Cited by 2,212Glutathione Transferases and PolymorphismsRedox biology and oxidative stressTrace Elements in Health

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

Zelko, Igor N, Mariani, Thomas J, Folz, Rodney J·2002·Free Radical Biology and Medicine

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1016/s0891-5849(02)00905-x

Cites

160 of 160 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Down's syndrome
Roizen, N., & Patterson, D. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12987-x · Cited by 1,386
Superoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters
Fridovich, I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18515 · Cited by 1,337
Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
Reaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., Wilcox, H. M., Flood, D. G., Beal, M. F., Brown, R. H., et al. (1996) · Nature Genetics · doi:10.1038/ng0596-43 · Cited by 1,285
Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1
Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S., Ohama, E., Reaume, A. G., Scott, R. W., & Cleveland, D. W. (1998) · Science · doi:10.1126/science.281.5384.1851 · Cited by 1,250
Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
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
Role of superoxide dismutase in cancer: a review.
Oberley, L. W., & Buettner, G. R. (1979) · PubMed · Cited by 982
Superoxide dismutases
Fridovich, I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83102-7 · Cited by 970
Mitochondrial Superoxide Dismutase
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43735-6 · Cited by 960
Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism
Wong, G. H. W., & Goeddel, D. V. (1988) · Science · doi:10.1126/science.3263703 · Cited by 914
Aspects of the Structure, Function, and Applications of Superoxide Dismutas
Bannister, J. V., Bannister, W. H., & Rotilio, G. (1987) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238709083738 · Cited by 860
Human copper-containing superoxide dismutase of high molecular weight.
Marklund, S. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.24.7634 · Cited by 749
Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
Wiedau‐Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 720
Superoxide and peroxynitrite inatherosclerosis.
White, C. R., Brock, T. A., Chang, L. Y., Crapo, J. D., BRISCOE, P. M., Ku, D. D., Bradley, W. A., Gianturco, S. H., Gore, J. Z., & Freeman, B. Α. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.1044 · Cited by 684
Trans-acting protein factors and the regulation of eukaryotic transcription: lessons from studies on DNA tumor viruses.Preprint
Jones, N., Rigby, P. W. J., & Ziff, E. B. (1988) · Genes & Development · doi:10.1101/gad.2.3.267 · Cited by 675
Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
Estévez, A. G., Crow, J. P., Sampson, J. B., Reiter, C., Zhuang, Y., Richardson, G. J., Tarpey, M. M., Barbeito, L., & Beckman, J. S. (1999) · Science · doi:10.1126/science.286.5449.2498 · Cited by 596
Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training
Fukai, T., Siegfried, M. R., Ushio‐Fukai, M., Cheng, Y., Kojda, G., & Harrison, D. G. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9551 · Cited by 555
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
Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia.
Carlsson, L. M. S., Jonsson, J., Edlund, H., & Marklund, S. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.14.6264 · Cited by 485
Diverse Roles of the Nuclear Orphan Receptor CAR in Regulating Hepatic Genes in Response to Phenobarbital
Ueda, A., Hamadeh, H. K., Webb, H. K., Yamamoto, Y., Sueyoshi, T., Afshari, C. A., Lehmann, J. M., & Negishi, M. (2002) · Molecular Pharmacology · doi:10.1124/mol.61.1.1 · Cited by 465
Superoxide dismutase in extracellular fluids
Marklund, S. L., Holme, E., & Hellner, L. (1982) · Clinica Chimica Acta · doi:10.1016/0009-8981(82)90360-6 · Cited by 438
Promoters for housekeeping genes
Dynan, W. S. (1986) · Trends in Genetics · doi:10.1016/0168-9525(86)90226-x · Cited by 386
The Interstitium of the Human Arterial Wall Contains Very Large Amounts of Extracellular Superoxide Dismutase
Strålin, P., Karlsson, K., Johansson, B. O., & Marklund, S. L. (1995) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.15.11.2032 · Cited by 386
Superoxide dismutase: The first twenty years (1968–1988)
McCord, J. M., & Fridovich, I. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90109-8 · Cited by 381
The Phenobarbital Response Enhancer Module in the Human Bilirubin Udp–Glucuronosyltransferase Ugt1a1 Gene and Regulation by the Nuclear Receptor Car
Sugatani, J., Kojima, H., Ueda, A., Kakizaki, S., Yoshinari, K., Gong, Q.-H., Owens, I. S., Negishi, M., & Sueyoshi, T. (2001) · Hepatology · doi:10.1053/jhep.2001.24172 · Cited by 377
Regulation of manganese superoxide dismutase by lipopolysaccharide, interleukin-1, and tumor necrosis factor. Role in the acute inflammatory response.
Visner, G. A., Dougall, W. C., Wilson, J. M., Burr, I. A., & Nick, H. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39880-1 · Cited by 376
Reduced Fertility in Female Mice Lacking Copper-Zinc Superoxide Dismutase
Ho, Y.-S., Gargano, M. D., Cao, J., Bronson, R. T., Heimler, I., & Hutz, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7765 · Cited by 333
Human Mn-superoxide dismutase in pulmonary epithelial cells of transgenic mice confers protection from oxygen injury.
Wispé, J. R., Warner, B. B., Clark, J. C., Dey, C. R., Neuman, J. T., Glasser, S. W., Crapo, J. D., Chang, L. Y., & Whitsett, J. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35927-1 · Cited by 314
Upregulation of Superoxide Dismutase and Nitric Oxide Synthase Mediates the Apoptosis-Suppressive Effects of Shear Stress on Endothelial Cells
Dimmeler, S., Hermann, C., Galle, J., & Zeiher, A. M. (1999) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.19.3.656 · Cited by 305
Shear Stress Modulates Expression of Cu/Zn Superoxide Dismutase in Human Aortic Endothelial Cells
Inoue, N., Ramasamy, S., Fukai, T., Nerem, R. M., & Harrison, D. G. (1996) · Circulation Research · doi:10.1161/01.res.79.1.32 · Cited by 299
Preparation for Birth into an O2-Rich Environment: the Antioxidant Enzymes in the Developing Rabbit Lung
Frank, L., & Groseclose, E. E. (1984) · Pediatric Research · doi:10.1203/00006450-198403000-00004 · Cited by 258
Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase.
Levanon, D., Lieman‐Hurwitz, J., Dafni, N., Wigderson, M., Sherman, L., Bernstein, Y., Laver-Rudich, Z., DANCIGER, E., Stein, O. E., & Groner, Y. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb02320.x · Cited by 249
Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes.
Chang, L. Y., Slot, J. W., Geuze, H. J., & Crapo, J. D. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.6.2169 · Cited by 248
Association between manganese superoxide dismutase (MnSOD) gene polymorphism and breast cancer risk
Mitrunen, K. (2001) · Carcinogenesis · doi:10.1093/carcin/22.5.827 · Cited by 244
Tumor Necrosis Factor Alpha and Interleukin-1β Regulate the Murine Manganese Superoxide Dismutase Gene Through a Complex Intronic Enhancer Involving C/EBP-β and NF-κB
Jones, P. L., Ping, D., & Boss, J. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6970 · Cited by 244
Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase.
Hjalmarsson, K., Marklund, S. L., Engström, Å., & Edlund, H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.18.6340 · Cited by 241
Conserved Patterns in the Cu,Zn Superoxide Dismutase Family
Bordo, D., Djinović‐Carugo, K., & Bolognesi, M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1298 · Cited by 230
On signal sequence polymorphisms and diseases of distribution.
Rosenblum, J. S., Gilula, N. B., & Lerner, R. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4471 · Cited by 228
Induction of mitochondrial manganese superoxide dismutase by interleukin 1
Masuda, A., Longo, D. L., Kobayashi, Y., Appella, E., Oppenheim, J. J., & Matsushima, K. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.15.3263930 · Cited by 227
Down's syndrome: Abnormal neuromuscular junction in tongue of transgenic mice with elevated levels of human Cu/Zn-superoxide dismutase
Avraham, K. B., Schickler, M., Sapoznikov, D., Yarom, R., & Groner, Y. (1988) · Cell · doi:10.1016/s0092-8674(88)91153-1 · Cited by 224
10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain.
Sandström, J., Nilsson, P., Karlsson, K., & Marklund, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32289-5 · Cited by 220
Regulation by cytokines of extracellular superoxide dismutase and other superoxide dismutase isoenzymes in fibroblasts.
Marklund, S. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50482-3 · Cited by 213
Molecular Structure and Organization of the Human Manganese Superoxide Dismutase Gene
Wan, X. S., Devalaraja, M. N., & Clair, D. K. S. (1994) · DNA and Cell Biology · doi:10.1089/dna.1994.13.1127 · Cited by 213
Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells.
Keller, G. A., Warner, T. G., Steimer, K. S., & Hallewell, R. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7381 · Cited by 211
Evolution of CuZn superoxide dismutase and the Greek Key β‐barrel structural motif
Getzoff, E. D., Tainer, J. A., Stempien, M. M., Bell, G. I., & Hallewell, R. A. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340050408 · Cited by 209
Modulation of Extracellular Superoxide Dismutase Expression by Angiotensin II and Hypertension
Fukai, T., Siegfried, M. R., Ushio‐Fukai, M., Griendling, K. K., & Harrison, D. G. (1999) · Circulation Research · doi:10.1161/01.res.85.1.23 · Cited by 190
Extracellular Superoxide Dismutase (SOD3): Tissue-Specific Expression, Genomic Characterization, and Computer-Assisted Sequence Analysis of the Human EC SOD Gene
Folz, R. J., & Crapo, J. D. (1994) · Genomics · doi:10.1006/geno.1994.1357 · Cited by 182
Self-citation
Developmental Characteristics of Pulmonary Superoxide Dismutase: Relationship to Idiopathic Respiratory Distress Syndrome
Autor, A. P., Frank, L., & Roberts, R. J. (1976) · Pediatric Research · doi:10.1203/00006450-197603000-00002 · Cited by 178
Redox regulation of manganese superoxide dismutase
Warner, B. B., Stuart, L., Gebb, S. A., & Wispé, J. R. (1996) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1996.271.1.l150 · Cited by 178
Polymorphisms in the SOD2 and HLA-DRB1 Genes Are Associated with Nonfamilial Idiopathic Dilated Cardiomyopathy in Japanese
Hiroi, S., Harada, H., Nishi, H., Satoh, M., Nagai, R., & Kimura, A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1036 · Cited by 177
A comparison of evolutionary rates of the two major kinds of superoxide dismutase
Smith, M., & Doolittle, R. F. (1992) · Journal of Molecular Evolution · doi:10.1007/bf00182394 · Cited by 167
Expression Profiling of the Developing Mouse Lung: Insights into the Establishment of the Extracellular Matrix
Mariani, T. J., Reed, J. J., & Shapiro, S. D. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.5.2001-00080c · Cited by 152
Self-citation
Mouse Extracellular Superoxide Dismutase: Primary Structure, Tissue-specific Gene Expression, Chromosomal Localization, and Lung In Situ Hybridization
Folz, R. J., Guan, J., Seldin, M. F., Oury, T. D., Enghild, J. J., & Crapo, J. D. (1997) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.17.4.2826 · Cited by 150
Self-citation
Manganese superoxide dismutase is induced by IFN-gamma in multiple cell types. Synergistic induction by IFN-gamma and tumor necrosis factor or IL-1
Harris, C., Derbin, K. S., Hunte, B., Krauss, M. R., Chen, K., Smith, D. M., & Epstein, L. B. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.1.149 · Cited by 138
The primary structure of human liver manganese superoxide dismutase.
Barra, D., Schininà, M. E., Simmaco, M., Bannister, J. V., Bannister, W. H., Rotilio, G., & Bossa, F. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90788-x · Cited by 137
Expression of extracellular superoxide dismutase by human cell lines
Marklund, S. L. (1990) · Biochemical Journal · doi:10.1042/bj2660213 · Cited by 132
Expression and Developmental Profile of Antioxidant Enzymes in Human Lung and Liver
Asikainen, T. M., Raivio, K. O., Saksela, M., & Kinnula, V. L. (1998) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.19.6.3248 · Cited by 132
Molecular Structure of a Functional Rat Gene for Manganese-containing Superoxide Dismutase
Ho, Y., Howard, A. J., & Crapo, J. D. (1991) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/4.3.278 · Cited by 131
Mutations in the promoter reveal a cause for the reduced expression of the human manganese superoxide dismutase gene in cancer cells
Xu, Y., Krishnan, A., Wan, X. S., Majima, H. J., Yeh, C., Ludewig, G., Kasarskis, E. J., & Clair, D. K. S. (1999) · Oncogene · doi:10.1038/sj.onc.1202265 · Cited by 129
Manganese Superoxide Dismutase: A Hepatic Acute Phase Protein Regulated by Interleukin-6 and Glucocorticoids*
Dougall, W. C., & Nick, H. S. (1991) · Endocrinology · doi:10.1210/endo-129-5-2376 · Cited by 127
Expression of manganese superoxide dismutase promotes cellular differentiation
Clair, D. K. S., Oberley, T. D., Muse, K. E., & Clair, W. H. S. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90153-8 · Cited by 127
Transcriptional Activation of the Cu,Zn-Superoxide Dismutase Gene through the AP2 Site by Ginsenoside Rb2 Extracted from a Medicinal Plant, Panax ginseng
Kim, Y. H., Park, K. H., & Rhoxy, H. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24539 · Cited by 125
Induction of the rat Cu/Zn superoxide dismutase gene through the peroxisome proliferator-responsive element by arachidonic acid
Yoo, H. Y., Chang, M. S., & Rho, H. M. (1999) · Gene · doi:10.1016/s0378-1119(99)00176-6 · Cited by 121
Superoxide dismutase isoenzymes of the synovial fluid in rheumatoid arthritis and in reactive arthritides.
Marklund, S. L., BJELLE, A. O., & Elmqvist, L.-G. (1986) · Annals of the Rheumatic Diseases · doi:10.1136/ard.45.10.847 · Cited by 121
Role of SOD-1 and nitric oxide/cyclic GMP cascade on neurofilament aggregation in ALS/MND
Chou, S. M., Wang, H. S., & Taniguchi, A. (1996) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(96)00090-1 · Cited by 118
The Activation of the Rat Copper/Zinc Superoxide Dismutase Gene by Hydrogen Peroxide through the Hydrogen Peroxide-responsive Element and by Paraquat and Heat Shock through the Same Heat Shock Element
Yoo, H. Y., Chang, M. S., & Rho, H. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23887 · Cited by 110
Phorbol ester induces manganese-superoxide dismutase in tumor necrosis factor-resistant cells.
Fujii, J., & Taniguchi, N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54474-4 · Cited by 108
Sublocalization of the gene encoding manganese superoxide dismutase (MnSOD/SOD2) to 6q25 by fluorescence in Situ hybridization and somatic cell hybrid mapping
Church, S. L., Grant, J. W., Meese, E. U., & Trent, J. M. (1992) · Genomics · doi:10.1016/s0888-7543(05)80202-2 · Cited by 106
Multiple cytokines regulate the expression of extracellular superoxide dismutase in human vascular smooth muscle cells
Strålin, P., & Marklund, S. L. (2000) · Atherosclerosis · doi:10.1016/s0021-9150(99)00427-x · Cited by 105
Comparison of effects of two polymorphic variants of manganese superoxide dismutase on human breast MCF-7 cancer cell phenotype.
Zhang, H. J., Yan, T., Oberley, T. D., & Oberley, L. W. (1999) · PubMed · Cited by 102
Assignment of the gene for cytoplasmic superoxide dismutase ( Sod-1 ) to a region of chromosome 16 and of Hprt to a region of the X chromosome in the mouse
Francke, U., & Taggart, R. T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.10.5230 · Cited by 99
Extracellular superoxide dismutase deficiency worsens outcome from focal cerebral ischemia in the mouse
Sheng, H., Brady, T. C., Pearlstein, R. D., Crapo, J. D., & Warner, D. S. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00316-x · Cited by 92
Transcriptional Activation of the Human Manganese Superoxide Dismutase Gene Mediated by Tetradecanoylphorbol Acetate
Kim, H., Roe, J., Chock, P. B., & Yim, M. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37455 · Cited by 91
Identification of copper/zinc superoxide dismutase as a nitric oxide-regulated gene in human (HaCaT) keratinocytes: implications for keratinocyte proliferation
FRANK, S., Kämpfer, H., Podda, M., Kaufmann, R., & Pfeilschifter, J. M. (2000) · Biochemical Journal · doi:10.1042/bj3460719 · Cited by 89
Two variants of extracellular‐superoxide dismutase: relationship to cardiovascular risk factors in an unselected middle‐aged population
Marklund, S., Nilsson, P. M., Israelsson, K., Schampi, I., Peltonen, M., & Asplund, K. (1997) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.1997.00160.x · Cited by 88
The Human Copper-Zinc Superoxide Dismutase Gene (SOD1) Proximal Promoter Is Regulated by Sp1, Egr-1, and WT1 via Non-canonical Binding Sites
Minc, E., de Coppet, P., Masson, P., Thiery, L., Dutertre, S., Amor-Guéret, M., & Jaulin, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.503 · Cited by 88
Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression
Perry, A. C. F., Jones, R., & Hall, L. N. (1993) · Biochemical Journal · doi:10.1042/bj2930021 · Cited by 85
On signal sequence polymorphims and diseases of distribution
Macmillan-Crow, L. (1996) · Medical Entomology and Zoology · Cited by 85
Rat lung antioxidant enzymes: differences in perinatal gene expression and regulation
Clerch, L. B., & Massaro, D. (1992) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1992.263.4.l466 · Cited by 84
Regulation of the synthesis of superoxide dismutases in rat lungs during oxidant and hyperthermic stresses.
Hass, M. A., & Massaro, D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)35421-3 · Cited by 81
Cell damage by excess CuZnSOD and down's syndrome
Groner, Y., Elroy-Sterol, O., Avraham, K. B., Schickler, M., Knobler, H. Y., Minc‐Golomb, D., Bar-Peled, O., Yarom, R., & Rotshenker, S. (1994) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(94)90138-4 · Cited by 80
Expression of Copper/Zinc Superoxide Dismutase and Glutathione Peroxidase in Organs of Developing Mouse Embryos, Fetuses, and Neonates
de Haan, J. B., Tymms, M. J., Cristiano, F., & Kola, I. (1994) · Pediatric Research · doi:10.1203/00006450-199402000-00013 · Cited by 80
Distribution of CuZn superoxide dismutase in rat liver
Liou, W., Chang, L., Geuze, H. J., Strous, G. J., CRAPO, J., & Slot, J. W. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90011-i · Cited by 79
Overexpression of copper-zinc superoxide dismutase in trisomy 21
de la Torre, R., Casado, Á., López-Fernández, E., Carrascosa, D., Ramírez, V., & Sáez, J. (1996) · Cellular and Molecular Life Sciences · doi:10.1007/bf01938872 · Cited by 77
ADP-ribosylation of p53 tumor suppressor protein: Mutant but not wild-type p53 is modified
Węsierska‐Gądek, J., Bugajska-Schretter, A., & Cerni, C. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(199607)62:1 · Cited by 76
Study of 5′-Flanking Region of Human Cu/Zn Superoxide Dismutase
Kim, H. T., Kim, Y. H., Nam, J. W., Lee, H. J., Rho, H. M., & Jung, G. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1877 · Cited by 75
Catalase, superoxide dismutase and glutathione peroxidase activities of lung and liver during human development
McElroy, M., Postle, A. D., & Kelly, F. J. (1992) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(92)90073-4 · Cited by 75
Regulation of the Manganese Superoxide Dismutase and Inducible Nitric Oxide Synthase Gene in Rat Neuronal and Glial Cells
Kifle, Y., Monnier, J. M., Chesrown, S. E., Raizada, M. K., & Nick, H. S. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66052128.x · Cited by 75
Manganese‐containing superoxide dismutase signal sequence polymorphism associated with sporadic motor neuron disease
van Landeghem, G. F., Tabatabaie, P., Beckman, G., Beckman, L. E., & Andersen, P. M. (1999) · European Journal of Neurology · doi:10.1046/j.1468-1331.1999.660639.x · Cited by 75
A Family of AP-2 Proteins Down-regulate Manganese Superoxide Dismutase Expression
Zhu, C., Huang, Y., Oberley, L. W., & Domann, F. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009708200 · Cited by 74
Cloning and characterization of the murine manganous superoxide dismutase-encoding gene
Jones, P. L., Kucera, G., Gordon, H., & Boss, J. M. (1995) · Gene · doi:10.1016/0378-1119(94)00666-g · Cited by 74
Tumor necrosis factor-alpha increases Mn-SOD expression: protection against oxidant injury
Warner, B. B., Burhans, M. S., Clark, J. C., & Wispé, J. R. (1991) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1991.260.4.l296 · Cited by 73
Identification of a homozygous missense mutation (Arg to Gly) in the critical binding region of the human EC-SOD gene (SOD3) and its association with dramatically increased serum enzyme levels
Folz, R. J., Peno-Green, L. A., & Crapo, J. D. (1994) · Human Molecular Genetics · doi:10.1093/hmg/3.12.2251 · Cited by 72
Self-citation
Regulation of manganese superoxide dismutase: IL-1 and TNF induction in pulmonary artery and microvascular endothelial cells
Visner, G. A., Chesrown, S. E., Monnier, J. M., Ryan, U. S., & Nick, H. S. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)92406-n · Cited by 71
Erratic overdispersion of three molecular clocks: GPDH, SOD, and XDH
Rodrı́guez-Trelles, F., Tarrı́o, R., & Ayala, F. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201392198 · Cited by 71
Rat lung antioxidant enzyme induction by ozone
Rahman, I., Clerch, L. B., & Massaro, D. (1991) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1991.260.6.l412 · Cited by 70
Prenatal Development of Antioxidant Enzymes in Rat Lung, Kidney, and Heart: Marked Increase in Immunoreactive Superoxide Dismutases, Glutathione Peroxidase, and Catalase in the Kidney
Hayashibe, H., Asayama, K., Dobashi, K., & Kato, K. (1990) · Pediatric Research · doi:10.1203/00006450-199005000-00011 · Cited by 69
Decreased Expression of Manganese Superoxide Dismutase in Transformed Cells Is Associated with Increased Cytosine Methylation of the SOD2 Gene
Huang, Y., He, T., & Domann, F. E. (1999) · DNA and Cell Biology · doi:10.1089/104454999315051 · Cited by 69
Molecular Manipulations of Extracellular Superoxide Dismutase: Functional Importance for Learning
Levin, E. D., Brady, T. C., Hochrein, E. C., Oury, T. D., Jonsson, L. M., Marklund, S. L., & Crapo, J. D. (1998) · Behavior Genetics · doi:10.1023/a:1021673703129 · Cited by 68
Extracellular superoxide dismutase is upregulated with inducible nitric oxide synthase after NF-κB activation
Brady, T. C., Chang, L., Day, B. J., & Crapo, J. D. (1997) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1997.273.5.l1002 · Cited by 66
Chromosome assignments of genes in man using mouse-human somatic cell hybrids: Mitochondrial superoxide dismutase (indophenol oxidase-B, tetrameric) to chromosome 6
Creagan, R. P., Tischfield, J. A., Ricciuti, F., & Ruddle, F. H. (1973) · Human Genetics · doi:10.1007/bf00385731 · Cited by 63
Solar simulated irradiation modulates gene expression and activity of antioxidant enzymes in cultured human dermal fibroblasts
Leccia, M. ‐., Yaar, M., Allen, N., Gleason, M. J., & Gilchrest, B. A. (2001) · Experimental Dermatology · doi:10.1034/j.1600-0625.2001.100407.x · Cited by 61
Heavy metal-mediated activation of the rat Cu/Zn superoxide dismutase gene via a metal-responsive element
Yoo, H. Y., Chang, M. S., & Rho, H. M. (1999) · Molecular and General Genetics MGG · doi:10.1007/s004380051088 · Cited by 59
Manganese Superoxide Dismutase
Whittaker, J. W. (2000) · CRC Press eBooks · doi:10.1201/9781482289893-28 · Cited by 59
Ontogeny of Antioxidant Enzymes in the Fetal Lamb Lung
Walther, F. J., Wade, A. B., Warburton, D., & Forman, H. J. (1991) · Experimental Lung Research · doi:10.3109/01902149109063280 · Cited by 57
Secretion of extracellular superoxide dismutase in neonatal lungs
Nozik‐Grayck, E., Dieterle, C. S., Piantadosi, C. A., Enghild, J. J., & Oury, T. D. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.5.l977 · Cited by 57
Regulation of copper/zinc and manganese superoxide dismutase by UVB irradiation, oxidative stress and cytokines
Isoherranen, K., Peltola, V. T., Laurikainen, L., Punnonen, J., Laihia, J. K., Ahotupa, M. O., & Punnonen, K. R. A. (1997) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(97)00071-7 · Cited by 54
Spl and C/EBP-related factor regulate the transcription of human Cu/Zn SOD gene
Seo, S., Kim, H. T., Cho, G., Rho, H. M., & Jung, G. (1996) · Gene · doi:10.1016/0378-1119(96)00383-6 · Cited by 54
Transcriptional Inhibition of Manganese Superoxide Dismutase (SOD2) Gene Expression by DNA Methylation of the 5′ CpG Island
Huang, Y., Peng, J., Oberley, L. W., & Domann, F. E. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00095-6 · Cited by 52
Localization of Extracellular Superoxide Dismutase in Rat Lung: Neutrophils and Macrophages as Carriers of the Enzyme
Loenders, B., Mechelen, E. V., Nicoläı, S., Buyssens, N., Osselaer, N. V., Jorens, P. G., Willems, J., Herman, A. G., & Slegers, H. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00434-6 · Cited by 52
Protein Kinase Cδ-dependent Induction of Manganese Superoxide Dismutase Gene Expression by Microtubule-active Anticancer Drugs
Das, K. C., Guo, X., & White, C. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34639 · Cited by 52
Identification and Functional Characterization of the Bovine Manganous Superoxide Dismutase Promoter
Meyrick, B. O., & Magnuson, M. A. (1994) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.10.1.8292376 · Cited by 52
Vasoactive factors and growth factors alter vascular smooth muscle cell EC-SOD expression
Strålin, P., & Marklund, S. L. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.4.h1621 · Cited by 50
Analysis of genes differentially expressed in astrocytes stimulated with lipopolysaccharide using cDNA arrays
Pang, Y., Cai, Z., & Rhodes, P. G. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02766-4 · Cited by 45
Effects of hypoxia on expression of superoxide dismutases in cultured ATII cells and lung fibroblasts
Jackson, R. M., Parish, G., & Ho, Y. (1996) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1996.271.6.l955 · Cited by 45
Regional localization of human extracellular superoxide dismutase gene to 4pter-q21
Hendrickson, D. J., Fisher, J. H., Jones, C., & Ho, Y. (1990) · Genomics · doi:10.1016/0888-7543(90)90264-u · Cited by 43
Transcriptional Regulation of the 5′ Proximal Promoter of the Human Manganese Superoxide Dismutase Gene
Yeh, C., Wan, X. S., & Clair, D. K. S. (1998) · DNA and Cell Biology · doi:10.1089/dna.1998.17.921 · Cited by 43
Early growth responsive‐1‐dependent manganese superoxide dismutase gene transcription mediated by platelet‐derived growth factor
Maehara, K., Oh‐hashi, K., & Isobe, K. (2001) · The FASEB Journal · doi:10.1096/fj.00-0909fje · Cited by 43
Purification and sequence of rat extracellular superoxide dismutase B secreted by C6 glioma.
Willems, J., Zwijsen, A., Slegers, H., Nicoläı, S., Bettadapura, J., Raymackers, J., & Scarcez, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74510-4 · Cited by 41
Studies on the expression of Cu,Zn superoxide dismutase in human tissues during development
Strange, R. C., Cotton, W., Fryer, A. A., Drew, R., Bradwell, A. R., Marshall, T., Collins, M. F., Bell, J. E., & Hume, R. (1988) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(88)90174-2 · Cited by 41
Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum
Yamada, H., Yamada, Y., Adachi, T., Goto, H., Ogasawara, N., Futenma, A., Kitano, M., Hirano, K., & Kato, K. (1995) · The Japanese Journal of Human Genetics · doi:10.1007/bf01883574 · Cited by 39
Rat Testicular Extracellular Superoxide Dismutase: Its Purification, Cellular Distribution, and Regulation1
Mruk, D. D., Cheng, C.-H., Cheng, Y.-H., Mo, M., Grima, J., Silvestrini, B., Lee, W. M., & Cheng, C. Y. (1998) · Biology of Reproduction · doi:10.1095/biolreprod59.2.298 · Cited by 39
Mutation screening of manganese superoxide dismutase in amyotrophic lateral sclerosis
Tomkins, J., Banner, S. J., McDermott, C. J., & Shaw, P. J. (2001) · Neuroreport · doi:10.1097/00001756-200108080-00008 · Cited by 38
The 3‘ Untranslated Region of Manganese Superoxide Dismutase RNA Contains a Translational Enhancer Element
Chung, D. J., Wright, A. E., & Clerch, L. B. (1998) · Biochemistry · doi:10.1021/bi980935g · Cited by 38
Distribution of MnSOD polymorphisms in sporadic ALS patients
Tomblyn, M. B., Kasarskis, E. J., Xu, Y., & Clair, D. K. S. (1998) · Journal of Molecular Neuroscience · doi:10.1007/bf02737086 · Cited by 36
Age-related change of plasma extracellular-superoxide dismutase
Adachi, T., Wang, J., & Wang, X. L. (2000) · Clinica Chimica Acta · doi:10.1016/s0009-8981(99)00187-4 · Cited by 36
Tyrosine Phosphorylation Regulates Manganese Superoxide Dismutase (MnSOD) RNA-Binding Protein Activity and MnSOD Protein Expression
Knirsch, L., & Clerch, L. B. (2001) · Biochemistry · doi:10.1021/bi010197n · Cited by 35
Cytokine-inducible enhancer with promoter activity in both the rat and human manganese-superoxide dismutase genes
Rogers, R. J., Chesrown, S. E., Kuo, S., Monnier, J. M., & Nick, H. S. (2000) · Biochemical Journal · doi:10.1042/bj3470233 · Cited by 33
Developmental regulation of rat lung Cu,Zn-superoxide dismutase
Hass, M. A., & Massaro, D. (1987) · Biochemical Journal · doi:10.1042/bj2460697 · Cited by 32
Polymorphism of extracellular superoxide dismutase (EC-SOD) gene: relation to the mutation responsible for high EC-SOD level in serum
Yamada, H., Yamada, Y., Adachi, T., Goto, H., Ogasawara, N., Futenma, A., Kitano, M., Miyai, H., Fukatsu, A., HIRANO, K., et al. (1997) · The Japanese Journal of Human Genetics · doi:10.1007/bf02766958 · Cited by 32
Isolation and analysis of the mouse genomic sequence encoding Cu2+-Zn2+ Superoxide dismutase
Benedetto, M. T., Anzai, Y., & Gordon, J. W. (1991) · Gene · doi:10.1016/0378-1119(91)90126-v · Cited by 30
Differential patterns of antioxidant enzyme mRNA expression in guinea pig lung and liver during development
Yuan, H. T., Bingle, C. D., & Kelly, F. J. (1996) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(95)00214-6 · Cited by 30
Association of extracellular‐superoxide dismutase phenotype with the endothelial constitutive nitric oxide synthase polymorphism
Adachi, T., & Wang, X. L. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00903-x · Cited by 28
Isolation and analysis of the rat genomic sequence encoding Cu/Zn Superoxide dismutase
Kim, Y. H., Yoo, H. Y., Guhung, J., Ji-Young, K., & Rho, H. M. (1993) · Gene · doi:10.1016/0378-1119(93)90650-r · Cited by 28
In Vivo Architecture of the Manganese Superoxide Dismutase Promoter
Kuo, S., Chesrown, S. E., Mellott, J. K., Rogers, R. J., Hsu, J.-L., & Nick, H. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3345 · Cited by 28
Characterization of the 5′ Flanking Region of the Human MnSOD Gene
Zhang, N. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0376 · Cited by 28
Induction of Superoxide Dismutase and Cytotoxicity by Manganese In Human Breast Cancer Cells
Thongphasuk, J., Oberley, L. W., & Oberley, T. D. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1179 · Cited by 28
Genetic polymorphisms of superoxide dismutase in Parkinson's disease
Farin, F. M., Hitosis, Y., Hallagan, S. E., Kushleika, J. V., Woods, J. S., Janssen, P. S., Smith‐Weller, T., Franklin, G. M., Swanson, P. D., & Checkoway, H. (2001) · Movement Disorders · doi:10.1002/mds.1153 · Cited by 27
Absence of mutations in the Mn superoxide dismutase or catalase genes in familial amyotrophic lateral sclerosis
Parboosingh, J. S., Rouleau, G. A., Meninger, V., McKenna-Yasek, D. M., Brown, R. H., & Figlewicz, D. A. (1995) · Neuromuscular Disorders · doi:10.1016/0960-8966(94)e0022-z · Cited by 27
A Region in the 3′ UTR of MnSOD RNA Enhances Translation of a Heterologous RNA
Knirsch, L., & Clerch, L. B. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2754 · Cited by 25
Xenobiotic-Responsive Element for the Transcriptional Activation of the Rat Cu/Zn Superoxide Dismutase Gene
Yoo, H. Y., Chang, M. S., & Rho, H. M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0299 · Cited by 24
C/EBPα is a major activator for the transcription of rat Cu/Zn superoxide dismutase gene in liver cell
Kim, Y. H., Yoo, H. Y., Chang, M. S., Jung, G., & Rho, H. M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01487-1 · Cited by 23
Structure and DNA sequence of the mouse MnSOD gene
DiSilvestre, D. A., Kleeberger, S. R., Johns, J., & Levitt, R. C. (1995) · Mammalian Genome · doi:10.1007/bf00352417 · Cited by 22
Perinatal Development of Heart, Kidney, and Liver Mitochondrial Antioxidant Defense
Vlessis, A. A., & Mela-Riker, L. M. (1989) · Pediatric Research · doi:10.1203/00006450-198909000-00013 · Cited by 21
Induction of two species of superoxide dismutase in some organs of rats by low dose X-irradiation.
Yamaoka, K., Sato, E., & Utsumi, K. (1994) · PubMed · Cited by 21
Induction of pulmonary Mn superoxide dismutase mRNA by interleukin-1
White, J. E., & Tsan, M. F. (1994) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1994.266.6.l664 · Cited by 20
C/EBPα and C/EBPβ play similar roles in the transcription of the human Cu/Zn SOD gene
Seo, S., Kang, S. S., Cho, G., Rho, H. M., & Jung, G. (1997) · Gene · doi:10.1016/s0378-1119(97)00484-8 · Cited by 19
Transcriptional activation of the human Cu/Zn superoxide dismutase gene by 2,3,7,8-tetrachlorodibenzo-p-dioxin through the xenobiotic-responsive element
Cho, J., Chang, M., & Rho, H. M. (2001) · Molecular Genetics and Genomics · doi:10.1007/s004380100536 · Cited by 19
Tissue-specific developmental regulation of superoxide dismutase (SOD-1 and SOD-2) activities in genetic strains of mice
Schisler, N. J., & Singh, S. M. (1985) · Biochemical Genetics · doi:10.1007/bf00504326 · Cited by 19
Rat copper/zinc superoxide dismutase gene: Isolation, characterization, and species comparison
Hsu, J.-L., Visner, G. A., Burr, I. A., & Nick, H. S. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90836-a · Cited by 19
Expression of Manganese Superoxide Dismutase in Ovine Kidney Cortex during Development
Carbone, G. M., Clair, D. K. S., Xu, Y. A., & Rose, J. C. (1994) · Pediatric Research · doi:10.1203/00006450-199401000-00010 · Cited by 14
Cyclic amp-induced differentiation increases the synthesis of extracellular superoxide dismutase in rat c6 glioma
Nicoläı, S., Willems, J., Zwijsen, A., Mechelen, E. V., & Slegers, H. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)00122-0 · Cited by 13
The transcriptional repression of the human Cu/Zn superoxide dismutase(sod1) gene by the aticancer drugg, mitocycin C(MMC)
Cho, G., Sang-Sun, K., Seo, S., Kim, Y., & Jung, G. (1997) · IUBMB Life · doi:10.1080/15216549700203391 · Cited by 12
Effect of Epidermal Growth Factor on Cu, Zn-Superoxide Dismutase Expression in Cultured Fibroblasts from Rat Skin
Nishiguchi, K., Kiyohara, Y., Komada, F., Iwakawa, S., & Okumura, K. (1994) · Pharmaceutical Research · doi:10.1023/a:1018978024740 · Cited by 10
Regulation of superoxide dismutase in primary cultures of rat colonic smooth muscle cells
Tannahill, C. L., Stevenot, S., Eaker, E. Y., Sallustio, J. E., Nick, H. S., & Valentine, J. F. (1997) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1997.272.5.g1230 · Cited by 10
Physical mapping of SOD1 to bovine chromosome 1
Schmutz, S. M., Cornwell, D. L., Moker, J. S., & Troyer, D. L. (2008) · Cytogenetics and Cell Genetics · doi:10.1159/000134156 · Cited by 7
[Induction of manganese superoxide dismutase by an immunopotentiator as a mechanism of inhibiting of malignant progression of murine tumor cells].
Habelhah, H. (1998) · PubMed · Cited by 5
Sequence Analysis, Tissue Expression and Chromosomal Localization of a Mouse Secreted Superoxide Dismutase Gene
Suh, J., Takai, S., Yamanishi, T., Kikuchi, T., Folz, R. J., Tanaka, K., Oh, Y., & Wada, K. (1997) · Molecules and Cells · doi:10.1016/s1016-8478(23)13281-x · Cited by 4
Self-citation

Research works printed but not linked: 3

Oberley, 1979, Role of superoxide dismutase in cancer, Cancer Res., 39, 1141
Clerch, 1992, Rat lung antioxidant enzymes, Am. J. Physiol., 263, L466
Warner, 1991, Tumor necrosis factor-alpha increases Mn-SOD expression, Am. J. Physiol., 260, L296

Sorted by citations

Copper-Zinc Superoxide Dismutase (SOD1) Is Released by Microglial Cells and Confers Neuroprotection against 6-OHDA Neurotoxicity
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

See all 2,212

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
ORCID: Zelko, Igor N
Mariani, Thomas J
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)
DOI: 10.1016/s0891-5849(02)00905-x
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks