The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Superoxide radical and superoxide dismutase
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSuperoxide radical and superoxide dismutaseIrwin FridovichCite this: Acc. Chem. Res. 1972, 5, 10, 321–326Publication Date (Print):October 1, 1972Publication History Published online1 May 2002Published inissue 1 October 1972https://pubs.acs.org/doi/10.1021/ar50058a001https://doi.org/10.1021/ar50058a001research-articleACS PublicationsRequest reuse permissionsArticle Views1271Altmetric-Citations384LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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Citations
Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citationMisra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45228-9 · Cited by 9,097
Self-citationThe Reduction of Cytochrome c by Milk Xanthine Oxidase
McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,197
Self-citationThe Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44679-6 · Cited by 1,174
Self-citationAn Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase
McCord, J. M., Keele, B. B., & Fridovich, I. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1024 · Cited by 973
Self-citationSuperoxide Dismutase from Escherichia coli B
Keele, B. B., McCord, J. M., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62675-4 · Cited by 559
Self-citationThe Utility of Superoxide Dismutase in Studying Free Radical Reactions
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63505-7 · Cited by 557
Self-citationAcid dissociation constant and decay kinetics of the perhydroxyl radical
Behar, D., Czapski, G., Rabani, J., Dorfman, L. M., & Schwarz, H. A. (1970) · The Journal of Physical Chemistry · doi:10.1021/j100711a009 · Cited by 499
Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M., & Sullivan, P. A. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90287-3 · Cited by 426
The Utility of Superoxide Dismutase in Studying Free Radical Reactions
McCord, J. M., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63246-6 · Cited by 388
Self-citationKnowles, P. F., Gibson, J. F., Pick, F. M., & Bray, R. C. (1969) · Biochemical Journal · doi:10.1042/bj1110053 · Cited by 244
Ballou, D., Palmer, G., & Massey, V. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90288-5 · Cited by 223
Haemocuprein and hepatocuprein, copper-protein compounds of blood and liver in mammals
Mann, T., & Keilin, D. (1938) · Proceedings of the Royal Society of London. Series B - Biological Sciences · doi:10.1098/rspb.1938.0058 · Cited by 216
Further Characterization of Bovine Superoxide Dismutase and Its Isolation from Bovine Heart
Keele, B. B., McCord, J. M., & Fridovich, I. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62263-x · Cited by 203
Self-citationStrobel, H. W., & Coon, M. J. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45853-5 · Cited by 189
Fridovich, I., & Handler, P. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60393-x · Cited by 188
Self-citationFridovich, I., & Handler, P. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63312-0 · Cited by 175
Self-citationTHE REDUCTION OF CYTOCHROME c BY XANTHINE OXIDASE
Horecker, B. L., & HEPPEL, L. A. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56885-x · Cited by 139
Isolation of Human Hepatocuprein and Cerebrocuprein
Carrico, R. J., & DEUTSCH, H. F. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63509-4 · Cited by 126
The Presence of Zinc in Human Cytocuprein and Some Properties of the Apoprotein
Carrico, R. J., & DEUTSCH, H. F. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63323-x · Cited by 115
Chemiluminescence Induced by Operation of Iron-Flavoproteins*
Greenlee, L. L., Fridovich, I., & Handler, P. (1962) · Biochemistry · doi:10.1021/bi00911a008 · Cited by 109
Self-citationOrme‐Johnson, W. H., & Beinert, H. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90289-7 · Cited by 105
Markowitz, H., Cartwright, G. E., & Wintrobe, M. M. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70331-1 · Cited by 100
Fridovich, I., & Handler, P. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49375-1 · Cited by 98
Self-citationPossible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
Hirata, F., & Hayaishi, O. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45852-3 · Cited by 81
CEREBROCUPREIN I. A COPPER‐CONTAINING PROTEIN ISOLATED FROM BRAIN
Porter, H., Folch, J., Beggrovs, J., et al. (1957) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1957.tb12081.x · Cited by 81
Preparation of Crystalline Erythrocuprein and Catalase from Human Erythrocytes
Stansell, M. J., & DEUTSCH, H. F. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97059-6 · Cited by 80
Some Chemical and Physical Properties of Erythrocuprein
KIMMEL, J. R., Markowitz, H., & Brown, D. M. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70332-3 · Cited by 76
On the Sonochemical Formation of Hydrogen Peroxide in Water
Anbar, M., & Pecht, I. (1964) · The Journal of Physical Chemistry · doi:10.1021/j100784a025 · Cited by 75
Competitive Inhibition by Myoglobin of the Reduction of Cytochrome c by Xanthine Oxidase
Fridovich, I. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93966-9 · Cited by 63
Self-citationPreparation and Physicochemical Properties of Human Erythrocuprein
Hartz, J. W., & DEUTSCH, H. F. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93663-x · Cited by 59
Reactions of superoxide anion, catechols, and cytochrome c
Miller, R. W. (1970) · Canadian Journal of Biochemistry · doi:10.1139/o70-145 · Cited by 57
ISOLATION OF PURIFIED COPPER PROTEIN FROM HORSE LIVER
Mohamed, M. S., & Greenberg, D. M. (1954) · The Journal of General Physiology · doi:10.1085/jgp.37.4.433 · Cited by 49
Forman, H. J., & Fridovich, I. (1972) · Science · doi:10.1126/science.175.4019.339 · Cited by 43
Self-citationA Reversible Association of Bovine Carbonic Anhydrase with Milk Xanthine Oxidase
Fridovich, I. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96112-0 · Cited by 24
Self-citation
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Radi, R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804932115 · Cited by 1,142
Mitochondrial role in cell aging
Miquel, J., Economos, A. C., Fleming, J., & Johnson, J. E. (1980) · Experimental Gerontology · doi:10.1016/0531-5565(80)90010-8 · Cited by 936
Photosensitized Oxidation and Singlet Oxygen: Consequences in Biological Systems
Foote, C. S. (1976) · Free Radicals in Biology · doi:10.1016/b978-0-12-566502-5.50010-x · Cited by 820
The inactivation of Fe-S cluster containing hydro-lyases by superoxide
Flint, D. H., Tuminello, J. F., & Emptage, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41538-4 · Cited by 637
Zielonka, J., & Kalyanaraman, B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.028 · Cited by 531
Metadata
- Authors
- Fridovich, I.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 1972-10-01
- Volume
- 5
- Issue
- 10
- Pages
- 321-326
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2570983626
- Cited by
- 469
- References
- 35
- FWCI
- 15.43
- Type
- journal article
- Language
- en
- Open access
- closed
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