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

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

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

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 1,785

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 1,313

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

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

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

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 907

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 814

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 809

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 819

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 785

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 696

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 657

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

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 584

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 573

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 617

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

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 533

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

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 551

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 485

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

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

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

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 461

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 455

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 475

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

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

Skrajnowska, D., & Bobrowska‐Korczak, B. (2019) · Nutrients · doi:10.3390/nu11102273 · Cited by 441

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 414

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 412

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 406

Nickel-based Enzyme Systems

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

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 381

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 381

Oxidative Stress in Neurodegenerative Diseases

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

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

Oxidative Stress during HIV Infection: Mechanisms and Consequences

Ivanov, A. V., Треворович, В.-Э. В., Ivanova, O. N., Kochetkov, S. N., Starodubova, E. S., Bartosch, B., & Isaguliants, M. G. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8910396 · Cited by 383

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

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 359

Reactive Oxygen Species and Redox Signaling in Chronic Kidney Disease

Irazabal, M. V., & Torres, V. E. (2020) · Cells · doi:10.3390/cells9061342 · Cited by 359

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 364

The oyster immunity

Wang, L., Song, X., & Song, L. (2017) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2017.05.025 · Cited by 341

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 339

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

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

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

Superoxide Radicals in the Execution of Cell Death

Fujii, J., Homma, T., & Osaki, T. (2022) · Antioxidants · doi:10.3390/antiox11030501 · Cited by 337

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

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 315

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 297

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

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

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

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 263

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

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 257

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 267

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

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 256

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 247

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 245

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 240

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 241

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 265

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 230

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 253

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 239

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 229

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 233

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 224

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 225

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 223

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

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

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 223

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

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

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 206

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

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

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 200

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

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

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

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

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 193

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

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

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

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

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

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

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 183

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 182

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 860

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 317

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