The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Contribution of hydrophobic interactions to protein stability
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
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
[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
Pace, C. N. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)31045-0 · Cited by 2,258
The Solubility of Amino Acids and Two Glycine Peptides in Aqueous Ethanol and Dioxane Solutions
Nozaki, Y., & Tanford, C. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77210-x · Cited by 1,432
Structural patterns in globular proteins
Levitt, M., & Chothia, C. (1976) · Nature · doi:10.1038/261552a0 · Cited by 1,276
Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of Proteins
Tanford, C. (1962) · Journal of the American Chemical Society · doi:10.1021/ja00881a009 · Cited by 1,005
ZOLLER, M. J., & SMITH, M. (1984) · DNA · doi:10.1089/dna.1.1984.3.479 · Cited by 886
Affinities of amino acid side chains for solvent water
Wolfenden, R., Andersson, L., Cullis, P. M., & Southgate, C. C. B. (1981) · Biochemistry · doi:10.1021/bi00507a030 · Cited by 865
Fauch, E., J-L, S. R., & Pliska (1983) · Chimie thérapeutique · Cited by 699
Folding and association of proteins
Jaenicke, R. (1987) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(87)90011-3 · Cited by 691
The Solubility of Amino Acids and Related Compounds in Aqueous Urea Solutions
Nozaki, Y., & Tanford, C. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51830-5 · Cited by 663
Cited by
Stability of Protein Pharmaceuticals
Manning, M. C., Patel, K., & Borchardt, R. T. (1989) · Pharmaceutical Research · doi:10.1023/a:1015929109894 · Cited by 1,078
Fersht, A. R., Matouschek, A., & Serrano, L. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90561-w · Cited by 932
Self-citationMembrane protein folding and oligomerization: the two-stage model
Popot, J. L., & Engelman, D. M. (1990) · Biochemistry · doi:10.1021/bi00469a001 · Cited by 932
De Novo Design and Structural Characterization of Proteins and Metalloproteins
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., & Lombardi, A. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.779 · Cited by 572
Rohloff, J. C., Gelinas, A. D., Jarvis, T. C., Ochsner, U. A., Schneider, D. J., Gold, L., & Janjic, N. (2014) · Molecular Therapy - Nucleic Acids · doi:10.1038/mtna.2014.49 · Cited by 533
Metadata
- Authors
- Kellis, J. T., Nyberg, K., S˘ail, D., & Fersht, A. R.
- Venue
- Nature
- Published
- 1988-06
- Volume
- 333
- Issue
- 6175
- Pages
- 784-786
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2032192940
- Cited by
- 431
- References
- 27
- FWCI
- 9.91
- 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: Contribution of hydrophobic interactions to protein stability. https://app.cochat.ai/papers/10.1038/333784a0
- The paper
- Kellis, J. T., Nyberg, K., S˘ail, D., & Fersht, A. R. (1988). Contribution of hydrophobic interactions to protein stability. Nature. https://doi.org/10.1038/333784a0
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.
