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1. Full Text Dual role of superoxide dismutase 2 induced in activated microglia: Oxidative stress tolerance and convergence of inflammatory responses
by Ishihara, Yasuhiro and Takemoto, Takuya and Itoh, Kouichi and Ishida, Atsuhiko and Yamazaki, Takeshi
Journal of Biological Chemistry, ISSN 0021-9258, 09/2015, Volume 290, Issue 37, pp. 22805 - 22817
Microglia are activated quickly in response to external pathogens or cell debris and clear these substances via the inflammatory response. However, excessive... 
NADPH OXIDASE | MITOCHONDRIAL ROS | INTERFERON-GAMMA | REDOX REGULATION | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NEURONAL INJURY | TOLL-LIKE RECEPTORS | GENE-EXPRESSION | NF-KAPPA-B | PARKINSONS-DISEASE | Inflammation - chemically induced | Inflammation - pathology | Poly I-C - pharmacology | Superoxide Dismutase - genetics | Superoxide Dismutase - biosynthesis | Oxidative Stress | Rats, Wistar | NADPH Oxidases - antagonists & inhibitors | NADPH Oxidases - metabolism | Microglia - enzymology | Rats | Gene Knockdown Techniques | Gene Expression Regulation, Enzymologic | Animals | Lipopolysaccharides - pharmacology | Inflammation - genetics | Microglia - pathology | NADPH Oxidases - genetics | Oligodeoxyribonucleotides - pharmacology | Cytokines - genetics | Inflammation - enzymology | Cytokines - biosynthesis | NF-kappaB | superoxide dismutase (SOD) | inflammation | microglia | oxidative stress | Neurobiology
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2. Full Text Extracellular superoxide dismutase
by Nozik-Grayck, Eva and Suliman, Hagir B and Piantadosi, Claude A
International Journal of Biochemistry and Cell Biology, ISSN 1357-2725, 2005, Volume 37, Issue 12, pp. 2466 - 2471
The extracellular space is protected from oxidant stress by the antioxidant enzyme extracellular superoxide dismutase (EC-SOD), which is highly expressed in... 
Antioxidant | Nitric oxide | Extracellular superoxide dismutase | antioxidant | nitric oxide | extracellular superoxide dismutase | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | Gene Expression Regulation, Enzymologic | Animals | Superoxide Dismutase - biosynthesis | Superoxide Dismutase - physiology | Humans | Protein Structure, Quaternary | Transcription, Genetic | Extracellular Space - enzymology | Antioxidants | Superoxide dismutase | Superoxide | Gene expression
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3. Full Text Superoxide dismutase downregulation in osteoarthritis progression and end-stage disease
by Scott, Jenny L and Gabrielides, Christos and Davidson, Rose K and Swingler, Tracey E and Clark, Ian M and Wallis, Gillian A and Boot-Handford, Raymond P and Kirkwood, Tom B L and Talyor, Robert W and Young, David A
Annals of the Rheumatic Diseases, ISSN 0003-4967, 08/2010, Volume 69, Issue 8, pp. 1502 - 1510
Background Oxidative stress is proposed as an important factor in osteoarthritis (OA). Objective To investigate the expression of the three superoxide... 
COLLAGEN-INDUCED ARTHRITIS | MATRIX METALLOPROTEINASES | IN-VITRO | DNA METHYLATION | CHONDROCYTES | ARTICULAR-CARTILAGE | NITRIC-OXIDE | HYDROGEN-PEROXIDE | RHEUMATOLOGY | EXPRESSION | OXIDATIVE FRAGMENTATION | Promoter Regions, Genetic | Superoxide Dismutase - genetics | Guinea Pigs | Superoxide Dismutase - biosynthesis | Down-Regulation | Humans | Cells, Cultured | Molecular Sequence Data | Male | Matrix Metalloproteinase 1 - biosynthesis | Superoxide Dismutase - deficiency | Cartilage, Articular - enzymology | Matrix Metalloproteinase 13 - biosynthesis | Disease Progression | Gene Expression Regulation, Enzymologic | Chondrocytes - enzymology | DNA Methylation | Animals | Base Sequence | Reverse Transcriptase Polymerase Chain Reaction - methods | Osteoarthritis, Hip - enzymology | Femur Neck - enzymology | Arthritis, Experimental - enzymology | Oxidative stress | Physiological aspects | Development and progression | Superoxide dismutase | Models | Research | Osteoarthritis | Risk factors | Studies | Antioxidants | Enzymes | Biomedical research | Collagen | Aging | DNA methylation | Arthritis
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4. Full Text Caloric restriction or catalase inactivation extends yeast chronological lifespan by inducing H2O2 and superoxide dismutase activity
by Ana Mesquita and Martin Weinberger and Alexandra Silva and Belém Sampaio-Marques and Bruno Almeida and Cecília Leão and Vítor Costa and Fernando Rodrigues and William C. Burhans and Paula Ludovico
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 08/2010, Volume 107, Issue 34, pp. 15123 - 15128
The free radical theory of aging posits oxidative damage to macromolecules as a primary determinant of lifespan. Recent studies challenge this theory by... 
Aging | Hormesis | Hydrogen peroxide | Oxidative damage | Antioxidant enzymes | APOPTOSIS | CELLS | OXIDATIVE STRESS | MECHANISM | NEUTROPHIL ACTIVATION | BUDDING YEAST | MULTIDISCIPLINARY SCIENCES | hydrogen peroxide | oxidative damage | antioxidant enzymes | SACCHAROMYCES-CEREVISIAE | DAMAGE | HYDROGEN-PEROXIDE | aging | hormesis | Reactive Oxygen Species - metabolism | Superoxide Dismutase - biosynthesis | Oxidative Stress | Catalase - genetics | Saccharomyces cerevisiae - genetics | Catalase - antagonists & inhibitors | DNA Primers - genetics | Hydrogen Peroxide - metabolism | Catalase - metabolism | Saccharomyces cerevisiae - cytology | Saccharomyces cerevisiae - metabolism | Culture Media | Models, Biological | Base Sequence | Saccharomyces cerevisiae - growth & development | Oxidative stress | Reactive oxygen species | Free radicals | Macromolecules | Superoxide dismutase | Longevity | Dietary restrictions | Catalase | Life span | superoxide anions | Age | Biological Sciences
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5. Full Text MicroRNA-377 is up-regulated and can lead to increased fibronectin production in diabetic nephropathy
by Wang, Qiang and Wang, Youli and Minto, Andrew W and Wang, Jinhua and Shi, Qun and Li, Xinmin and Quigg, Richard J
FASEB Journal, ISSN 0892-6638, 12/2008, Volume 22, Issue 12, pp. 4126 - 4135
Intrinsic glomerular cells in a diabetic milieu have transcriptional activation of genes that influence the development of diabetic nephropathy. The cellular... 
Glomerulus | Extracellular matrix | microRNA | Diabetes | APOPTOSIS | ACTIVATION | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | glomerulus | CELL BIOLOGY | KIDNEY GLOMERULI | SIGNALING PATHWAY | GLUCOSE | ENDOTHELIAL-CELLS | BIOLOGY | MESANGIAL CELLS | diabetes | SUPEROXIDE-DISMUTASE | RENAL INJURY | extracellular matrix | Up-Regulation | Fibronectins - biosynthesis | Superoxide Dismutase - biosynthesis | Diabetic Nephropathies - metabolism | Humans | Cells, Cultured | Protein Phosphatase 2C | MicroRNAs - biosynthesis | p21-Activated Kinases - biosynthesis | Animals | Glomerular Mesangium - metabolism | Phosphoprotein Phosphatases - biosynthesis | Female | Mice, Inbred NOD | Mice | MicroRNAs - physiology | Research Communications
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6. Full Text Melatonin enhances antioxidative enzyme gene expression (CAT, GPx, SOD), prevents their UVR‐induced depletion, and protects against the formation of DNA damage (8‐hydroxy‐2'‐deoxyguanosine) in ex vivo human skin
by Fischer, Tobias W and Kleszczyński, Konrad and Hardkop, Lena H and Kruse, Nathalie and Zillikens, Detlef
Journal of Pineal Research, ISSN 0742-3098, 04/2013, Volume 54, Issue 3, pp. 303 - 312
UV radiation (UVR) induces serious structural and functional alterations in human skin leading to skin aging and carcinogenesis. Reactive oxygen species are... 
8‐hydroxy‐2'‐deoxyguanosine | ultraviolet radiation | superoxide dismutase | human full‐thickness skin | melatonin | catalase | glutathione peroxidase | human full-thickness skin | 8-hydroxy-2'-deoxyguanosine | OXIDATIVE STRESS | PHYSIOLOGY | MECHANISM | INDUCED APOPTOSIS | GLUTATHIONE-PEROXIDASE | KERATINOCYTES | NEUROSCIENCES | OXYGEN | IN-VITRO | ENDOCRINOLOGY & METABOLISM | SYSTEMS | ULTRAVIOLET-RADIATION | HUMAN EPIDERMIS | 8-hydroxy-2 '-deoxyguanosine | Immunohistochemistry | Superoxide Dismutase - genetics | Skin Physiological Phenomena - drug effects | Superoxide Dismutase - biosynthesis | Skin - metabolism | Antioxidants - metabolism | Humans | Middle Aged | Young Adult | Ultraviolet Rays | Adult | Real-Time Polymerase Chain Reaction | Deoxyguanosine - analogs & derivatives | Organ Culture Techniques | Superoxide Dismutase - metabolism | Glutathione Peroxidase - metabolism | Catalase - genetics | Antioxidants - pharmacology | Glutathione Peroxidase - biosynthesis | Skin - enzymology | Glutathione Peroxidase - genetics | Catalase - metabolism | Analysis of Variance | Skin - radiation effects | Deoxyguanosine - metabolism | DNA Damage | Catalase - biosynthesis | Melatonin - pharmacology | Skin - drug effects | Enzymes | Melatonin | Nuclear radiation | DNA damage | Genes | DNA | Genetic research | Superoxide | Skin | Gene expression | Index Medicus
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7. Full Text Subcellular distribution of superoxide dismutases (SOD) in rat liver. Cu,Zn-SOD in mitochondria
by Okado-Matsumoto, Ayako and Fridovich, Irwin
Journal of Biological Chemistry, ISSN 0021-9258, 10/2001, Volume 276, Issue 42, pp. 38388 - 38393
Rat liver was homogenized in isotonic buffer, fractionated by differential centrifugation, and then subfractionated by equilibrium sedimentation in Nycodenz... 
LOCALIZATION | SITE | MECHANISM | ACIDS | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | REACTIVITY | RADICALS | COPPER-ZINC | Detergents - pharmacology | Immunoassay | Centrifugation, Density Gradient | Superoxide Dismutase - biosynthesis | Liver - metabolism | Rats | Immunoblotting | Mice, Transgenic | Mitochondria - metabolism | Mitochondria, Liver - enzymology | Rats, Sprague-Dawley | Mice, Knockout | Dose-Response Relationship, Drug | Superoxide Dismutase - chemistry | Cyanides - metabolism | Animals | Lysosomes - metabolism | Time Factors | Sodium Dodecyl Sulfate - pharmacology | Cytosol - metabolism | Cell Membrane - metabolism | Mice | Hydrogen-Ion Concentration
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8. Full Text Sirtuin 1 attenuates oxidative stress via upregulation of superoxide dismutase 2 and catalase in astrocytes
by Cheng, Yi and Takeuchi, Hideyuki and Sonobe, Yoshifumi and Jin, Shijie and Wang, Yue and Horiuchi, Hiroshi and Parajuli, Bijay and Kawanokuchi, Jun and Mizuno, Tetsuya and Suzumura, Akio
Journal of Neuroimmunology, ISSN 0165-5728, 2014, Volume 269, Issue 1, pp. 38 - 43
Abstract Sirtuin 1 (SIRT1) exerts a neuroprotective effect on various neurologic diseases. Here we investigated the protective functions of SIRT1 in... 
Neurology | Allergy and Immunology | Reactive oxygen species | Forkhead box protein O4 | Astrocyte | Catalase | Sirtuin 1 | Superoxide dismutase 2 | sirtuin 1 | P53 ACETYLATION | ACTIVATION | PGC-1-ALPHA | TRANSCRIPTION | IMMUNOLOGY | CELL-SURVIVAL | NEUROSCIENCES | DAMAGE | LONGEVITY | DISEASES | GENE | MICROGLIA | Forkhead box protein 04 | Animals, Newborn | Animals | Reactive Oxygen Species - metabolism | Superoxide Dismutase - biosynthesis | Mice, Inbred C57BL | Oxidative Stress - physiology | Up-Regulation - physiology | Cells, Cultured | Sirtuin 1 - biosynthesis | Mice | Catalase - biosynthesis | Astrocytes - metabolism | Superoxide
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9. Full Text The overexpression of major antioxidant enzymes does not extend the lifespan of mice
by Perez, Viviana I and Van Remmen, Holly and Bokov, Alex and Epstein, Charles J and Vijg, Jan and Richardson, Arlan
Aging Cell, ISSN 1474-9718, 02/2009, Volume 8, Issue 1, pp. 73 - 75
Summary We evaluated the effect of overexpressing antioxidant enzymes on the lifespans of transgenic mice that overexpress copper zinc superoxide dismutase... 
transgenic and knockout mice | aging | antioxidant enzymes | Aging | Antioxidant enzymes | Transgenic and knockout mice | CATALASE | UBIQUITOUS OVEREXPRESSION | MANGANESE SUPEROXIDE-DISMUTASE | ADULT DROSOPHILA-MELANOGASTER | EXPRESSION | TRANSGENIC MICE | CELL BIOLOGY | GERIATRICS & GERONTOLOGY | Superoxide Dismutase - genetics | Superoxide Dismutase - biosynthesis | Oxidative Stress | Catalase - genetics | Humans | Mice, Inbred C57BL | Mice, Transgenic | Reverse Transcriptase Polymerase Chain Reaction | Hydrogen Peroxide - metabolism | Animals | Mice | Catalase - biosynthesis | Longevity - physiology | Disease Models, Animal | Antioxidants | Physiological aspects | Medical colleges | Superoxide dismutase | Superoxide | Hydrogen peroxide | Short Take
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10. Full Text Titanium dioxide nanoparticles induce strong oxidative stress and mitochondrial damage in glial cells
by Huerta-García, Elizabeth and Pérez-Arizti, José Antonio and Márquez-Ramírez, Sandra Gissela and Delgado-Buenrostro, Norma Laura and Chirino, Yolanda Irasema and Iglesias, Gisela Gutiérrez and López-Marure, Rebeca
Free Radical Biology and Medicine, ISSN 0891-5849, 08/2014, Volume 73, pp. 84 - 94
Titanium dioxide nanoparticles (TiO NPs) are widely used in the chemical, electrical, and electronic industries. TiO NPs can enter directly into the brain... 
Nanoparticles | Oxidative stress | Free radicals | Lipoperoxidation | ROS | Mitochondrial damage | Glial cells | Titanium dioxide | PARTICLES | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | BRAIN MICROGLIA | IN-VITRO | REACTIVE OXYGEN | EPITHELIAL-CELLS | ENDOTHELIAL-CELLS | ENDOCRINOLOGY & METABOLISM | MICE | CYTOTOXICITY | TIO2 NANOPARTICLES | Superoxide Dismutase - genetics | Superoxide Dismutase - biosynthesis | Oxidation-Reduction | Catalase - genetics | Neuroglia - pathology | Fluoresceins - metabolism | Humans | Brain Injuries - chemically induced | Fatty Acids, Unsaturated - metabolism | Mitochondria - drug effects | Glutathione Peroxidase - biosynthesis | Membrane Potential, Mitochondrial - drug effects | Glutathione Peroxidase - genetics | Titanium - toxicity | RNA, Messenger - biosynthesis | Metal Nanoparticles - toxicity | Neuroglia - cytology | Cell Line, Tumor | Oxidative Stress - drug effects | Catalase - biosynthesis | Antioxidants | Enzymes | Evaluation | Brain | Lipids | Superoxide | Mitochondrial DNA | Injuries | Index Medicus
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11. Full Text Schwann Cells Expressing Dismutase Active Mutant SOD1 Unexpectedly Slow Disease Progression in ALS Mice
by Christian S. Lobsiger and Severine Boillee and Melissa McAlonis-Downes and Amir M. Khan and M. Laura Feltri and Koji Yamanaka and Don W. Cleveland
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2009, Volume 106, Issue 11, pp. 4465 - 4470
Neurodegeneration in an inherited form of ALS is non-cell-autonomous, with ALS-causing mutant SOD1 damage developed within multiple cell types. Selective... 
Motor neurons | Axons | Nervous system diseases | Astrocytes | Neuroglia | Schwann cells | Disease progression | Motor neuron disease | Amyotrophic lateral sclerosis | Sciatic nerve | Neurodegeneration | Non-cell-autonomous | Superoxide dismutase amyotrophic lateral sclerosis | motor neurons | non-cell-autonomous | PRIMARY TARGET | MULTIDISCIPLINARY SCIENCES | neurodegeneration | SPINAL-CORD | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | amyotrophic lateral sclerosis | FAMILIAL ALS | SCIATIC-NERVE | superoxide dismutase | MOUSE MODEL | LINKED SOD1 | SUPEROXIDE-DISMUTASE | TRANSGENIC MICE | Insulin-Like Growth Factor I - biosynthesis | Superoxide Dismutase - biosynthesis | Down-Regulation | Amyotrophic Lateral Sclerosis - prevention & control | Schwann Cells - metabolism | Disease Progression | Amyotrophic Lateral Sclerosis - pathology | Animals | Superoxide Dismutase - physiology | Mice | Neurons - metabolism | Superoxide Dismutase-1 | Disease Models, Animal | Development and progression | Health aspects | Biological Sciences
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12. Full Text Overexpression of Mn-superoxide dismutase in Oxya chinensis mediates increased malathion tolerance
by Wu, Haihua and Zhang, Jianzhen and Zhang, Yiwei and Shi, Xuekai and Ma, Enbo
Chemosphere, ISSN 0045-6535, 08/2017, Volume 181, pp. 352 - 359
Superoxide dismutase (SOD) is the first line of defense against oxidative damage. Malathion is an organophosphate insecticide and can induce the production of... 
Superoxide dismutase (SOD) | Malathion | RNA interference | Oxya chinensis | Transcriptional analysis | Recombinant proteins | IMMUNE-RESPONSE | PROTEIN | CU/ZN | SOD | CHALLENGE | ENVIRONMENTAL SCIENCES | CLONING | ENZYMES | RESISTANCE | STRESS | EXPRESSION | Up-Regulation | Animals | Reactive Oxygen Species - metabolism | Superoxide Dismutase - biosynthesis | Oxidation-Reduction | Grasshoppers - metabolism | Oxidative Stress - physiology | Escherichia coli - metabolism | Malathion - pharmacology | Insecticides | Superoxide Dismutase - metabolism | Proteins | Pets | Superoxide | RNA | Analysis
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13. Full Text Decreases in manganese superoxide dismutase expression and activity contribute to oxidative stress in persistent pulmonary hypertension of the newborn
by Afolayan, Adeleye J and Eis, Annie and Teng, Ru-Jeng and Bakhutashvili, Ivane and Kaul, Sushma and Davis, Jonathan M and Konduri, Girija G
American Journal of Physiology - Lung Cellular and Molecular Physiology, ISSN 1040-0605, 11/2012, Volume 303, Issue 10, pp. L870 - L879
Afolayan AJ, Eis A, Teng R, Bakhutashvili I, Kaul S, Davis JM, Konduri GG. Decreases in manganese superoxide dismutase expression and activity contribute to... 
Antioxidants | Endothelial nitric oxide synthase | Gene transduction | Catalase | Mitochondrial superoxide | Vasodilation | NADPH OXIDASE | CELLS | PHYSIOLOGY | ENDOTHELIAL NO SYNTHASE | antioxidants | vasodilation | 100-PERCENT OXYGEN | NITRIC-OXIDE SYNTHASE | RELAXING FACTOR | MITOCHONDRIA | gene transduction | mitochondrial superoxide | RESPIRATORY SYSTEM | GENE-EXPRESSION | endothelial nitric oxide synthase | HYDROGEN-PEROXIDE | catalase | FETAL LAMBS | Mitochondria - enzymology | Superoxide Dismutase - genetics | Adenoviridae | Superoxide Dismutase - biosynthesis | Oxidative Stress | Humans | Nitric Oxide Synthase Type III - biosynthesis | RNA, Messenger - biosynthesis | Vasodilation - genetics | Mitochondria - genetics | Superoxides - metabolism | Infant, Newborn | Persistent Fetal Circulation Syndrome - physiopathology | Disease Models, Animal | Nitric Oxide - biosynthesis | Transduction, Genetic | RNA, Messenger - genetics | Persistent Fetal Circulation Syndrome - genetics | Pulmonary Artery - physiopathology | Mitochondria - pathology | Nitric Oxide Synthase Type III - genetics | Pulmonary Artery - enzymology | Hydrogen Peroxide - metabolism | Gene Expression Regulation, Enzymologic | Animals | Nitric Oxide - genetics | Sheep | Endothelial Cells - pathology | Genetic Vectors | Endothelial Cells - enzymology | Persistent Fetal Circulation Syndrome - pathology | Pulmonary Artery - pathology | Persistent Fetal Circulation Syndrome - enzymology | Oxidative stress | Physiological aspects | Development and progression | Superoxide | Genetic aspects | Research | Gene expression | Health aspects | Pulmonary hypertension
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14. Full Text p53-Induced Up-Regulation of MnSOD and GPx but not Catalase Increases Oxidative Stress and Apoptosis
by Hussain, S. Perwez and Amstad, Paul and He, Peijun and Robles, Ana and Lupold, Shawn and