The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
[3]Theory of protein solubility
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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
Physical chemistry of macromolecules
(2007) · Choice Reviews Online · doi:10.5860/choice.45-2038 · Cited by 3,765
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
Physical chemistry of macromolecules
Fixman, M. (1962) · Comparative Biochemistry and Physiology · doi:10.1016/0010-406x(62)90048-8 · Cited by 2,017
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
Structure and stability of biological macromolecules
Timasheff, S. N., & Fasman, G. D. (1969) · Cited by 1,316
Self-citationMechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures
Gekko, K., & Timasheff, S. N. (1981) · Biochemistry · doi:10.1021/bi00519a023 · Cited by 1,181
Self-citationThe stabilization of proteins by sucrose.
Lee, J. C., & Timasheff, S. N. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68947-7 · Cited by 1,112
Self-citationStabilization of protein structure by sugars
Arakawa, T., & Timasheff, S. N. (1982) · Biochemistry · doi:10.1021/bi00268a033 · Cited by 1,083
Self-citationMelander, W., & Horváth, C. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90434-9 · Cited by 914
Cited by
Kramer, R. M., Shende, V. R., Motl, N., Pace, C. N., & Scholtz, J. M. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.01.060 · Cited by 418
Predicting the Solubility of Recombinant Proteins in Escherichia coli
Wilkinson, D. L., & Harrison, R. G. (1991) · Nature Biotechnology · doi:10.1038/nbt0591-443 · Cited by 250
High-concentration protein formulations: How high is high?
Garidel, P., Kuhn, A. B., Schäfer, L. V., Karow-Zwick, A. R., & Blech, M. (2017) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2017.06.029 · Cited by 187
Ahrer, K., Buchacher, A., Iberer, G., & Jungbauer, A. (2006) · Journal of Biochemical and Biophysical Methods · doi:10.1016/j.jbbm.2005.12.003 · Cited by 80
Metadata
- Authors
- Arakawa, T., & Timasheff, S. N.
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 1985
- Volume
- 114
- Pages
- 49-77
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W2218139562
- Cited by
- 367
- References
- 18
- FWCI
- 3.37
- Type
- book chapter
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: [3]Theory of protein solubility. https://app.cochat.ai/papers/10.1016/0076-6879(85)14005-x
- The paper
- Arakawa, T., & Timasheff, S. N. (1985). [3]Theory of protein solubility. Methods in Enzymology. https://doi.org/10.1016/0076-6879(85)14005-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.
