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1. Full Text The Structure of Human Extracellular Copper–Zinc Superoxide Dismutase at 1.7 Å Resolution: Insights into Heparin and Collagen Binding
by Antonyuk, Svetlana V and Strange, Richard W and Marklund, Stefan L and Hasnain, S. Samar and Medicinska fakulteten and Klinisk kemi and Institutionen för medicinsk biovetenskap and Umeå universitet
Journal of Molecular Biology, ISSN 0022-2836, 2009, Volume 388, Issue 2, pp. 310 - 326
Extracellular superoxide dismutase (SOD3) is a homotetrameric copper- and zinc-containing glycoprotein with affinity for heparin. The level of SOD3 is... 
heparin | collagen | extracellular superoxide dismutase | hyperoxia | stroke | Heparin - metabolism | Humans | Protein Multimerization | Crystallography, X-Ray | Zinc | Superoxide Dismutase - chemistry | Collagen - metabolism | Protein Binding | Protein Conformation | Superoxide Dismutase-1 | Copper | Binding Sites | Superoxide Dismutase - metabolism | Polyethylene glycol | Collagen | Nitric oxide | Crystals | Superoxide dismutase | Oxides | Chemical properties | Heparin | Structure | Index Medicus | extracellular superoxide dismutase; heparin; collagen; hyperoxia; stroke
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2. Full Text N‐Glycosylation is essential for the secretion of extracellular superoxide dismutase
by Ota, Fumi and Kizuka, Yasuhiko and Kitazume, Shinobu and Adachi, Tetsuo and Taniguchi, Naoyuki
FEBS Letters, ISSN 0014-5793, 10/2016, Volume 590, Issue 19, pp. 3357 - 3367
Extracellular superoxide dismutase ( EC ‐ SOD or SOD 3) protects against various oxidative stress‐related diseases by scavenging reactive superoxides in the... 
glycan | secretion | extracellular superoxide dismutase | Secretion | Glycan | Extracellular superoxide dismutase | SUBSTITUTION | VARIANTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LUNG-FUNCTION | NUCLEAR TRANSLOCATION | CELL BIOLOGY | HEPARIN-BINDING DOMAIN | BIOPHYSICS | INFLAMMATION | STRESS | EC-SOD | EXPRESSION | OXIDATIVE FRAGMENTATION | Superoxide Dismutase - chemistry | Humans | Secretory Pathway | HEK293 Cells | Glycosylation | Protein Processing, Post-Translational | Superoxide Dismutase - metabolism | Protein Transport | Index Medicus
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3. Full Text Extracellular superoxide dismutase suppresses hypoxia-inducible factor-1α in pancreatic cancer
by Sibenaller, Zita A and Welsh, Jessemae L and Du, Changbin and Du, Juan and Witmer, Jordan R and Schrock, Hannah E and Buettner, Garry R and Goswami, Prabhat C and Cieslak, John A and Cullen, Joseph J
Free Radical Biology and Medicine, ISSN 0891-5849, 04/2014, Volume 69, pp. 357 - 366
Hypoxia-inducible factor-1 (HIF-1) is a heterodimeric transcription factor that governs cellular responses to reduced oxygen availability by mediating crucial... 
Hypoxia-inducible factor | Superoxide | Extracellular superoxide dismutase | Free radicals | Pancreatic cancer | CELLS | ASSAY | ANGIOGENESIS | STABILIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIAL ROS | CARCINOGENESIS | ENDOCRINOLOGY & METABOLISM | DEGRADATION | HIF-1-ALPHA | EXPRESSION | ENDOTHELIAL GROWTH-FACTOR | Glutathione Peroxidase - metabolism | Pancreatic Neoplasms - metabolism | Neoplasm Proteins - biosynthesis | Antioxidants - metabolism | Humans | Pancreatic Neoplasms - pathology | Gene Expression Regulation, Neoplastic | Pancreatic Neoplasms - genetics | Signal Transduction - genetics | Vascular Endothelial Growth Factor A - metabolism | Glutathione Peroxidase - biosynthesis | Neoplasm Proteins - metabolism | Vascular Endothelial Growth Factor A - genetics | Hydrogen Peroxide - metabolism | Superoxides - metabolism | Transcription, Genetic | Tumor Cells, Cultured | Neoplasm Proteins - genetics | Index Medicus
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4. Full Text Histone acetylation regulates the cell-specific and interferon-γ - Inducible expression of extracellular superoxide dismutase in human pulmonary arteries
by Zelko, Igor N and Stepp, Marcus W and Vorst, Alan L and Folz, Rodney J
American Journal of Respiratory Cell and Molecular Biology, ISSN 1044-1549, 11/2011, Volume 45, Issue 5, pp. 953 - 961
Extracellular superoxide dismutase (EC-SOD) is the major antioxidant enzyme present in the vascular wall, and is responsible for both the protection of vessels... 
Promoter | Extracellular superoxide dismutase | Transcription | Pulmonary arteries | Epigenetic | Smooth muscle cells | Endothelial cells | endothelial cells | ACTIVATION | METHYLATION | CYTOKINES | transcription | epigenetic | PEROXYNITRITE | NITRIC-OXIDE SYNTHASE | IFN-GAMMA | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROLIFERATION | PROTECTS | CELL BIOLOGY | smooth muscle cells | RESPIRATORY SYSTEM | pulmonary arteries | promoter | extracellular superoxide dismutase | HYPERTENSION | Gene Expression Regulation, Enzymologic - drug effects | Superoxide Dismutase - genetics | Superoxide Dismutase - biosynthesis | Humans | STAT Transcription Factors - metabolism | Janus Kinases - metabolism | Interferon-gamma - metabolism | Promoter Regions, Genetic - drug effects | Pulmonary Artery - enzymology | Gene Expression Regulation, Enzymologic - genetics | CpG Islands | Histone Deacetylase Inhibitors - pharmacology | Epigenesis, Genetic - drug effects | Acetylation | Histones - metabolism | DNA Methylation - drug effects | Endothelial Cells - enzymology | Hydroxamic Acids - pharmacology | Muscle, Smooth, Vascular - enzymology | Endothelial Cells - drug effects | Muscle, Smooth, Vascular - drug effects | Index Medicus
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5. Full Text Overexpression of superoxide dismutase 3 gene blocks high-fat diet-induced obesity, fatty liver and insulin resistance
by Cui, R and Gao, M and Qu, S and Liu, D
Gene Therapy, ISSN 0969-7128, 09/2014, Volume 21, Issue 9, pp. 840 - 848
Oxidative stress has an important role in the development of obesity and obesity-associated metabolic disorders. As an endogenous antioxidant enzyme,... 
MEDICINE, RESEARCH & EXPERIMENTAL | POPULATION | OXIDATIVE STRESS | MACROPHAGES | BIOCHEMISTRY & MOLECULAR BIOLOGY | INJURY | RATS | GRAFT FUNCTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | DISEASE | GENETICS & HEREDITY | HORMONE ADIPONECTIN | EXTRACELLULAR-SUPEROXIDE DISMUTASE | EXPRESSION | Gene Transfer Techniques | Genetic Therapy | Superoxide Dismutase - genetics | Genetic Vectors - administration & dosage | Fatty Liver - blood | Liver - metabolism | Mice, Inbred C57BL | Fatty Liver - prevention & control | Gene Expression Regulation | Insulin Resistance | Diet, High-Fat - adverse effects | Male | Obesity - blood | Glucose Intolerance - blood | Adipose Tissue - metabolism | Glucose Intolerance - prevention & control | Animals | Obesity - prevention & control | Plasmids - genetics | Mice | Superoxide Dismutase - metabolism | Obesity | Care and treatment | Genetic transformation | Physiological aspects | Superoxide dismutase | Properties | Methods | Ketogenic diet | Oxidative stress | Gene therapy | Rodents | Metabolic disorders | Index Medicus | gene therapy | fatty liver | superoxide dismutase 3 | insulin resistance | obesity
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6. Full Text Epigenetic regulation of extracellular-superoxide dismutase in human monocytes
by Kamiya, Tetsuro and Machiura, Masatomo and Makino, Junya and Hara, Hirokazu and Hozumi, Isao and Adachi, Tetsuo
Free Radical Biology and Medicine, ISSN 0891-5849, 08/2013, Volume 61, pp. 197 - 205
Extracellular-superoxide dismutase (EC-SOD) is a major SOD isozyme mainly present in the vascular wall and plays an important role in normal redox homeostasis.... 
Extracellular-superoxide dismutase | DNA methylation | 12-O-tetradecanoylphorbol-13-acetate | Histone acetylation | Differentiation | 12-O- tetradecanoylphorbol-13-acetate | HISTONE ACETYLTRANSFERASES | OXIDATIVE STRESS | U937 CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-REGULATION | CANCER | HYPOMETHYLATION | ENDOCRINOLOGY & METABOLISM | EC-SOD | EXPRESSION | Azacitidine - pharmacology | Monocytes - enzymology | DNA Methylation | Superoxide Dismutase - genetics | Tetradecanoylphorbol Acetate - pharmacology | Epigenesis, Genetic | Humans | Cell Line, Tumor | Histones - metabolism | Extracellular Space - enzymology | Histones | Superoxide | Methylation | Laws, regulations and rules | Index Medicus
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7. Full Text Extracellular‐superoxide dismutase expression during monocytic differentiation of U937 cells
by Kamiya, Tetsuro and Makino, Junya and Hara, Hirokazu and Inagaki, Naoki and Adachi, Tetsuo
Journal of Cellular Biochemistry, ISSN 0730-2312, 01/2011, Volume 112, Issue 1, pp. 244 - 255
Leukemic cell lines, such as U937, THP‐1, and HL60 cells, can differentiate into macrophages following exposure to various agents including 12‐ O... 
12 | extracellular‐superoxide dismutase | nuclear factor‐κB | tetradecanoylphorbol‐13‐acetate | mitogen‐activated protein kinase | reactive oxygen species | Extracellular-superoxide dismutase | Mitogenactivated protein kinase | 12-O-tetradecanoylphorbol-13-Acetate | Reactive oxygen species | Nuclear factor-κB | 3T3-L1 ADIPOCYTES | COBALT CHLORIDE | NADPH OXIDASE | PROTEIN-KINASE-C | OXIDATIVE STRESS | METABOLIC SYNDROME | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR FACTOR-kappa B | MITOGEN-ACTIVATED PROTEIN KINASE | CELL BIOLOGY | SIGNAL-TRANSDUCTION | REACTIVE OXYGEN | REACTIVE OXYGEN SPECIES | 12-O-TETRADECANOYLPHORBOL-13-ACETATE | EXTRACELLULAR-SUPEROXIDE DISMUTASE | NF-KAPPA-B | EC-SOD | Superoxide Dismutase - genetics | Reactive Oxygen Species - metabolism | Tetradecanoylphorbol Acetate - pharmacology | Signal Transduction | U937 Cells | Humans | HL-60 Cells | NF-kappa B - metabolism | Cell Differentiation | RNA, Messenger - metabolism | Superoxide Dismutase - metabolism | Index Medicus
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8. Full Text Biomimetic superoxide dismutase stabilized by photopolymerization for superoxide anions biosensing and cell monitoring
by Yuan, Ling and Liu, Suli and Tu, Wenwen and Zhang, Zengsong and Bao, Jianchun and Dai, Zhihui
Analytical Chemistry, ISSN 0003-2700, 05/2014, Volume 86, Issue 10, pp. 4783 - 4790
Photopolymerization strategy, as one of the immobilization methods, has attracted considerable interest because of some advantages, such as easy operation,... 
NADPH OXIDASE | CHEMISTRY, ANALYTICAL | OXIDATIVE STRESS | 3RD-GENERATION BIOSENSOR | PHOTO-CROSS-LINKING | EXTRACELLULAR-SUPEROXIDE | ANTIOXIDATIVE SYSTEM | NUCLEOTIDE-BINDING SITE | DIRECT ELECTRON-TRANSFER | CARBON NANOTUBES | LIVING CELLS | Superoxide Dismutase - chemistry | Anions | Reactive Oxygen Species - chemistry | Biomimetics | Electrochemical Techniques | Humans | Biosensing Techniques | Cell Physiological Phenomena | Superoxides - chemistry | Polymerization | Enzymes, Immobilized | HeLa Cells | Superoxide dismutase | Radiation chemistry | Usage | Research | Nanotubes | Ultraviolet radiation | Biochemistry | Cellular biology | Biosensors | Index Medicus | Platforms | Photopolymerization | Irradiation | Photopolymers | Monitoring
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9. Full Text Inhibitory effects of extracellular superoxide dismutase on ultraviolet B-induced melanogenesis in murine skin and melanocytes
by Kim, Hae-Young and Kim, Tae-Yoon and Sah, Shyam Kishor and Choi, Sung S
Life Sciences, ISSN 0024-3205, 10/2018, Volume 210, pp. 201 - 208
Several anti-melanogenic molecules have been developed or identified, but their uses are limited due to either adverse effects or instability during the... 
Melanocytes | Extracellular superoxide dismutase | Melanogenesis | Endothelin-1 | MEDICINE, RESEARCH & EXPERIMENTAL | TGF-BETA | MELANOMA | SIGNALING PATHWAY | INFLAMMATION | NORMAL HUMAN KERATINOCYTES | NEWBORN MOUSE LUNG | PHARMACOLOGY & PHARMACY | MICE | VASCULAR ENDOTHELIAL-CELLS | GROWTH-FACTOR | EXPRESSION | Signal Transduction | Apoptosis - drug effects | Apoptosis - radiation effects | Rats, Inbred F344 | Cells, Cultured | Rats | Melanocytes - radiation effects | Superoxide Dismutase - administration & dosage | Animals | Ultraviolet Rays | Melanocytes - drug effects | Skin - radiation effects | Melanocytes - pathology | Cell Proliferation - drug effects | Skin - drug effects | Skin - pathology | Cell Proliferation - radiation effects | Antioxidants | Medical colleges | Endothelin | Bone morphogenetic proteins | Genetic engineering | Superoxide | Skin | Transforming growth factors | Gene expression | Mitogens | Protein kinases | Cell proliferation | Protein kinase A | Protein kinase C | Downstream effects | Genes | Homeostasis | Bromodeoxyuridine | Superoxide dismutase | Proteins | β-catenin | Signal transduction | Inhibition | a-Melanocyte-stimulating hormone | Growth factors | Microphthalmia-associated transcription factor | Enzymes | Stability | Transforming growth factor-b1 | Transgenic mice | Melanocortin | MAP kinase | Stability analysis | Endothelin 1 | Cells | Polymerase chain reaction | Signaling | Tyrosinase | Melanin | Index Medicus
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10. Full Text Histone deacetylation contributes to low extracellular superoxide dismutase expression in human idiopathic pulmonary arterial hypertension
by Nozik-Grayck, Eva and Woods, Crystal and Stearman, Robert S and Venkataraman, Sujatha and Ferguson, Bradley S and Swain, Kalin and Bowler, Russell P and Geraci, Mark W and Ihida-Stansbury, Kaori and Stenmark, Kurt R and McKinsey, Timothy A and Domann, Frederick E
American Journal of Physiology - Lung Cellular and Molecular Physiology, ISSN 1040-0605, 07/2016, Volume 311, Issue 1, pp. L124 - L134
Histone deacetylation contributes to low extracellular superoxide dismutase expression in human idiopathic pulmonary arterial hypertension. Am J Physiol Lung... 
DNA methylation | Idiopathic pulmonary arterial hypertension | Extracellular superoxide dismutase | Histone deacetylation | OXIDATIVE STRESS | PHYSIOLOGY | CELL-PROLIFERATION | POLYMORPHISM | CANCER | idiopathic pulmonary arterial hypertension | ECSOD EXPRESSION | SIRTUIN 3 DEFICIENCY | OVEREXPRESSION | DISEASE RISK | RESPIRATORY SYSTEM | EPIGENETIC REGULATION | histone deacetylation | extracellular superoxide dismutase | EC-SOD | Promoter Regions, Genetic | Gene Expression | Superoxide Dismutase - genetics | Myocytes, Smooth Muscle - enzymology | Humans | Middle Aged | Cells, Cultured | Rats | Male | Young Adult | Muscle, Smooth, Vascular - pathology | Animals | Adult | Female | Histone Deacetylase Inhibitors - pharmacology | Protein Processing, Post-Translational | Acetylation | Histones - metabolism | Enzyme Repression | Hypertension, Pulmonary - enzymology | Superoxide Dismutase - metabolism | Histones | Genetic aspects | Gene expression | Observations | Genetic regulation | Health aspects | Pulmonary hypertension | Enzymes | Protein expression | Index Medicus
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11. Full Text Extracellular superoxide dismutase ameliorates streptozotocin-induced rat diabetic nephropathy via inhibiting the ROS/ERK1/2 signaling
by Kuo, Chia-Wen and Shen, Chih-Jie and Tung, Yu-Tang and Chen, Hsiao-Ling and Chen, Chuan-Mu and Chen, Yu-Hsuan and Chang, Wen-Hui and Cheng, Kai-Chung and Yang, Shang-Hsun
Life Sciences, ISSN 0024-3205, 08/2015, Volume 135, pp. 77 - 86
Diabetic nephropathy is the leading cause of end stage renal disease in developed countries throughout the world. The imbalance between the production of... 
Mitogen activated protein kinase | Diabetic nephropathy | Transforming growth factor-beta | Extracellular superoxide dismutase | Angiotensin II receptor 1 | MEDICINE, RESEARCH & EXPERIMENTAL | CELLS | OXIDATIVE STRESS | PROTEIN-KINASE | RECEPTOR EXPRESSION | MELLITUS | GENE-EXPRESSION | NITRIC-OXIDE | PHARMACOLOGY & PHARMACY | UP-REGULATION | ENDOTHELIAL GROWTH-FACTOR | TRANSGENIC MICE | Diabetes Mellitus, Experimental - drug therapy | Diabetic Nephropathies - pathology | Reactive Oxygen Species - metabolism | Superoxide Dismutase - pharmacology | Kidney - pathology | Diabetic Nephropathies - metabolism | Humans | Diabetic Nephropathies - drug therapy | Rats | Male | Recombinant Proteins - pharmacology | Rats, Sprague-Dawley | Gene Expression Regulation - drug effects | Kidney - metabolism | Animals | MAP Kinase Signaling System - drug effects | Mitogen-Activated Protein Kinase 3 - metabolism | Diabetes Mellitus, Experimental - pathology | Phosphorylation - drug effects | Diabetes Mellitus, Experimental - metabolism | Antioxidants | Superoxide | Chronic kidney failure | Streptozocin | Diabetic nephropathies | Index Medicus
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12. Full Text Superoxide dismutase from Helicobacter pylori suppresses the production of pro‐inflammatory cytokines during in vivo infection
by Stent, Andrew and Every, Alison L and Chionh, Yok T and Ng, Garrett Z and Sutton, Philip
Helicobacter, ISSN 1083-4389, 02/2018, Volume 23, Issue 1, pp. e12459 - n/a
BackgroundHelicobacter pylori has undergone considerable adaptation to allow chronic persistence within the gastric environment. While H.pylori-associated... 
cytokines | Helicobacter pylori | immune response | superoxide dismutase | MYCOBACTERIUM-TUBERCULOSIS | OXIDATIVE STRESS | ACTIVATION | MICROBIOLOGY | EXTRACELLULAR-SUPEROXIDE | COLITIS | IMMUNE-RESPONSES | MOUSE MODEL | MICE | GASTROENTEROLOGY & HEPATOLOGY | NF-KAPPA-B | EXPRESSION | Cytokines | Monoclonal antibodies | Helicobacter infections | Superoxide | Health aspects | Antiulcer drugs | Pathogens | Immune response | Chronic infection | Cultures | Superoxide dismutase | Inflammation | Infections | Macrophages | Immunity | Gastritis | Lipopolysaccharides | Antioxidants | Immune systems | Rodents | Animal tissues | Bacteria | Mice | Colonization | Recombinant | Index Medicus
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13. Full Text Leukocyte-derived extracellular superoxide dismutase does not contribute to airspace EC-SOD after interstitial pulmonary injury
by Michelle L. Manni and Michael W. Epperly and Wei Han and Timothy S. Blackwell and Steven R. Duncan and Jon D. Piganelli and Tim D. Oury
American Journal of Physiology - Lung Cellular and Molecular Physiology, ISSN 1040-0605, 01/2012, Volume 302, Issue 1, pp. 160 - 166
The antioxidant enzyme extracellular superoxide dismutase (EC-SOD) is abundant in the lung and is known to limit inflammation and fibrosis following numerous... 
Antioxidant | Asbestos-induced pulmonary fibrosis | Extracellular superoxide dismutase | FIBROSIS | LOCALIZATION | antioxidant | asbestos-induced pulmonary fibrosis | PHYSIOLOGY | INDUCED LUNG INJURY | IN-SITU HYBRIDIZATION | HYPEROXIA | PROTECTS | RESPIRATORY SYSTEM | INFLAMMATION | MICE | extracellular superoxide dismutase | MOUSE LUNG | OXIDATIVE FRAGMENTATION | Lung - pathology | Superoxide Dismutase - secretion | Free Radical Scavengers - metabolism | Asbestos - administration & dosage | Mice, Inbred C57BL | Leukocytes - enzymology | Lung - enzymology | Mice, Knockout | Lung Injury - enzymology | Lung Injury - physiopathology | Animals | Pulmonary Fibrosis - enzymology | Pulmonary Fibrosis - physiopathology | Asbestos - adverse effects | Pulmonary Fibrosis - chemically induced | Bronchoalveolar Lavage Fluid - cytology | Mice | Bronchoalveolar Lavage Fluid - chemistry | Inflammation - enzymology | Superoxide Dismutase - metabolism | Disease Models, Animal |