The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Understanding protein folding via free-energy surfaces from theory and experiment
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Citations
Cites
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648 · cited 1×
“For a folding reaction that is ratelimited by an entropic barrier15, increasing the fraction of contacts that are short-range in the native state (and thus the transition state) accelerates folding in two related ways: (1) it facilitates locating the transition state by a diffusive search, and ( 2 ) it lowers the entr…”
BackgroundFrom Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Cited by
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Self-citationProtein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
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
The structural basis of protein folding and its links with human disease
Dobson, C. M. (2001) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.2000.0758 · Cited by 932
Self-citationDirect Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 911
Self-citation
Metadata
- Authors
- Dinner, A. R., Šali, A., Smith, L. J., Dobson, C. M., & Karplus, M.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 25
- Issue
- 7
- Pages
- 331-339
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2152474890
- Cited by
- 496
- References
- 2
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
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How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Understanding protein folding via free-energy surfaces from theory and experiment. https://app.cochat.ai/papers/10.1016/s0968-0004(00)01610-8
- The paper
- Dinner, A. R., Šali, A., Smith, L. J., Dobson, C. M., & Karplus, M. (2000). Understanding protein folding via free-energy surfaces from theory and experiment. Trends in Biochemical Sciences. https://doi.org/10.1016/s0968-0004(00)01610-8
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.
