The DOI matches its Crossref record; 160 of the 162 references it cites were found in a registry or an index.
Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
Abstract
Superoxide dismutases are an ubiquitous family of enzymes that function to efficiently catalyze the dismutation of superoxide anions. Three unique and highly compartmentalized mammalian superoxide dismutases have been biochemically and molecularly characterized to date. SOD1, or CuZn-SOD (EC 1.15.1.1), was the first enzyme to be characterized and is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. SOD3, or EC-SOD (EC 1.15.1.1), is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. What role(s) these SODs play in both normal and disease states is only slowly beginning to be understood. A molecular understanding of each of these genes has proven useful toward the deciphering of their biological roles. For example, a variety of single amino acid mutations in SOD1 have been linked to familial amyotrophic lateral sclerosis. Knocking out the SOD2 gene in mice results in a lethal cardiomyopathy. A single amino acid mutation in human SOD3 is associated with 10 to 30-fold increases in serum SOD3 levels. As more information is obtained, further insights will be gained.
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“This enzyme catalyzes the dismutation of superoxide anion radical very effectively by a “Ping Pong” mechanism with remarkably high reaction rates according to the reaction (Zelko et al. 2002)12”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Zelko et al. 2002
In the citing paper
“There are three main forms of superoxide dismutase present in humans, Cu, Zn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) (Zelko et al. 2002).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Zelko et al. 2002
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Cites
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Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
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Polazzi, E., Mengoni, I., Caprini, M., Peña‐Altamira, E., Kurtys, E., & Monti, B. (2012) · Neurosignals · doi:10.1159/000337115 · Cited by 9,023
Free radicals, antioxidants and functional foods: impact on human health
Lobo, V, Patil, A., Phatak, A., & Chandra, N. (2010) · Pharmacognosy Reviews · doi:10.4103/0973-7847.70902 · Cited by 5,435
Oxidative Stress and Antioxidant Defense
Birben, E., Şahiner, Ü. M., Saçkesen, C., ERZURUM, S. C., & Kalaycı, Ö. (2012) · World Allergy Organization Journal · doi:10.1097/wox.0b013e3182439613 · Cited by 5,190
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases
Fukai, T., & Ushio‐Fukai, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3999 · Cited by 2,074
Metadata
- Authors
- Zelko, I. N., Mariani, T. J., & Folz, R. J.
- Affiliations
- Duke University (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Folz, Rodney J
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2002-08
- Volume
- 33
- Issue
- 3
- Pages
- 337-349
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2104109524
- Cited by
- 2,212
- References
- 162
- Citations by year
- 2026: 77 · 2025: 123 · 2024: 119 · 2023: 109 · 2022: 131 · 2021: 140 · 2020: 117 · 2019: 130 · 2018: 134 · 2017: 133 · 2016: 124 · 2015: 93 · 2014: 103 · 2013: 99 · 2012: 104
- FWCI
- 12.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl055166-04)
- National Heart, Lung, and Blood Institute (HL55166, P01HL031992, HL 31992)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- superoxide dismutase, SOD1, manganese superoxide dismutase, SOD3, gene structure, gene evolution, gene expression, SOD1 mutations, amyotrophic lateral sclerosis, superoxide dismutase isoforms
- MeSH terms
- Animals, Multigene Family, Humans, Superoxide Dismutase, Gene Expression Regulation, Enzymologic, Evolution, Molecular
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