The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Superoxide Dismutases
Abstract
This chapter contains sections titled: Introduction Assays Isoenzymes and Electromorphs Structure and Evolutionary Relationships Mechanisms Biosynthesis Conclusions
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Citations
Cites
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Self-citationWeisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43969-0 · Cited by 895
Self-citationA simplified assay method of superoxide dismutase activity for clinical use
Masayasu, M., & Hiroshi, Y. (1979) · Clinica Chimica Acta · doi:10.1016/0009-8981(79)90211-0 · Cited by 557
Electrostatic recognition between superoxide and copper, zinc superoxide dismutase
Getzoff, E. D., Tainer, J. A., Weiner, P. K., Kollman, P. A., Richardson, J. S., & Richardson, D. C. (1983) · Nature · doi:10.1038/306287a0 · Cited by 554
Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
Cudd, A., & Fridovich, I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33779-7 · Cited by 211
Self-citationChemistry of superoxide ion. II. Reaction with hydroperoxides
Peters, J. W., & Foote, C. S. (1976) · Journal of the American Chemical Society · doi:10.1021/ja00419a058 · Cited by 78
Cited by
Fish bioaccumulation and biomarkers in environmental risk assessment: a review
van der Oost, R., Beyer, J., & Vermeulen, N. P. E. (2003) · Environmental Toxicology and Pharmacology · doi:10.1016/s1382-6689(02)00126-6 · Cited by 4,895
Role of superoxide dismutases (SODs) in controlling oxidative stress in plants
Alscher, R. G. (2002) · Journal of Experimental Botany · doi:10.1093/jexbot/53.372.1331 · Cited by 2,771
Lebovitz, R. M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N., Huang, S., & Matzuk, M. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9782 · Cited by 1,023
Groundworks for an evolutionary biochemistry: The iron-sulphur world
Wächtershäuser, G. (1992) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(92)90022-x · Cited by 677
Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells.
Crapo, J. D., Oury, T., Rabouille, C., Slot, J. W., & Chang, L. Y. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10405 · Cited by 503
Metadata
- Authors
- Fridovich, I.
- Venue
- Advances in Enzymology - and Related Areas of Molecular Biology
- Publisher
- Wiley
- Published
- 1986-01
- Volume
- 58
- Pages
- 61-97
- ISSN
- 0065-258X (ISSN-L)
- 1934-4694
- OpenAlex
- W4211087088
- Cited by
- 468
- References
- 6
- Type
- other
- Language
- en
- Open access
- closed
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How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
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- CoChat. (2026). Citation check: Superoxide Dismutases. https://app.cochat.ai/papers/10.1002/9780470123041.ch2
- The paper
- Fridovich, I. (1986). Superoxide Dismutases. Advances in Enzymology - and Related Areas of Molecular Biology. https://doi.org/10.1002/9780470123041.ch2
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.
