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

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 · see citing works

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 · see citing works

Superoxide radical and superoxide dismutases

Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455 · see citing works

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 · see citing works

Down's syndrome

Roizen, N., & Patterson, D. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12987-x · Cited by 1,333 · see citing works

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 · see citing works

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 1,231 · see citing works

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 · see citing works

Role of superoxide dismutase in cancer: a review.

Oberley, L. W., & Buettner, G. R. (1979) · PubMed · Cited by 982 · see citing works

Superoxide dismutases

Fridovich, I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83102-7 · Cited by 964 · see citing works

Mitochondrial Superoxide Dismutase

Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43735-6 · Cited by 960 · see citing works

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 · see citing works

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 856 · see citing works

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 · see citing works

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 · see citing works

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 685 · see citing works

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 · see citing works

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 · see citing works

Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training

Fukai, T., Siegfried, M. R., Ushio‐Fukai, M., Cheng, Y. C., Kojda, G., & Harrison, D. G. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9551 · Cited by 552 · see citing works

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 · see citing works

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 487 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Promoters for housekeeping genes

Dynan, W. S. (1986) · Trends in Genetics · doi:10.1016/0168-9525(86)90226-x · Cited by 385 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 300 · see citing works

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 297 · see citing works

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 · see citing works

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 250 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 231 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 206 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 171 · see citing works

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 153 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Expression of extracellular superoxide dismutase by human cell lines

Marklund, S. L. (1990) · Biochemical Journal · doi:10.1042/bj2660213 · Cited by 132 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 107 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

On signal sequence polymorphims and diseases of distribution

Macmillan-Crow, L. (1996) · Medical Entomology and Zoology · Cited by 85 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 67 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Manganese Superoxide Dismutase

Whittaker, J. W. (2000) · CRC Press eBooks · doi:10.1201/9781482289893-28 · Cited by 59 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 53 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Developmental regulation of rat lung Cu,Zn-superoxide dismutase

Hass, M. A., & Massaro, D. (1987) · Biochemical Journal · doi:10.1042/bj2460697 · Cited by 32 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Active transforming growth factor-β in human melanoma cell lines: No evidence for plasmin-related activation of latent TGF-β

Bízik, J., Felnerova, D., Grofova, M., & Vaheri, A. I. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(199607)62:1 · Cited by 10 · see citing works

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 · see citing works

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 · see citing works

[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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 4,960 · see citing works

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 · see citing works

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 2,009 · see citing works

Physiological functions of mineral micronutrients (Cu, Zn, Mn, Fe, Ni, Mo, B, Cl)

Hänsch, R., & Mendel, R. R. (2009) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2009.05.006 · Cited by 1,702 · see citing works

Redox metabolism: ROS as specific molecular regulators of cell signaling and function

Lennicke, C., & Cochemé, H. M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.018 · Cited by 1,273 · see citing works

Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease

Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works

Peroxiredoxins are conserved markers of circadian rhythms

Edgar, R. S., Green, E. W., Zhao, Y., Gerben Van Ooijen, A., Olmedo, M., Qin, X., Xu, Y. Q., Pan, M., Valekunja, U. K., Feeney, K. A., et al. (2012) · Nature · doi:10.1038/nature11088 · Cited by 915 · see citing works

Regulation of superoxide dismutase genes: Implications in disease

Lu, M., & Clair, D. K. S. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.018 · Cited by 913 · see citing works

Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans

Marrocco, I., Fabio Altieri, F., & Peluso, I. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6501046 · Cited by 874 · see citing works

Reactive Oxygen Species-Induced Activation of the MAP Kinase Signaling Pathways

McCubrey, J. A., LaHair, M. M., & Franklin, R. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1775 · Cited by 804 · see citing works

Boronate Oxidation as a Bioorthogonal Reaction Approach for Studying the Chemistry of Hydrogen Peroxide in Living Systems

Lippert, A. R., de Bittner, G. C. V., & Chang, C. J. (2011) · Accounts of Chemical Research · doi:10.1021/ar200126t · Cited by 800 · see citing works

Endothelial dysfunction — A major mediator of diabetic vascular disease

Sena, C. M., Pereira, A. M., & Seiça, R. M. F. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.006 · Cited by 796 · see citing works

Particulate air pollutants and asthma

Li, N., Hao, M., Phalen, R. F., Hinds, W. C., & Nel, A. E. (2003) · Clinical Immunology · doi:10.1016/j.clim.2003.08.006 · Cited by 771 · see citing works

Thioredoxins, Glutaredoxins, and Peroxiredoxins—Molecular Mechanisms and Health Significance: from Cofactors to Antioxidants to Redox Signaling

Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 677 · see citing works

Extracellular superoxide dismutase in biology and medicine

Fattman, C. L., Schaefer, L. M., & Oury, T. D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00275-2 · Cited by 654 · see citing works

Superoxide Dismutases in the Lung and Human Lung Diseases

Kinnula, V. L., & Crapo, J. D. (2003) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200212-1479so · Cited by 620 · see citing works

Role of Copper on Mitochondrial Function and Metabolism

Ruíz, L. M., Libedinsky, A., & Elorza, Á. A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.711227 · Cited by 571 · see citing works

The interacting pathways for prevention and repair of oxidative DNA damage

Slupphaug, G., Kavli, B., & Krokan, H. E. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.06.002 · Cited by 558 · see citing works

Oxidative cell death in cancer: mechanisms and therapeutic opportunities

An, X., Yu, W., Liu, J., Tang, D., Li, Y., & Chen, X. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06939-5 · Cited by 568 · see citing works

Measurement of Reactive Oxygen Species in Cardiovascular Studies

Dikalov, S., Griendling, K. K., & Harrison, D. G. (2007) · Hypertension · doi:10.1161/01.hyp.0000258594.87211.6b · Cited by 532 · see citing works

The Role of Oxidative Stress in Diabetic Complications

Niedowicz, D. M., & Daleke, D. L. (2005) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:43:2:289 · Cited by 528 · see citing works

Markers of Oxidative Stress during Diabetes Mellitus

Tiwari, B. K., Pandey, K. B., Abidi, A. B., & Rizvi, S. I. (2013) · Journal of Biomarkers · doi:10.1155/2013/378790 · Cited by 517 · see citing works

Mitochondrial Oxidative Stress—A Causative Factor and Therapeutic Target in Many Diseases

Kowalczyk, P., Sulejczak, D., Kleczkowska, P., Bukowska‐Ośko, I., Kucia, M., Popiel, M., Wietrak, E., Kramkowski, K., Wrzosek, K., & Kaczyńska, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413384 · Cited by 528 · see citing works

Superoxide dismutase evolution and life span regulation

Landis, G. N., & Tower, J. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.08.012 · Cited by 474 · see citing works

Antioxidant Activity of Sulfur and Selenium: A Review of Reactive Oxygen Species Scavenging, Glutathione Peroxidase, and Metal-Binding Antioxidant Mechanisms

Battin, E. E., & Brumaghim, J. L. (2009) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-009-9054-7 · Cited by 479 · see citing works

Dynamic changes in mitochondrial biogenesis and antioxidant enzymes during the spontaneous differentiation of human embryonic stem cells

Cho, Y. M., Kwon, S., Pak, Y. K., Seol, H. W., Choi, Y. M., Park, D. J., Park, K. S., & Lee, H. K. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.020 · Cited by 465 · see citing works

Vascular protection: superoxide dismutase isoforms in the vessel wall.

Faraci, F., & Didion, S. (2004) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000133604.20182.cf · Cited by 528 · see citing works

Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics

Dalle‐Donne, I., Scaloni, A., Giustarini, D., Cavarra, E., Tell, G., Lungarella, G., Colombo, R., Rossi, R., & Milzani, A. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.20006 · Cited by 448 · see citing works

Role of oxidative stress in neurodegenerative disorders: a review of reactive oxygen species and prevention by antioxidants

Houldsworth, A. (2023) · Brain Communications · doi:10.1093/braincomms/fcad356 · Cited by 444 · see citing works

Gingival crevicular fluid as a source of biomarkers for periodontitis

Barros, S. P., Williams, R. C., Offenbacher, S., & Morelli, T. (2015) · Periodontology 2000 · doi:10.1111/prd.12107 · Cited by 422 · see citing works

Oxidative stress and antioxidant mechanisms in human body

Azab, A. E., Adwas, A. A., Elsayed, A. S. I., Adwas, A. A., Elsayed, A. S. I., & Quwaydir, F. A. (2019) · Journal of Applied Biotechnology & Bioengineering · doi:10.15406/jabb.2019.06.00173 · Cited by 422 · see citing works

Role of Zinc in Immune System and Anti-Cancer Defense Mechanisms

Skrajnowska, D., & Bobrowska‐Korczak, B. (2019) · Nutrients · doi:10.3390/nu11102273 · Cited by 426 · see citing works

Understanding of ROS-Inducing Strategy in Anticancer Therapy

Kim, S. J., Kim, H. S., & Seo, Y. R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/5381692 · Cited by 404 · see citing works

Electrochemical Monitoring of Single Cell Secretion: Vesicular Exocytosis and Oxidative Stress

Amatore, C. A., Arbault, S., Guille‐Collignon, M., & Lemaître, F. (2008) · Chemical Reviews · doi:10.1021/cr068062g · Cited by 406 · see citing works

Evolutionary fate of retroposed gene copies in the human genome

Vinckenbosch, N., Dupanloup, I., & Kaessmann, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511307103 · Cited by 405 · see citing works

Nickel-based Enzyme Systems

Ragsdale, S. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r900020200 · Cited by 400 · see citing works

Oxidative Stress in the Regulation of Normal and Neoplastic Hematopoiesis

Ghaffari, S. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2142 · Cited by 377 · see citing works

Superoxide dismutases in malignant cells and human tumors

Kinnula, V. L., & Crapo, J. D. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.12.010 · Cited by 373 · see citing works

Oxidative Stress in Neurodegenerative Diseases

Crichton, R. R., & Ward, R. J. (2013) · Wiley eBooks · doi:10.1002/9781118553480.ch04 · Cited by 372 · see citing works

Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle

Lawler, J. M. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00186-2 · Cited by 370 · see citing works

Oxidative Stress during HIV Infection: Mechanisms and Consequences

Ivanov, A., Valuev-Elliston, V., Ivanova, O., Kochetkov, S., Starodubova, E., Bartosch, B., & Isaguliants, M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8910396 · Cited by 345 · see citing works

Manganese Superoxide Dismutase: Guardian of the Powerhouse

Holley, A. K., Bakthavatchalu, V., Velez-Roman, J. M., & St. Clair, D. K. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107114 · Cited by 358 · see citing works

Oxidative damage to RNA: mechanisms, consequences, and diseases

Kong, Q., & Lin, C. G. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0277-y · Cited by 350 · see citing works

Reactive Oxygen Species and Redox Signaling in Chronic Kidney Disease

Irazabal, M. V., & Torres, V. E. (2020) · Cells · doi:10.3390/cells9061342 · Cited by 354 · see citing works

Innate-adaptive immunity interplay and redox regulation in immune response

Sun, L., Wang, X., Saredy, J., Yuan, Z., Yang, X., & Wang, H. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101759 · Cited by 343 · see citing works

The oyster immunity

Wang, L., Song, X., & Song, L. (2017) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2017.05.025 · Cited by 336 · see citing works

Is SOD1 loss of function involved in amyotrophic lateral sclerosis?

Saccon, R. A., Bunton-Stasyshyn, R. K. A., Fisher, E., & Fratta, P. (2013) · Brain · doi:10.1093/brain/awt097 · Cited by 318 · see citing works

Reactive oxygen species (ROS) – a family of fate deciding molecules pivotal in constructive inflammation and wound healing

Bryan, N., Ahswin, H., Smart, N. J., Bayon, Y., Wohlert, S., & Hunt, J. A. (2012) · European Cells and Materials · doi:10.22203/ecm.v024a18 · Cited by 317 · see citing works

The Applications and Mechanisms of Superoxide Dismutase in Medicine, Food, and Cosmetics

Zheng, M., Liu, Y., Zhang, G., Yang, Z., Xu, W., & Chen, Q. (2023) · Antioxidants · doi:10.3390/antiox12091675 · Cited by 349 · see citing works

Myeloid-related proteins 8 and 14 induce a specific inflammatory response in human microvascular endothelial cells

Viemann, D., Strey, A., Janning, A., Jurk, K., Klimmek, K., Vogl, T., Hirono, K., Ichida, F., Foell, D., Kehrel, B. E., et al. (2004) · Blood · doi:10.1182/blood-2004-07-2520 · Cited by 316 · see citing works

Superoxide Radicals in the Execution of Cell Death

Fujii, J., Homma, T., & Osaki, T. (2022) · Antioxidants · doi:10.3390/antiox11030501 · Cited by 321 · see citing works

Superoxide dismutase: An updated review on its health benefits and industrial applications

Islam, M. N., Rauf, A., Fahad, F. I., Emran, T. B., Mitra, S., Olatunde, A., Shariati, M. A., Rebezov, M., Rengasamy, K. R. R., & Mubarak, M. S. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1913400 · Cited by 307 · see citing works

Molecular Mechanisms behind Free Radical Scavengers Function against Oxidative Stress

Ahmadinejad, F., Møller, S. G., Chaleshtori, M. H., Bidkhori, G., & Jami, M. (2017) · Antioxidants · doi:10.3390/antiox6030051 · Cited by 299 · see citing works

The implications of oxidative stress and antioxidant therapies in Inflammatory Bowel Disease: Clinical aspects and animal models

Ciobica, A. S., Balmuș, I.-M., Trifan, A. V., & Stanciu, C. (2016) · Saudi Journal of Gastroenterology · doi:10.4103/1319-3767.173753 · Cited by 292 · see citing works

Studies on oxidants and antioxidants with a brief glance at their relevance to the immune system

Aslani, B. A., & Ghobadi, S. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.01.014 · Cited by 276 · see citing works

Protein oxidation and cellular homeostasis: Emphasis on metabolism

Cecarini, V., Gee, J., Fioretti, E., Amici, M., Angeletti, M., Eleuteri, A. M., & Keller, J. N. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.08.039 · Cited by 274 · see citing works

On the selectivity of superoxide dismutase mimetics and its importance in pharmacological studies

Muscoli, C., Cuzzocrea, S., Riley, D. P., Zweier, J. L., Thiemermann, C., Wang, Z., & Salvemini, D. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705430 · Cited by 271 · see citing works

Microvesicles: ROS scavengers and ROS producers

Bodega, G., Alique, M., Puebla, L., Carracedo, J., & Ramı́rez, R. (2019) · Journal of Extracellular Vesicles · doi:10.1080/20013078.2019.1626654 · Cited by 257 · see citing works

Antioxidant Systems in Poultry Biology: Superoxide Dismutase

Surai, P. F. (2016) · Journal of Animal Research and Nutrition · doi:10.21767/2572-5459.100008 · Cited by 257 · see citing works

Reperfusion and Neurovascular Dysfunction in Stroke: from Basic Mechanisms to Potential Strategies for Neuroprotection

Jung, J. E., Kim, G. S., Chen, H., Maier, C. M., Narasimhan, P., Song, Y. S., Niizuma, K., Katsu, M., Okami, N., Yoshioka, H., et al. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8102-z · Cited by 256 · see citing works

Control and dysregulation of redox signalling in the gastrointestinal tract

Campbell, E. L., & Colgan, S. P. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0079-5 · Cited by 258 · see citing works

An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis

Rotunno, M. S., & Bosco, D. A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00253 · Cited by 246 · see citing works

Oxidative stress and mitochondrial impairment: Key drivers in neurodegenerative disorders

Wen, P., Sun, Z., Gou, F., Wang, J., Fan, Q., Zhao, D., & Yang, L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102667 · Cited by 253 · see citing works

Blockade of Histone Deacetylase Inhibitor-Induced RelA/p65 Acetylation and NF-κB Activation Potentiates Apoptosis in Leukemia Cells through a Process Mediated by Oxidative Damage, XIAP Downregulation, and c-Jun N-Terminal Kinase 1 Activation

Dai, Y., Rahmani, M., Dent, P., & Grant, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5429-5444.2005 · Cited by 245 · see citing works

Oxidative stress is bane in chronic liver diseases: Clinical and experimental perspective

Ezhilarasan, D. (2018) · Arab Journal of Gastroenterology · doi:10.1016/j.ajg.2018.03.002 · Cited by 239 · see citing works

Peroxisome proliferator-activated receptor γ (PPARγ): A master gatekeeper in CNS injury and repair

Cai, W., Yang, T., Liu, H., Han, L., Zhang, K., Hu, X., Zhang, X., Yin, K., Gao, Y., Bennett, M. V. L., et al. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.10.002 · Cited by 238 · see citing works

MicroRNAs and their role on fish oxidative stress during xenobiotic environmental exposures

Burgos-Aceves, M. A., Cohen, A., Smith, Y., & Faggio, C. (2017) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2017.12.001 · Cited by 240 · see citing works

Antioxidants-Related Superoxide Dismutase (SOD), Catalase (CAT), Glutathione Peroxidase (GPX), Glutathione-S-Transferase (GST), and Nitric Oxide Synthase (NOS) Gene Variants Analysis in an Obese Population: A Preliminary Case-Control Study

Gusti, A. M. T., Qusti, S. Y., Alshammari, E. M., Toraih, E. A., & Fawzy, M. S. (2021) · Antioxidants · doi:10.3390/antiox10040595 · Cited by 238 · see citing works

Hydrogen Peroxide as a Paracrine Vascular Mediator: Regulation and Signaling Leading to Dysfunction

Ardanaz, N., & Pagano, P. J. (2006) · Experimental Biology and Medicine · doi:10.1177/153537020623100302 · Cited by 228 · see citing works

Mitochondrial Superoxide Dismutase: What the Established, the Intriguing, and the Novel Reveal About a Key Cellular Redox Switch

Palma, F. R., He, C., Danes, J. M., Paviani, V., Coelho, D. R., Gantner, B. N., & Bonini, M. G. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7962 · Cited by 229 · see citing works

Antioxidants Mediate Both Iron Homeostasis and Oxidative Stress

Imam, M. U., Zhang, S., Ma, J., Wang, H., & Wang, F. (2017) · Nutrients · doi:10.3390/nu9070671 · Cited by 226 · see citing works

Dietary implications on mechanisms of sarcopenia: roles of protein, amino acids and antioxidants

Kim, J., Wilson, J. M., & Lee, S.-R. (2009) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2009.06.014 · Cited by 222 · see citing works

Adaptive homeostasis and the free radical theory of ageing

Pomatto, L. C. D., & Davies, K. J. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.016 · Cited by 224 · see citing works

A small molecule promotes cartilage extracellular matrix generation and inhibits osteoarthritis development

Shi, Y., Hu, X., Cheng, J., Zhang, X., Zhao, F., Shi, W., Ren, B., Yu, H., Yang, P., Li, Z., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09839-x · Cited by 223 · see citing works

Role of Oxidative Stress as Key Regulator of Muscle Wasting during Cachexia

Ábrigo, J., Elorza, Á. A., Riedel, C. A., Vilos, C., Simón, F., Cabrera, D., Estrada, L. D., & Cabello‐Verrugio, C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2063179 · Cited by 221 · see citing works

Targeting the Redox Balance in Inflammatory Skin Conditions

Wagener, F. A. D. T. G., Carels, C. E. L., & Lundvig, D. M. S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14059126 · Cited by 219 · see citing works

Characterization of Mitochondrial and Extra-mitochondrial Oxygen Consuming Reactions in Human Hematopoietic Stem Cells

Piccoli, C., Ria, R., Scrima, R., Cela, O., D'Aprile, A., Boffoli, D., Falzetti, F., Tabilio, A., & Capitanio, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500047200 · Cited by 209 · see citing works

Regulation of Cu/Zn-Superoxide Dismutase Expression via the Phosphatidylinositol 3 Kinase/Akt Pathway and Nuclear Factor-κB

Rojo, A. I., Salinas, M., Martı́n, D., Perona, R., & Cuadrado, A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2111-04.2004 · Cited by 216 · see citing works

Oxidative stress and antioxidant therapy in cystic fibrosis

Galli, F., Battistoni, A., Gambari, R., Alfonso Pompella, C., Bragonzi, A., Pilolli, F., Iuliano, L., Piroddi, M., Dechecchi, M. C., & Cabrini, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.012 · Cited by 207 · see citing works

Protective role of apigenin on rotenone induced rat model of Parkinson's disease: Suppression of neuroinflammation and oxidative stress mediated apoptosis

Anusha, C., Sumathi, T., & Joseph, L. D. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.03.016 · Cited by 209 · see citing works

Selenium Supplementation Restores the Antioxidative Capacity and Prevents Cell Damage in Bone Marrow Stromal Cells In Vitro

Ebert, R., Ulmer, M., Zeck, S., Meissner‐Weigl, J., Schneider, D., Stopper, H., Schupp, N., Kassem, M., & Jakob, F. (2006) · STEM CELLS · doi:10.1634/stemcells.2005-0117 · Cited by 200 · see citing works

Comparative Genomic Analyses of Copper Transporters and Cuproproteomes Reveal Evolutionary Dynamics of Copper Utilization and Its Link to Oxygen

Ridge, P. G., Zhang, Y., & Gladyshev, V. N. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001378 · Cited by 200 · see citing works

Effects of high temperatures on functional responses of haemocytes in the clam Chamelea gallina

Monari, M., Matozzo, V., Foschi, J., Cattani, O., Serrazanetti, G. P., & Marin, M. G. (2006) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2006.03.016 · Cited by 200 · see citing works

Age-dependent changes in the expression of superoxide dismutases and catalase are associated with ultrastructural modifications in human granulosa cells

Tatone, C., Carbone, M. C., Falone, S., Aimola, P., Giardinelli, A., Caserta, D., Marci, R., Pandolfi, A., Ragnelli, A. M., & Amicarelli, F. (2006) · Molecular Human Reproduction · doi:10.1093/molehr/gal080 · Cited by 197 · see citing works

Extracellular superoxide dismutase and its role in cancer

Griess, B., Tom, E. C., Domann, F. E., & Teoh-Fitzgerald, M. L. T. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.013 · Cited by 195 · see citing works

Impaired Extracellular Secretion of Mutant Superoxide Dismutase 1 Associates with Neurotoxicity in Familial Amyotrophic Lateral Sclerosis

Turner, B. J., Atkin, J. D., Farg, M. A., Zang, D. W., Rembach, A., Lopes, E. C., Patch, J. D., Hill, A. F., & Cheema, S. S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4253-04.2005 · Cited by 193 · see citing works

Pharmacology of free radicals and the impact of reactive oxygen species on the testis.

Aprioku, J. S. (2013) · Europe PMC (PubMed Central) · Cited by 188 · see citing works

Oxidative stress in the development, maintenance and resolution of paclitaxel-induced painful neuropathy

Duggett, N. A., Griffiths, L. A., McKenna, O. E., de Santis, V., Yongsanguanchai, N., Mokori, E. B., & Flatters, S. J. L. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.06.050 · Cited by 189 · see citing works

Copper at synapse: Release, binding and modulation of neurotransmission

D’Ambrosi, N., & Rossi, L. C. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.07.006 · Cited by 187 · see citing works

Oxidative stress, a trigger of hepatitis C and B virus-induced liver carcinogenesis

Ivanov, A. V., Треворович, В.-Э. В., Tyurina, D. A., Ivanova, O. N., Kochetkov, S. N., Bartosch, B., & Isaguliants, M. G. (2016) · Oncotarget · doi:10.18632/oncotarget.13904 · Cited by 188 · see citing works

PM2.5 Exposure and Asthma Development: The Key Role of Oxidative Stress

Liu, K., Hua, S., & Song, L. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3618806 · Cited by 187 · see citing works

Extracellular Superoxide Dismutase Inhibits Inflammation by Preventing Oxidative Fragmentation of Hyaluronan

Gao, F., Koenitzer, J. R., Tobolewski, J. M., Jiang, D., Liang, J., Noble, P. W., & Oury, T. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m709273200 · Cited by 186 · see citing works

A CRISPR screen identifies a pathway required for paraquat-induced cell death

Reczek, C. R., Birsoy, K., Kong, H., Martínez‐Reyes, I., Wang, T., Gao, P., Sabatini, D. M., & Chandel, N. S. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2499 · Cited by 184 · see citing works

The effects of dietary restriction on oxidative stress in rodents

Walsh, M. E., Shi, Y., & Van Remmen, H. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.037 · Cited by 181 · see citing works

The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution

Hatori, Y., & Lutsenko, S. (2016) · Antioxidants · doi:10.3390/antiox5030025 · Cited by 183 · see citing works

MicroRNA-21 Modulates the Levels of Reactive Oxygen Species by Targeting SOD3 and TNF α

Zhang, X., Ng, W. L., Wang, P., Tian, L., Werner, E., Wang, H., Doetsch, P. W., & Wang, Y. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0639 · Cited by 181 · see citing works

The SOD Gene Family in Tomato: Identification, Phylogenetic Relationships, and Expression Patterns

Feng, K., Yu, J., Cheng, Y., Ruan, M., Wang, R., Ye, Q., Zhou, G., Li, Z., Yao, Z., Yang, Y., et al. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01279 · Cited by 181 · see citing works

Regulation of redox balance in cancer and T cells

Kong, H., & Chandel, N. S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000257 · Cited by 180 · see citing works

STRUCTURES, EVOLUTION, AND EXPRESSION

Zelko, I. N., Mariani, T. J., & Folz, R. J. (2002)

Study Progress of Cu,Zn Superoxide Dismutase——From Gene to Function

Chang-lu, W. (2008) · Xiandai shengwu yixue jinzhan

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 856 · see citing works

Superoxide dismutases: active sites that save, but a protein that kills

Miller, A. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.02.011 · Cited by 315 · see citing works

Superoxide Dismutase: Free Radical Degradation in Health and Disease

Kessler, E., Cross, D., Olson, S., Person, A., Smith, H. R., & Kaja, S. (2015) · The FASEB Journal · doi:10.1096/fasebj.29.1_supplement.lb71 · Cited by 5 · see citing works