The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Energetics of enzyme catalysis.
Open accessAbstract
Quantitative studies of the energetics of enzymatic reactions and the corresponding reactions in aqueous solutions indicate that charge stabilization is the most important energy contribution in enzyme catalysis. Low electrostatic stabilization in aqueous solutions is shown to be consistent with surprisingly large electrostatic stabilization effects in active sites of enzymes. This is established quantitatively by comparing the relative stabilization of the transition states of the reaction of lysozyme and the corresponding reaction is aqueous solution.
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Cites
Warshel, A., & Levitt, M. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90311-9 · Cited by 4,479
Self-citationPERUTZ, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,926
Enzyme structure and mechanism
Fersht, A. (1977) · Medical Entomology and Zoology · Cited by 2,875
Catalysis in micellar and macromolecular systems
Fendler, J. H., & Fendler, E. J. (2012) · Cited by 1,079
Page, M. I., & Jencks, W. P. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.8.1678 · Cited by 1,014
Crystallographic studies of the activity of hen egg-white lysozyme
Blake, C. C. F., Johnson, L. N., Mair, G. A., North, A. C. T., Phillips, D. C., & Sarma, V. R. (1967) · Proceedings of the Royal Society of London. Series B. Biological Sciences · doi:10.1098/rspb.1967.0035 · Cited by 656
Subtilisin. Stereochemical mechanism involving transition-state stabilization
Robertus, J. D., Kraut, J., Alden, R. A., & Birktoft, J. J. (1972) · Biochemistry · doi:10.1021/bi00773a016 · Cited by 377
Moras, D., Olsen, K. W., Sabesan, M. N., Buehner, M., Ford, G. C., & Rossmann, M. G. (1977) · Worldwide Protein Data Bank · doi:10.2210/pdb1gpd/pdb · Cited by 329
Kester, W. R., & Matthews, B. W. (1977) · Biochemistry · doi:10.1021/bi00630a030 · Cited by 238
Mechanism of tertiary structural change in hemoglobin.
Gelin, B. R., & Karplus, M. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.3.801 · Cited by 217
Cited by
Electrostatic Basis for Enzyme Catalysis
Warshel, A., Sharma, P. K., Kato, M., Xiang, Y., Liu, H., & Olsson, M. H. M. (2006) · Chemical Reviews · doi:10.1021/cr0503106 · Cited by 1,444
Self-citationA relationship between protein stability and protein function.
Shoichet, B. K., Baase, W. A., Kuroki, R., & Matthews, B. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.2.452 · Cited by 709
Theoretical Methods for the Description of the Solvent Effect in Biomolecular Systems
Orozco, M., & Luque, F. J. (2000) · Chemical Reviews · doi:10.1021/cr990052a · Cited by 622
Extreme electric fields power catalysis in the active site of ketosteroid isomerase
Fried, S. D., Bagchi, S., & Boxer, S. G. (2014) · Science · doi:10.1126/science.1259802 · Cited by 554
Legler, G. (1990) · Advances in Carbohydrate Chemistry and Biochemistry · doi:10.1016/s0065-2318(08)60034-7 · Cited by 553
Metadata
- Authors
- Warshel, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1978-11
- Volume
- 75
- Issue
- 11
- Pages
- 5250-5254
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2050357762
- Cited by
- 485
- References
- 10
- FWCI
- 14.10
- Type
- journal article
- Language
- en
- Open access
- green
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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.
