The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Theoretical studies of protein folding and unfolding
Overview
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
The nature of folded states of globular proteins
Honeycutt, J. D., & Thirumalai, D. (1992) · Biopolymers · doi:10.1002/bip.360320610 · Cited by 360
A lattice model for protein structure prediction at low resolution.
Hinds, D. A., & Levitt, M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.2536 · Cited by 217
De novo and inverse folding predictions of protein structure and dynamics
Godzik, A., Kolinski, A., & Skolnick, J. (1993) · Journal of Computer-Aided Molecular Design · doi:10.1007/bf02337559 · Cited by 91
Cited by
Anatomy of hot spots in protein interfaces
Bogan, A. A., & Thorn, K. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1843 · Cited by 1,988
Nucleation mechanisms in protein folding
Fersht, A. R. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80002-4 · Cited by 545
Shea, J.-E., & Brooks III, C. L. (2001) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.52.1.499 · Cited by 481
Accelerated Poisson–Boltzmann calculations for static and dynamic systems
Luo, R., David, L., & Gilson, M. K. (2002) · Journal of Computational Chemistry · doi:10.1002/jcc.10120 · Cited by 462
Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics
Chan, H. S., & Dill, K. A. (1998) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19980101)30:1<2::aid-prot2>3.0.co;2-r · Cited by 438
Metadata
- Authors
- Karplus, M., & Šali, A.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 1995-02
- Volume
- 5
- Issue
- 1
- Pages
- 58-73
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2072417182
- Cited by
- 258
- References
- 3
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- closed
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: Theoretical studies of protein folding and unfolding. https://app.cochat.ai/papers/10.1016/0959-440x(95)80010-x
- The paper
- Karplus, M., & Šali, A. (1995). Theoretical studies of protein folding and unfolding. Current Opinion in Structural Biology. https://doi.org/10.1016/0959-440x(95)80010-x
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.