopy
Wüthrich, K. (1989) · Science · doi:10.1126/science.2911719 · Cited by 454
Cited by
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Self-citationAtomic-level characterization of the structural dynamics of proteins
Shaw, D. E., Maragakis, P., Lindorff-Larsen, K., Piana, S., Dror, R. O., Eastwood, M. P., Bank, J. A., Jumper, J. M., Salmon, J. K., Shan, Y., et al. (2010) · Science · doi:10.1126/science.1187409 · Cited by 1,923
Small-world view of the amino acids that play a key role in protein folding
Vendruscolo, M., Dokholyan, N. V., Paci, E., & Karplus, M. (2002) · Physical Review E · doi:10.1103/physreve.65.061910 · Cited by 384
Self-citationAtomic-level description of ubiquitin folding
Piana, S., Lindorff-Larsen, K., & Shaw, D. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218321110 · Cited by 326
Controlling Allosteric Networks in Proteins
Dokholyan, N. V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00544 · Cited by 260
Metadata
- Authors
- Vendruscolo, M., Paci, E., Dobson, C. M., & Karplus, M.
- Venue
- Nature
- Published
- 2001-02
- Volume
- 409
- Issue
- 6820
- Pages
- 641-645
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1536428180
- Cited by
- 431
- References
- 27
- FWCI
- 9.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Three key residues form a critical contact network in a protein folding transition state. https://app.cochat.ai/papers/10.1038/35054591
- The paper
- Vendruscolo, M., Paci, E., Dobson, C. M., & Karplus, M. (2001). Three key residues form a critical contact network in a protein folding transition state. Nature. https://doi.org/10.1038/35054591
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.
