The DOI matches its Crossref record; 160 of the 160 references it cites were found in a registry or an index.
Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?
Open accessOverview
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
Principles of polymer chemistry
(1995) · Choice Reviews Online · doi:10.5860/choice.33-2140 · Cited by 15,218
Some Factors in the Interpretation of Protein Denaturation
Kauzmann, W. (1959) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,870
Physical chemistry of macromolecules
(2007) · Choice Reviews Online · doi:10.5860/choice.45-2038 · Cited by 3,765
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
Conformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,938
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
From 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
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins: Structure, Function, and Genetics · doi:10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7 · Cited by 2,078
Self-citationIntrinsically unstructured proteins
Tompa, P. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02169-2 · Cited by 2,050
Protein misfolding, evolution and disease
Dobson, C. M. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01445-0 · Cited by 1,952
Cited by
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Flexible nets: The roles of intrinsic disorder in protein interaction networks
Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122
Self-citationPorat, Y., Abramowitz, A., & Gazit, E. (2006) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2005.00318.x · Cited by 989
Function and structure of inherently disordered proteins
Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963
Self-citationLength-dependent prediction of protein intrinsic disorder
Peng, K., Radivojac, P., Vucetic, S., Dunker, A. K., & Obradovic, Z. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-208 · Cited by 928
Metadata
- Authors
- Uversky, V. N.
- Venue
- Cellular and Molecular Life Sciences (CMLS)
- Published
- 2003-09-01
- Volume
- 60
- Issue
- 9
- Pages
- 1852-1871
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- OpenAlex
- W2060723204
- Cited by
- 314
- References
- 160
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- green
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: Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go? https://app.cochat.ai/papers/10.1007/s00018-003-3096-6
- The paper
- Uversky, V. N. (2003). Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go? Cellular and Molecular Life Sciences (CMLS). https://doi.org/10.1007/s00018-003-3096-6
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.
