The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.
Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated
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Citations
Cites
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
Physical chemistry of macromolecules
(2007) · Choice Reviews Online · doi:10.5860/choice.45-2038 · Cited by 3,765
Living with Water Stress: Evolution of Osmolyte Systems
Yancey, P. H., Clark, M. E., Hand, S. C., Bowlus, R. D., & Somero, G. N. (1982) · Science · doi:10.1126/science.7112124 · Cited by 3,740
Zur Lehre von der Wirkung der Salze: Zweite Mittheilung
Hofmeister, F. (1888) · Archiv für Experimentelle Pathologie und Pharmakologie · doi:10.1007/bf01918191 · Cited by 2,956
(2015) · An Einstein Encyclopedia · doi:10.1515/9781400873364-029 · Cited by 2,581
Proteins, amino acids and peptides
Oppermann, R. H. (1943) · Journal of the Franklin Institute · doi:10.1016/s0016-0032(43)91372-9 · Cited by 2,168
Tanford, C. (1968) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60401-5 · Cited by 2,130
Physical chemistry of macromolecules
Fixman, M. (1962) · Comparative Biochemistry and Physiology · doi:10.1016/0010-406x(62)90048-8 · Cited by 2,017
Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look
Wyman, J. (1964) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60190-4 · Cited by 1,608
The Hofmeister effect and the behaviour of water at interfaces
Collins, K. D., & Washabaugh, M. W. (1985) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005369 · Cited by 1,605
Cited by
Chi, E. Y., Krishnan, S., Randolph, T. W., & Carpenter, J. F. (2003) · Pharmaceutical Research · doi:10.1023/a:1025771421906 · Cited by 1,379
WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION
Levy, Y., & Onuchic, J. N. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102134 · Cited by 1,048
Protein aggregation and its inhibition in biopharmaceutics
Wang, W. (2005) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2004.11.014 · Cited by 983
Timasheff, S. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122225399 · Cited by 718
Self-citationStabilization of multimeric enzymes: Strategies to prevent subunit dissociation
Fernandez-Lafuente, R. (2009) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2009.08.009 · Cited by 621
Metadata
- Authors
- Timasheff, S. N.
- Venue
- Advances in Protein Chemistry
- Publisher
- Elsevier
- Published
- 1998
- Volume
- 51
- Pages
- 355-432
- ISSN
- 0065-3233 (ISSN-L)
- OpenAlex
- W1576271719
- Cited by
- 620
- References
- 96
- FWCI
- 24.45
- Type
- book chapter
- Language
- en
- Open access
- closed
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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.
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- CoChat. (2026). Citation check: Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated. https://app.cochat.ai/papers/10.1016/s0065-3233(08)60656-7
- The paper
- Timasheff, S. N. (1998). Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated. Advances in Protein Chemistry. https://doi.org/10.1016/s0065-3233(08)60656-7
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.
