Antioxidant enzymes and human diseases

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

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

Requirement for Generation of H ₂ O ₂ for Platelet-Derived Growth Factor Signal Transduction

Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works

Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer

WISEMAN, H., & HALLIWELL, B. (1996) · Biochemical Journal · doi:10.1042/bj3130017 · Cited by 2,345 · see citing works

The role of lipid peroxidation and antioxidants in oxidative modification of LDL

Esterbauer, H., Gebicki, J. M., Puhl, H., & Jürgens, G. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90181-f · Cited by 2,307 · see citing works

Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase

Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789 · see citing works

Oxidative burst: an early plant response to pathogen infection

Wojtaszek, P. (1997) · Biochemical Journal · doi:10.1042/bj3220681 · Cited by 1,313 · see citing works

Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins

Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y., Pinsky, D. J., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36966-1 · Cited by 1,305 · see citing works

Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide

Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208 · see citing works

Oxidative Stress, Antioxidants, and Animal Function

Miller, J. K., Brzezińska-Ślebodzińska, E., & Madsen, F. C. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77620-1 · Cited by 771 · see citing works

Reactive oxygen species released from mitochondria during brief hypoxia induce preconditioning in cardiomyocytes

Vanden Hoek, T. L., Becker, L. B., Shao, Z., Li, C., & Schumacker, P. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18092 · Cited by 721 · see citing works

Intracellular Signaling by Reactive Oxygen Species during Hypoxia in Cardiomyocytes

Duranteau, J., Chandel, N. S., Kulisz, A., Shao, Z., & Schumacker, P. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11619 · Cited by 679 · see citing works

Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions.

Schmidt, A. M., Hori, O., Brett, J., Yan, S. D., Wautier, J., & Stern, D. (1994) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.14.10.1521 · Cited by 636 · see citing works

Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress.

Yan, S. D., Chen, X., Schmidt, A. M., Brett, J., Godman, G., Zou, Y. S., Scott, C. W., Caputo, C., Frappier, T., & Smith, M. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7787 · Cited by 565 · see citing works

[53] Glutathione peroxidase and hydroperoxides

Tappel, A. L. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)52055-7 · Cited by 509 · see citing works

Peroxynitrite-Mediated Inactivation of Manganese Superoxide Dismutase Involves Nitration and Oxidation of Critical Tyrosine Residues

MacMillan-Crow, L. A., Crow, J. P., & Thompson, J. A. (1998) · Biochemistry · doi:10.1021/bi971894b · Cited by 508 · see citing works

Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells

Ghosh, J., & Myers, C. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13182 · Cited by 500 · see citing works

Protection against oxygen toxicity by intravenous injection of liposome-entrapped catalase and superoxide dismutase.

Turrens, J. F., Crapo, J. D., & Freeman, B. Α. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111210 · Cited by 485 · see citing works

Mice with a Homozygous Null Mutation for the Most Abundant Glutathione Peroxidase, Gpx1, Show Increased Susceptibility to the Oxidative Stress-inducing Agents Paraquat and Hydrogen Peroxide

de Haan, J. B., Bladier, C., Griffiths, P., Kelner, M. J., O’Shea, R. D., Cheung, N. S., Bronson, R. T., Silvestro, M. J., Wild, S., Zheng, S. S., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22528 · Cited by 450 · see citing works

Inactivation of Human Manganese-superoxide Dismutase by Peroxynitrite Is Caused by Exclusive Nitration of Tyrosine 34 to 3-Nitrotyrosine

Yamakura, F., Taka, H., Fujimura, T., & Murayama, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14085 · Cited by 442 · see citing works

Lipid peroxidation, antioxidant protection and aging

Rikans, L. E., & Hornbrook, K. R. (1997) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(97)00067-7 · Cited by 413 · see citing works

Differential regulation of antioxidant enzymes in response to oxidants.

Shull, S., Heintz, N. H., Periasamy, M., Manohar, M., Janssen, Y. M., Marsh, J. P., & Mossman, B. T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54242-3 · Cited by 403 · see citing works

Advanced glycation end products (AGEs) on the surface of diabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: a link between surface-associated AGEs and diabetic complications.

Wautier, J., Wautier, M.-P., Schmidt, A. M., Anderson, G. M., Hori, O., Zoukourian, C., Capron, L., Chappey, O., Yan, S. D., & Brett, J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7742 · Cited by 353 · see citing works

Carotenoid mixtures protect multilamellar liposomes against oxidative damage: synergistic effects of lycopene and lutein

Stahl, W., Junghans, A., de Boer, B., Driomina, E. S., Briviba, K., & Sies, H. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00434-7 · Cited by 347 · see citing works

Genetic Classification of Primary Neurodegenerative Disease

Hardy, J., & Gwinn, K. A. (1998) · Science · doi:10.1126/science.282.5391.1075 · Cited by 341 · 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

Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase.

Farr, S. B., D’Ari, R., & Touati, D. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8268 · Cited by 309 · see citing works

Superoxide anion generation in Drosophila during melanotic encapsulation of parasites.

Nappi, A. J., Vass, E., Frey, F., et al. (1995) · PubMed · Cited by 295 · see citing works

Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein

REQUENA, J. R., FU, M. X., AHMED, M. U., JENKINS, A. J., LYONS, T. J., BAYNES, J. W., & THORPE, S. R. (1997) · Biochemical Journal · doi:10.1042/bj3220317 · Cited by 293 · see citing works

Prion protein expression and superoxide dismutase activity

Brown, D. R., & Besinger, A. (1998) · Biochemical Journal · doi:10.1042/bj3340423 · Cited by 271 · see citing works

The Copper Chaperone CCS Directly Interacts with Copper/Zinc Superoxide Dismutase

Casareno, R. L. B., Waggoner, D., & Gitlin, J. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.23625 · Cited by 270 · see citing works

Protection against peroxynitrite-induced fibroblast injury and arthritis development by inhibition of poly(ADP-ribose) synthase

Szabó, C., Virág, L., Cuzzocrea, S., Scott, G. S., Hake, P. W., O’Connor, M., Zingarelli, B., Salzman, A. L., & Kun, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3867 · Cited by 262 · see citing works

New biomarker evidence of oxidative DNA damage in patients with non‐insulin‐dependent diabetes mellitus

Leinonen, J. S., Lehtimäki, T. J., Toyokuni, S., Okada, K., Tanaka, T. U., Hiai, H., Ochi, H., Laippala, P. J., Rantalaiho, V. M., Wirta, O., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01273-8 · Cited by 262 · see citing works

A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen.

van Loon, A. P. G. M., Pesold-Hurt, B., & Schatz, G. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.3820 · Cited by 262 · see citing works

Genetic Neurodegenerative Diseases: The Human Illness and Transgenic Models

Price, D. L., Sisodia, S. S., & Borchelt, D. (1998) · Science · doi:10.1126/science.282.5391.1079 · Cited by 258 · see citing works

Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque

Fu, S., Davies, M. J., Stocker, R., & Dean, R. T. (1998) · Biochemical Journal · doi:10.1042/bj3330519 · Cited by 256 · see citing works

Simultaneous Overexpression of Copper- and Zinc-containing Superoxide Dismutase and Catalase Retards Age-related Oxidative Damage and Increases Metabolic Potential in Drosophila melanogaster

Sohal, R. S., Agarwal, A., Agarwal, S., & Orr, W. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.26.15671 · Cited by 239 · see citing works

Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutant

Williamson, T. L., Bruijn, L. I., Zhu, Q., Anderson, K. L., Anderson, S., Julien, J., & Cleveland, D. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9631 · Cited by 238 · see citing works

Glucose Deprivation-induced Cytotoxicity and Alterations in Mitogen-activated Protein Kinase Activation Are Mediated by Oxidative Stress in Multidrug-resistant Human Breast Carcinoma Cells

Lee, Y. J., Galoforo, S., Berns, C. M., Chen, J. C., Davis, B. H., Sim, J. E., Corry, P. M., & Spitz, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5294 · Cited by 225 · see citing works

Dopamine induces apoptosis-like cell death in cultured chick sympathetic neurons — A possible novel pathogenetic mechanism in Parkinson's disease

Ziv, I., Melamed, E., Nardi, N., et al. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90258-5 · Cited by 222 · 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

Protective effect of neurofilament heavy gene overexpression in motor neuron disease induced by mutant superoxide dismutase

Couillard‐Després, S., Zhu, Q., Wong, P. C., Price, D. L., Cleveland, D. W., & Julien, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9626 · Cited by 211 · see citing works

Superoxide dismutase (SOD)-catalase conjugates. Role of hydrogen peroxide and the Fenton reaction in SOD toxicity.

Mao, G. D., Thomas, P. D., Lopaschuk, G. D., & Poznansky, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54167-3 · Cited by 205 · see citing works

Ultraviolet-Induced Cell Death Blocked by a Selenoprotein from a Human Dermatotropic Poxvirus

Shisler, J. L., Senkevich, T. G., Berry, M. J., & Moss, B. (1998) · Science · doi:10.1126/science.279.5347.102 · Cited by 200 · see citing works

Glutathione peroxidase compensates for the hypersensitivity of Cu,Zn-superoxide dismutase overproducers to oxidant stress.

Amstad, P., Moret, R., & Cerutti, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42068-0 · Cited by 196 · see citing works

Origin of superoxide production by endothelial nitric oxide synthase

Stroes, E. S. G., Hijmering, M. L., van Zandvoort, M. A. M. J., Wever, R. M. F., Rabelink, T. J., & van Faassen, E. E. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01292-7 · Cited by 188 · see citing works

Effect of Inorganic Phosphate Concentration on the Nature of Inner Mitochondrial Membrane Alterations Mediated by Ca2+ Ions

Kowaltowski, A. J., Castilho, R. F., Grijalba, M. T., Bechara, E. J. H., & Vercesi, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2929 · Cited by 186 · see citing works

Overexpression of human glutathione peroxidase protects transgenic mice against focal cerebral ischemia/reperfusion damage

Weisbrot-Lefkowitz, M., Reuhl, K. R., Perry, B., et al. (1998) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00313-6 · Cited by 182 · see citing works

Indirect mutagenesis by oxidative DNA damage: Formation of the pyrimidopurinone adduct of deoxyguanosine by base propenal

Dedon, P. C., Plastaras, J. P., Rouzer, C. A., & Marnett, L. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11113 · Cited by 176 · see citing works

Suppression of Leukotriene Formation in RBL-2H3 Cells That Overexpressed Phospholipid Hydroperoxide Glutathione Peroxidase

Imai, H., Narashima, K., Arai, M., Sakamoto, H., Chiba, N., & Nakagawa, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.1990 · Cited by 169 · see citing works

Quercetin metabolites inhibit copper ion‐induced lipid peroxidation in rat plasma1

da Silva, E. L., Piskuła, M. K., Yamamoto, N., Moon, J., & Terao, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00709-1 · Cited by 167 · see citing works

Evidence for the production of peroxynitrite in inflammatory CNS demyelination

Cross, A. H., Manning, P. T., Stern, M. K., & Misko, T. P. (1997) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00145-8 · Cited by 163 · see citing works

Distribution of CuZn superoxide dismutase and Mn superoxide dismutase in human tissues and extracellular fluids.

Marklund, S. L. (1980) · PubMed · Cited by 161 · see citing works

Apoptosis, reproductive failure, and oxidative stress in Chinese hamster ovary cells with compromised genomic integrity.

Limoli, C. L., Hartmann, A., Shephard, L. B., Yang, C., Boothman, D. A., Bartholomew, J., & Morgan, W. F. (1998) · PubMed · Cited by 160 · see citing works

Thioredoxin-linked mitigation of allergic responses to wheat

Buchanan, B. B., Adamidi, C., Lozano, R. M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5372 · Cited by 144 · see citing works

Rheumatoid arthritis and metal compounds—perspectives on the role of oxygen radical detoxification†

Aaseth, J., Haugen, M. A., & Førre, Ø. (1998) · The Analyst · doi:10.1039/a704840h · Cited by 138 · see citing works

Antioxidants reduce cyclooxygenase-2 expression, prostaglandin production, and proliferation in colorectal cancer cells.

Chinery, R., Beauchamp, R. D., Shyr, Y., et al. (1998) · PubMed · Cited by 135 · see citing works

Citrus auraptene exerts dose-dependent chemopreventive activity in rat large bowel tumorigenesis: the inhibition correlates with suppression of cell proliferation and lipid peroxidation and with induction of phase II drug-metabolizing enzymes.

Tanaka, T., Kawabata, K., Kakumoto, M., Hara, A., Murakami, A., Kuki, W., Takahashi, Y., Yonei, H., Maeda, M., Ota, T., et al. (1998) · PubMed · Cited by 132 · see citing works

Reactive oxygen species and nitric oxide in viral diseases

Peterhans, E. (1997) · Biological Trace Element Research · doi:10.1007/bf02778986 · Cited by 129 · see citing works

Virulence of catalase-deficient aspergillus nidulans in p47(phox)-/- mice. Implications for fungal pathogenicity and host defense in chronic granulomatous disease.

Chang, Y. C., Segal, B. H., Holland, S. M., Miller, G., & Kwon-Chung, K. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2301 · Cited by 121 · see citing works

Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H 2 O 2

Singh, R. J., Karoui, H., Gunther, M. R., Beckman, J. S., Mason, R. P., & Kalyanaraman, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.6675 · Cited by 117 · see citing works

Early Glycoxidation Damage in Brains from Down's Syndrome

Odetti, P. R., Angelini, G., Dapino, D., Zaccheo, D., Garibaldi, S., Dagna-Bricarelli, F., Piombo, G., Perry, G. L., Smith, M. A., Traverso, N., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8186 · Cited by 116 · see citing works

Lower intracellular hydrogen peroxide levels in cells overexpressing CuZn-superoxide dismutase

Teixeira, H. D., Schumacher, R. I., & Meneghini, R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7872 · Cited by 112 · see citing works

Alteration of endogenous glutathione peroxidase, manganese superoxide dismutase, and glutathione transferase activity in cells transfected with a copper-zinc superoxide dismutase expression vector. Explanation for variations in paraquat resistance.

Kelner, M. J., & Bagnell, R. D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38527-8 · Cited by 108 · see citing works

Effects of oxidative stress on expression of extracellular superoxide dismutase, CuZn-superoxide dismutase and Mn-superoxide dismutase in human dermal fibroblasts

Strålin, P., & Marklund, S. L. (1994) · Biochemical Journal · doi:10.1042/bj2980347 · Cited by 107 · see citing works

Helicobacter pyloriGenerates Superoxide Radicals and Modulates Nitric Oxide Metabolism

Nagata, K., Yu, H., Nishikawa, M., Kashiba, M., Nakamura, A., Sato, E. F., Tamura, T., & Inoue, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14071 · Cited by 106 · see citing works

Oxidative Stress Inhibits Calpain Activity in Situ

Guttmann, R. P., & Johnson, G. V. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13331 · Cited by 103 · see citing works

Enhancement of erythrocyte superoxide dismutase activity: effects on cellular oxidant defense

Scott, M., Jw, E., Fa, K., et al. (1989) · Blood · doi:10.1182/blood.v74.7.2542.2542 · Cited by 94 · see citing works

Reduced platelet glutathione peroxidase activity and serum selenium concentration in atopic asthmatic patients

Misso, N. L. A., Powers, K., Gillon, R. L., Stewart, G. A., & Thompson, P. J. (1996) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.1996.tb00616.x · Cited by 91 · see citing works

Superoxide-mediated Decomposition of BiologicalS-Nitrosothiols

Aleryani, S., Milo, E., Rose, Y., & Kostka, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6041 · Cited by 91 · see citing works

The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract

Hall, L., Williams, K., Perry, A. C. F., Frayne, J., & JURY, J. A. (1998) · Biochemical Journal · doi:10.1042/bj3330005 · Cited by 89 · see citing works

Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn) superoxide dismutase and Fe-superoxide dismutase

Vance, C. K., & Miller, A.-F. (1998) · Biochemistry · doi:10.1021/bi972580r · Cited by 89 · see citing works

Overexpression of hMTH1 mRNA: a molecular marker of oxidative stress in lung cancer cells

Kennedy, C. H., Cueto, R., Belinsky, S. A., Lechner, J. F., & Pryor, W. A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00505-5 · Cited by 86 · see citing works

Impaired production of nitric oxide, superoxide, and hydrogen peroxide in glucose 6‐phosphate‐dehydrogenase‐deficient granulocytes

Tsai, K.-J., Hung, I., Chow, C. K., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01174-0 · Cited by 84 · see citing works

Induction of Spermidine/Spermine N1-Acetyltransferase in Human Cancer Cells in Response to Increased Production of Reactive Oxygen Species

Chopra, S., & WALLACE, H. M. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00601-1 · Cited by 79 · see citing works

Biochemical Defense Mechanisms against Copper-Induced Oxidative Damage in the Blue Crab,Callinectes sapidus

Brouwer, M. H., & Brouwer, T. H. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0568 · Cited by 78 · see citing works

Hydrogen peroxide-induced DNA damage is independent of nuclear calcium but dependent on redox-active ions

Jornot, L., Petersen, H., & Junod, A. F. (1998) · Biochemical Journal · doi:10.1042/bj3350085 · Cited by 77 · see citing works

Overproduction of human Mn‐superoxide dismutase modulates paraquat‐mediated toxicity in mammalian cells

Clair, D. K. S., Oberley, T. D., & Ho, Y.-S. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81186-c · Cited by 74 · see citing works

Nerve Growth Factor Treatment Prevents the Increase in Superoxide Produced by Epidermal Growth Factor in PC12 Cells

Mills, E., Takeda, K., Yu, Z., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22165 · Cited by 74 · see citing works

Role of the Dimeric Structure in Cu,Zn Superoxide Dismutase

Battistoni, A., Folcarelli, S., Cervoni, L., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5655 · Cited by 73 · see citing works

DNA excision repair profiles of normal and leukemic human lymphocytes: functional analysis at the single-cell level.

Buschfort, C., Muller, M. R., Seeber, S., et al. (1997) · PubMed · Cited by 71 · see citing works

Antioxidant enzymes and fatty acid status in erythrocytes of Down syndrome patients

Pastor, M.-C., Sierra, C., Doladé, M., Navarro, E., Brandi, N., Cabré, E., Mira, Á., & Serés, A. (1998) · Clinical Chemistry · doi:10.1093/clinchem/44.5.924 · Cited by 69 · see citing works

Antioxidant enzymes and fatty acid status in erythrocytes of Down's syndrome patients.

Pastor, M.-C., Sierra, C., Doladé, M., et al. (1998) · PubMed · Cited by 67 · see citing works

Induction of superoxide dismutase in leukocytes by paraquat: correlation with age and possible predictor of longevity

Niwa, Y., Ishimoto, K., & Kanoh, T. (1990) · Blood · doi:10.1182/blood.v76.4.835.835 · Cited by 66 · see citing works

Oxidative Damage, Plasma Antioxidant Capacity, and Glucemic Control in Elderly NIDDM Patients

Aguirre, F., Martin, I., Grinspon, D., Ruiz, M. C., Hager, A., Paoli, T. D., Ihlo, J. E., Farach, H. A., & Poole, C. P. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00293-1 · Cited by 66 · see citing works

Regulation of manganese superoxide dismutase and other antioxidant genes in normal and leukemic hematopoietic cells and their relationship to cytotoxicity by tumor necrosis factor

Kizaki, M., Sakashita, A., Karmakar, A., Lin, C., & Koeffler, H. (1993) · Blood · doi:10.1182/blood.v82.4.1142.1142 · Cited by 65 · see citing works

A Yeast Homologue of the Human Phosphotyrosyl Phosphatase Activator PTPA Is Implicated in Protection against Oxidative DNA Damage Induced by the Model Carcinogen 4-Nitroquinoline 1-Oxide

Ramotar, D., Bélanger, E., Brodeur, I., Masson, J., & Drobetsky, E. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21489 · Cited by 63 · see citing works

Human serum, cysteine and histidine inhibit the oxidation of low density lipoprotein less at acidic pH

Patterson, R. A., & Leake, D. S. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01002-3 · Cited by 59 · see citing works

Ceruloplasmin Copper Induces Oxidant Damage by a Redox Process Utilizing Cell-Derived Superoxide as Reductant

Mukhopadhyay, C. K., & Fox, P. L. (1998) · Biochemistry · doi:10.1021/bi981137t · Cited by 58 · see citing works

Cells enriched for catalase are sensitized to the toxicities of bleomycin, adriamycin, and paraquat.

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