Relevant bibliographies by topics / Superoxide dismutase

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Superoxide dismutase'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 July 2024

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Journal articles on the topic "Superoxide dismutase"

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Öhman, Michael, and Stefan L. Marklund. "Plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-containing superoxide dismutase in alcoholics treated with disulfiram." Clinical Science 70, no. 4 (April 1, 1986): 365–69. http://dx.doi.org/10.1042/cs0700365.

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1. Disulfiram has long been used in the treatment of chronic alcoholism. It is in vivo partially reduced to diethyldithiocarbamate, which is an efficient inhibitor of Cu, Zn-containing superoxide dismutase both in vitro and in vivo. The recently described extracellular superoxide dismutase is even more sensitive to diethyldithiocarbamate than Cu, Zn-superoxide dismutase. 2. To test for the possibility that long term treatment with disulfiram leads to inhibition of the superoxide dismutases, plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-superoxide dismutase were determined in 12 disulfiram-treated alcoholics, and compared with 11 non-treated alcoholics and 19 healthy controls. 3. Plasma extracellular superoxide dismutase was moderately reduced (about 20%) in the disulfiram-treated alcoholics as compared with the non-treated alcoholics and the healthy controls. No effect of disulfiram treatment on erythrocyte Cu, Zn-superoxide dismutase activity was demonstrated.
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James, E. R. "Superoxide dismutase." Parasitology Today 10, no. 12 (January 1994): 481–84. http://dx.doi.org/10.1016/0169-4758(94)90161-9.

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YUASA, Makoto, Kenichi OYAIZU, and Hidenori MURATA. "Superoxide Dismutase Mimics." Oleoscience 6, no. 6 (2006): 307–17. http://dx.doi.org/10.5650/oleoscience.6.307.

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Simovic, Misho O., Martin J. D. Bonham, Fikri M. Abu-Zidan, and John A. Windsor. "Manganese Superoxide Dismutase." Pancreas 15, no. 1 (July 1997): 78–82. http://dx.doi.org/10.1097/00006676-199707000-00011.

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&NA;. "Superoxide dismutase cream." Inpharma Weekly &NA;, no. 796 (July 1991): 6. http://dx.doi.org/10.2165/00128413-199107960-00014.

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Rosenthal, Rosalind A., Susan R. Doctrow, and Wyeth B. Callaway. "Superoxide Dismutase Mimics." Antioxidants & Redox Signaling 14, no. 6 (March 15, 2011): 1173. http://dx.doi.org/10.1089/ars.2010.3758.

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Salvemini, Daniela, Carolina Muscoli, Dennis P. Riley, and Salvatore Cuzzocrea. "Superoxide Dismutase Mimetics." Pulmonary Pharmacology & Therapeutics 15, no. 5 (October 2002): 439–47. http://dx.doi.org/10.1006/pupt.2002.0374.

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Nozik-Grayck, Eva, Hagir B. Suliman, and Claude A. Piantadosi. "Extracellular superoxide dismutase." International Journal of Biochemistry & Cell Biology 37, no. 12 (December 2005): 2466–71. http://dx.doi.org/10.1016/j.biocel.2005.06.012.

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Hunaiti, A. "Radial Diffusion as a Simple and Rapid Method for Screening Superoxide Dismutase Activity." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 24, no. 5 (September 1987): 511–12. http://dx.doi.org/10.1177/000456328702400515.

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Superoxide dismutases are of great interest due to their increasing medical applications in therapy and diagnosis of some diseases. The radial diffusion assay was evaluated for its usefulness as a simple, cheap and accurate assay for screening superoxide dismutase activity. In this assay O2− radicals were generated from the interaction of reduced riboflavin with molecular oxygen upon exposure of agar gel containing riboflavin and N,N,N̄,N̄-tetramethylethylene diamine (TEMED) to light. If nitrotctrazolium dye is also present, it will be reduced to the blue insoluble formazan, whilst if superoxide dismutase is present it will prevent this blueing.1 The developed assay was found to give reproducible estimates of pure samples of superoxide dismutase with a lower limit of measurements of about 10 mg. It can be adapted to measure the levels of superoxide dismutase in various crude biological samples.
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Chary, P., D. Dillon, A. L. Schroeder, and D. O. Natvig. "Superoxide dismutase (sod-1) null mutants of Neurospora crassa: oxidative stress sensitivity, spontaneous mutation rate and response to mutagens." Genetics 137, no. 3 (July 1, 1994): 723–30. http://dx.doi.org/10.1093/genetics/137.3.723.

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Abstract Enzymatic superoxide-dismutase activity is believed to be important in defense against the toxic effects of superoxide. Although superoxide dismutases are among the best studied proteins, numerous questions remain concerning the specific biological roles of the various superoxide-dismutase types. In part, this is because the proposed damaging effects of superoxide are manifold, ranging from inactivation of certain metabolic enzymes to DNA damage. Studies with superoxide-deficient mutants have proven valuable, but surprisingly few such studies have been reported. We have constructed and characterized Neurospora crassa mutants that are null for sod-1, the gene that encodes copper-zinc superoxide dismutase. Mutant strains are sensitive to paraquat and elevated oxygen concentrations, and they exhibit an increased spontaneous mutation rate. They appear to have near wild-type sensitive to near- and far-UV, heat shock and gamma-irradiation. Unlike the equivalent Saccharomyces cerevisiae mutant and the sodA sodB double mutant of Escherichia coli, they do not exhibit aerobic auxotrophy. These results are discussed in the context of an attempt to identify consensus phenotypes among superoxide dismutase-deficient mutants. N. crassa sod-1 null mutant strains were also employed in genetic and subcellular fractionation studies. Results support the hypothesis that a single gene (sod-1), located between Fsr-12 and leu-3 on linkage group I, is responsible for most or all CuZn superoxide dismutase activity in this organism.
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Dissertations / Theses on the topic "Superoxide dismutase"

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Dufernez, Fabienne. "Les superoxyde dismutases des protistes : caractérisation et origine phylogénétique." Lille 2, 2005. http://www.theses.fr/2005LIL2S030.

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Les organismes aérobies ont développé des mécanismes pour se protéger des attaques des espèces activées de l'oxygène produites lors du métabolisme cellulaire. La superoxyde dismutase (SOD) est une métalloenzyme du système de défense anti-oxydant. Elle catalyse la dismutation de l'anion superoxyde en peroxyde d'hydrogène. Les SOD se divisent en 2 grandes familles qui diffèrent fondamentalement d'un point de vue structural : les SOD qui utilisent simultanément le cuivre et le zinc comme métaux cofacteurs (Cu/Zn-SOD) et les SOD utilisant soit le fer (FeSOD) soit le manganèse (MnSOD) comme métal cofacteur. Sur la base d'un alignement de 261 séquences de SOD et de 12 structures cristallographiques de SOD à fer et à manganèse, nous avons analysé les conservations en terme de structure et de séquence parmi les SOD à fer et à manganèse. Les résidus caractéristiques de la fonction enzymatique, de la conformation en dimère ou tétramère et de la spécificité de métal ont été identifiés. Toutes ces données nous ont été utiles lors de nos études de SOD de nombreux protozoaires. Les protozoaires parasites étudiés jusqu'à présent ont ,en effet, la particularité de ne contenir qu'un seul type de SOD, des FeSOD qui différent des Cu/Zn SOD et SOD tétramérique à manganèse présentes chez l'humain. Ceci fait de la SOD à fer des protistes une cible thérapeutique potentielle. Chez Trypanosoma brucei, agent de la maladie du sommeil, nous avons identifié 4 gènes de SOD après interrogation des banques de données du programme de séquençage : soda, sodb1 et sodb2 ainsi que sodc nouvellement identifié. Ces 4 gènes correspondaient à des SOD dimériques à fer. Les protéines recombinantes correspondantes ont été produites et se sont révélées actives. Des modélisations structurales ont été réalisées par homologie avec des structures cristallographiques connues et ont montrées une grande similarité de structure entre ces FeSOD. Afin de déterminer la localisation cellulaire, nous avons réalisé des expériences de fusion de chacune de ces enzymes avec la GFP, ces constructions ont été transfectées dans des cellules procycliques de trypanosome. Nous avons alors mis en évidence la localisation mitochondriale des 2 enzymes FeSODA et FeSODC et la présence des FeSODB dans le cytoplasme et les glycosomes, localisation confirmée par un marquage sur fractions cellulaires : la FeSODB1 étant plutôt cytosolique et la FeSODB2 plutôt glycosomale. Chez le dinoflagellé Crypthecodinium cohnii nous n'avons retrouvé que des activités SOD correspondantes à des SOD à fer. Une famille multigénique codant pour des FeSOD a été caractérisée. La protéine recombinante correspondante à un gène complet de FeSOD dimérique a été produite et s'est révelée active. Les SOD d'un second prostiste parasite Trichomonas vaginalis ont également été étudiées. T. Vaginalis est responsable de la trichomoniase humaine, la maladie sexuellement transmissible la plus répandue à travers le monde. La recherche dans les bases de données du programme de séquençage du parasite nous a permis d'identifier 7 gènes de SOD chez ce parasite. Ces SOD comportent toutes les caractéristiques des SOD à fer dimériques et sont actives lorsqu'on les produit sous forme de protéines recombinantes. La protéine recombinante SOD6 de T. Vaginalis a été également purifiée et la structure cristallographique obtenue. Ces données sont essentielles pour la conception éventuelle d'inhibiteurs. Toutes ces séquences de FeSOD ont été incluses dans une large analyse phylogénétique afin de proposer une origine pour les FeSOD des protistes. Cette analyse confirme l'origine bactérienne de ces enzymes via des transferts de gènes de bactéries vers les protistes, suivi de duplications successives.
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Olofsson, Eva. "Superoxide dismutase 1 and cataract." Doctoral thesis, Umeå : Umeå universitet, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-21032.

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Kolahi-Ahari, Ali. "A study of superoxide dismutase activity and superoxide production in kiwifruit." Thesis, University of Canterbury. Biological Sciences, 2006. http://hdl.handle.net/10092/1343.

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The activity of superoxide dismutase (SOD) was determined in three kiwifruit (Actinidia) species including A. deliciosa, A. chinensis, and A. arguta. Among the species tested, the highest SOD activity was found in crude extracts prepared from fruit tissues of A. deliciosa. The highest enzyme activity was localized in seed, followed by locules, core and outer pericarp (OP). SOD activity in crude extract of whole fruit remained stable for at least one month when stored at -20℃. The effect of synthetic protease inhibitors (PI) on SOD activity was investigated. Supplementing crude kiwifruit extracts with PI improved SOD activity in freshly prepared extracts, and in extracts stored at 4℃, but had no effect on those stored at -20℃. Among the PI used, iodoacetamide (an inhibitor of cysteine proteases, for example, actinidin which is a principal protease found in kiwifruit) and PMSF (an inhibitor of serine proteases), had the most and least influence on SOD activity in crude kiwifruit extracts, respectively. There was a significant increase in SOD activity in kiwifruit (that were relatively firm) when the fruits were stored at low temperature (4℃). An increase in SOD activity was also correlated with a decrease in fruit firmness. Staining fruit tissues with nitroblue tetrazolium (NBT) provided evidence for stress-induced superoxide generation in kiwifruit tissues. Taken together, the changes in SOD activity and the capacity for stress-inducible superoxide production in post-harvest kiwifruit suggest that SOD might play a fundamental role in the storage life/ripening of kiwifruit.
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Parker, Michael William. "Structural studies on manganese superoxide dismutase." Thesis, University of Oxford, 1985. https://ora.ox.ac.uk/objects/uuid:b8fff51f-1e2f-41b1-baff-4e95b499f0de.

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Superoxide dismutases are widely distributed enzymes which catalyse the dismutation of superoxide radicals to dioxygen and hydrogen peroxide and are considered to be an important agent of an organism's defence against oxygen toxicity. The crystallization and low resolution structure determination of manganese superoxide dismutase (E.G. 1.15.1.1) from Bacillus stearothermophiluB is described. The enzyme crystallized in space group P21212 with two monomers per asymmetric unit and cell dimensions of ̲a=72.2Å, ̲b=111.1Å and ̲c=51.1Å. The crystals diffracted to beyond 2Å resolution but were fragile and prone to cell dimension changes. The cell dimension variability was overcome to some extent by crossllnking with glutaraldehyde. An electron density map was calculated to 6Å resolution initially by the method of multiple isomorphous replacement using data obtained from six heavy atom derivatives. The final map was calculated from single isomorphous replacement data using a map modification procedure. The fitting of an alpha carbon model of iron superoxide dismutase into the map suggested the iron and manganese enzymes are structurally related. The position of the metal atoms in the model solved difference Patterson maps calculated from data collected from a manganese-free crystal and from anomalous dispersion data. The latter data were collected using synchrotron radiation tuned close to the manganese absorption edge. The low resolution map and the availability of 2.4Å resolution native data paves the way for higher resolution X-ray studies of the crystals. A detailed analysis of amino acid sequences has been carried out on the various metal-containing superoxide dismutases. The results indicate that the enzymes can be classified according to their metal cofactor. The distribution and homology of the enzyme classes supports the endosymbiotic theory of the origin of cell organelles. The presence of the copper/zinc enzyme in Photobacterium leiognathi is shown to support the case for a eukaryote to prokaryote gene transfer.
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Barkley, Katherine Byer. "Characterization of superoxide dismutase from Actinomyces." Diss., Virginia Polytechnic Institute and State University, 1988. http://hdl.handle.net/10919/53905.

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The anaerobes Actinomyces naeslundii, A. odontolyticus and Actinomyces strain ii E1S.25D produce a Mn-containing superoxide dismutase (MnSOD). Actinomyces, once classified as yeast based on their morphology, are saprophytic organisms found among the normal flora of the mouth but can act as endogenous pathogens resulting in gingivitis and actinomycosis. The ability of Actinomyces to scavenge superoxide may increase survival of the cell from the O₂⁻-dependent killing by polymorphonuclear leukocytes and also enable the organism to be transported through an oxygenated environment from one site to another. The MnSODs were purified 85-240 fold from crude extracts with 30-60% yield by two chemical fractionations and three chromatography steps. The enzymes, Mr 96,000, were tetramers of equally sized, noncovalently associated subunits similar to the MnSOD found in Saccharomyces cerevisiae. Each of the Actinomyces MnSODs contained 0.5 g-atoms Mn/subunit and were stable in the presence of 1 mM NaCN, 1 mM NaN₃ and 2.5 mM H₂O₂. The MnSODs from Actinomyces have isoelectric points of 4.2-4.6 and are negatively charged at physiological pH. Amino acid analyses of the high molecular weight MnSODs from Actinomyces, yeast, chicken liver, and Thermus thermophilus indicated similar composition of each subunit. The second order rate constants of each Actinomyces MnSOD were measured at pH 7.8 and found to be in the range of 0.9 - 2.8 x 10⁹ M⁻¹ sec⁻¹ as compared to the rate of 1.8 x 10⁹ M⁻¹ sec⁻¹ for yeast MnSODs. Structural relatedness was evaluated by immunological studies. Rabbit antisera to each of the Actinomyces MnSODs were prepared. The MnSODs from A. naeslundii and Actinomyces strain E1S.25D both showed complete identity with their respective antibodies and partial identity with the antibody prepared against A. odontolyticus MnSOD. None of the antisera cross reacted with bovine Cu/Zn SOD, Bacteroides Fe- or MnSOD or MnSODs from either Haemophilus influenzae, Deinococcus radiodurans, or S. cerevisiae.
Ph. D.
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Meissner, Felix. "Superoxide dismutase 1 regulates caspase-1." Berlin mbv, 2008. http://d-nb.info/992999286/04.

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Jonsson, P. Andreas. "Superoxide dismutase 1 and amyotrophic lateral sclerosis." Doctoral thesis, Umeå : Medical Biosciences, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-611.

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Enayat, Zinat Ellaheh. "Superoxide dismutase mutations and amyotrophic lateral sclerosis." Thesis, King's College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.400500.

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Blackney, Michael James. "Characterising the Drosophila extracellular superoxide Dismutase gene." Thesis, University of Southampton, 2010. https://eprints.soton.ac.uk/179761/.

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The indiscriminate action of reactive oxygen species (ROS), if left unregulated, has long been considered contributory to a range of disease processes within the animal kingdom and is also a factor associated with ageing. Consequently modifying the molecular mechanisms that regulate ROS levels may prove therapeutic and could also positively affect longevity. One of the key components of this machinery is the superoxide dismutase (SOD) family of enzymes which regulate ROS levels by scavenging the ROS superoxide. Mammals have three distinct SOD enzymes each responsible for managing superoxide levels in different cellular compartments. In Drosophila homologues of two of the mammalian SODs, the intracellular (SOD1) and mitochondrial (SOD2) SODs, have been identified and studied extensively demonstrating a clear link between SOD and oxidative protection and survival. Recently the sequence of a third sod gene, homologous to both the relatively poorly characterised mammalian (sod3) and C. elegans (sod-4) extracellular sod, was identified in Drosophila and is also predicted to locate extracellularly (sod3). To date, no (published) work has been carried out to assess the role of sod3 within insects. This thesis reports the molecular and biochemical characteristics of sod3 in Drosophila. Detailed within are the steps taken to clone the sod3 gene which appears to be expressed as two gene products formed by alternative splicing. Furthermore, a combination of gene expression, proteomic and functional analysis of a number of sod mutants was used to: i) reveal sex specific sod gene expression; ii) validate a sod3 hypomorph mutant; iii) indicate a functional role for sod3 in protection against H2O2 induced oxidative stress; iv) suggest a SOD1-SOD3 co-dependency for maintaining Cu Zn SOD activity; v) demonstrate the appearance of genetic modifiers in the sod3 hypomorph. The findings of this report and further studies on the Drosophila sod3 gene should encourage the re-evaluation of the previous work concerning SOD’s influence on disease states and lifespan regulation.
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Matemadombo, Fungisai. "Metallophthalocyanines as electrocatalysts and superoxide dismutase mimics." Thesis, Rhodes University, 2010. http://hdl.handle.net/10962/d1004985.

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Syntheses, spectral, electrochemical, and spectroelectrochemical studies of iron, cobalt, and manganese phthalocyanines are reported. The novel coordination of cobalt tetracarboxy metallophthalocyanine to an electrode premodified with aryl radicals and its use in the detection of thiocyanate are reported. This work describes the catalytic activity of cobalt phthalocyanine (CoPc) derivatives adsorbed onto glassy carbon electrodes for the electrocatalytical detection of nitrite, Lcysteine, and melatonin. The modified electrodes efficiently detected nitrite. The CoPc derivative modified electrodes proficiently detected L-cysteine whereas an un-modified electrode could not. This work presents the innovative electrochemical detection of melatonin using electrodes adsorbed with CoPc derivatives. These electrodes detected melatonin at more favorable electrochemical parameters relative to an un-modified gold electrode. The limits of melatonin detection of the modified electrodes lay in the 10⁻⁷ to 10⁻⁶ M region. The modified electrodes accurately detected capsule melatonin concentrations as specified by the supplier and could differentiate between a mixture of melatonin, tryptophan, and ascorbic acid. They reliably detected nitrite, L-cysteine, and melatonin in the 10⁻⁴ to 10⁻² M region. Metallophthalocyanine complexes substituted with thio groups were employed as self assembled monolayers (SAMs). Voltammetry, impedance, atomic force microscopy, and scanning electrochemical microscopy proved that the SAMs all act as selective and efficient barriers to ion permeability. All the SAMs in this work can be used as effective electrochemical sensors of nitrite and L-cysteine in the 10⁻⁴ to 10⁻² M region with competitive limits of detection whereas an un-modified electrode cannot detect Lcysteine. The manganese phthalocyanine SAM modified electrodes are arguably better nitrite and L-cysteine electrocatalysts relative to their iron and cobalt counterparts. Manganese phthalocyanines were used as superoxide dismutase (SOD) mimics. All manganese phthalocyanine complexes in this work acted as SOD mimics in an enzymatic system of superoxide production. From cellular studies, complexes 6d, 6e, 8d, 8e act as intracellular SOD mimics and are without significantly high cellular toxicity.
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Books on the topic "Superoxide dismutase"

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Lester, Packer, ed. Superoxide dismutase. San Diego, Calif: Academic Press, 2002.

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Karlsson, Kurt. Extracellular-superoxide dismutase: Association with glycosaminoglycans. [s.l.]: [s.n.], 1988.

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International Conference on Superoxide and Superoxide Dismutase (4th 1985 Rome, Italy). Superoxide and superoxide dismutase in chemistry, biology, and medicine: Proceedings of the 4th International Conference on Superoxide and Superoxide Dismutase, held in Rome, Italy, 1-6 September 1985. Amsterdam: Elsevier Science Publishers, 1986.

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Ingrid, Emerit, Packer Lester, Auclair Christian, and Society for Free Radical Research., eds. Antioxidants in therapy and preventive medicine. New York: Plenum Press, 1990.

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Joyce, Caroline. Superoxide dismutase gene expression in copper deficient rats. [S.l: The Author], 1992.

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Karpinski, Stanislaw. Copper-zinc superoxide dismutases in Scots pine (Pinus sylvestris L.): Analyses of isoforms, cDNAs and environmental stress responses. Umeå: Swedish University of Agricultural Sciences, Faculty of Forestry, Dept. of Forest Genetics and Plant Physiology, 1994.

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Murphy, Loretta Mary. XaAFS and EPR studies on Bovine Cu, Zn Superoxide dismutase. Manchester: University of Manchester, 1995.

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Kang yang hua jiao su zhi mu SOD. Taibei Shi: Yuan qi zhai chu ban she you xian gong si, 2016.

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Hough, Michael Alexander. A crystal structure study of CuZn superoxide dismutase from bovine erythrocytes. Leicester: De Montfort University, 1998.

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Ayub, M. A. Z. Effects of recombination and environmental conditions on superoxide dismutase production by yeast. Manchester: UMIST, 1991.

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Book chapters on the topic "Superoxide dismutase"

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Bährle-Rapp, Marina. "Superoxide Dismutase." In Springer Lexikon Kosmetik und Körperpflege, 539. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_10232.

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Schomburg, Dietmar, and Dörte Stephan. "Superoxide dismutase." In Enzyme Handbook, 853–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_179.

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Gooch, Jan W. "Superoxide Dismutase." In Encyclopedic Dictionary of Polymers, 926. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14898.

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Bryngelson, Peter A., and Michael J. Maroney. "Nickel Superoxide Dismutase." In Nickel and Its Surprising Impact in Nature, 417–43. Chichester, UK: John Wiley & Sons, Ltd, 2007. http://dx.doi.org/10.1002/9780470028131.ch10.

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Ryan, Kelly C., and Michael J. Maroney. "Nickel Superoxide Dismutase." In Encyclopedia of Metalloproteins, 1505–15. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_84.

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Leung, Alexander K. C., Cham Pion Kao, Andrew L. Wong, Alexander K. C. Leung, Thomas Kolter, Ute Schepers, Konrad Sandhoff, et al. "Superoxide Dismutase Defects." In Encyclopedia of Molecular Mechanisms of Disease, 2008–10. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_1691.

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Laukkanen, Mikko O., and Alessia Parascandolo. "Superoxide Dismutase 1-3." In Encyclopedia of Signaling Molecules, 5232–38. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101647.

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Pecci, Laura, Gabriella Montefoschi, Mario Fontana, Silvestro Duprè, Mara Costa, and Doriano Cavallini. "Hypotaurine and Superoxide Dismutase." In Advances in Experimental Medicine and Biology, 163–68. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/0-306-46838-7_17.

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Laukkanen, Mikko O., and Alessia Parascandolo. "Superoxide Dismutase 1-3." In Encyclopedia of Signaling Molecules, 1–6. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101647-1.

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D’Orazio, Melania, and Andrea Battistoni. "Zinc in Superoxide Dismutase." In Encyclopedia of Metalloproteins, 2444–48. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_197.

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Conference papers on the topic "Superoxide dismutase"

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Meoni, E., EA Regan, J. Luby, RP Bowler, and JD Crapo. "Extracellular Superoxide Dismutase in COPD and Healthy Smokers." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4175.

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Ganguly, K., M. Depner, SC Wesselkamper, M. Schreiber, F. Gao, TD Oury, EV Mutius, M. Kabesch, GD Leikauf, and H. Schulz. "Superoxide Dismutase 3, Extracellular (SOD3) Variants and Lung Function." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1790.

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Ghosh, Sudakshina, Belinda Willard, Suzy A. Comhair, Kulwant S. Aulak, Michael Kinter, and Serpil C. Erzurum. "Janus Function Of Copper-Zinc Superoxide Dismutase In Human Asthma." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2791.

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Stojiljković, Vesna, Ljubica Gavrilović, Snežana Pejić, Ana Todorović, Nataša Popović, Ivan Pavlović, and Snežana B. Pajović. "SUPEROXIDE DISMUTASE AND LIPID PEROXIDATION IN CHILDREN AFFECTED BY CELIAC DISEASE." In RAD Conference. RAD Association, 2017. http://dx.doi.org/10.21175/radproc.2017.49.

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Faisal, Muhammad Ali, Salsa Maulida, Siti Intania Mairudi, and Eko Suhartono. "Superoxide dismutase and catalase activity in cataract lens of diabetes mellitus." In INTERNATIONAL CONFERENCE ON BIOINFORMATICS AND NANO-MEDICINE FROM NATURAL RESOURCES FOR BIOMEDICAL RESEARCH: 3rd Annual Scientific Meeting for Biomedical Sciences. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5110016.

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Schwindt, CD, S. Leu, F. Zaldivar, and DM Cooper. "Brief Exercise Decreases Superoxide Dismutase in Healthy, but Not Asthmatic Children." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1289.

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Cui, Ye, Jennifer Robertson, Shyam Maharaj, Lisa Waldhauser, Laszlo Farkas, Martin R. J. Kolb, and Jack Gauldie. "Gene Transfer Of Extracellular Superoxide Dismutase Ameliorates Pulmonary Fibrosis In Rats." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2003.

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Xiaoming Hang, Cong Liu, Yang Liu, and Yeqing Sun. "Joint toxic effects of naphthalene and cadmium on zebrafish superoxide dismutase." In 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5964306.

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Ghosh, Sudakshina, Belinda Willard, Suzy Comhair, Weiling Xu, Sruti Shiva, Kulwant Aulak, Michael Kinter, and Serpil C. Erzurum. "Redox Dependent Function Of Copper-Zinc Superoxide Dismutase In Human Asthma." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4960.

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Mizushima, Tohru, and Ken-ichiro Tanaka. "Protective And Therapeutic Effects Of Lecithinized Superoxide Dismutase Against Pulmonary Fibrosis." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5180.

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Reports on the topic "Superoxide dismutase"

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Champaigne, Rachel. The Role of Mitochondrial Superoxide Dismutase (SOD2) During a Coxiella Burnetii Infection. Portland State University Library, January 2015. http://dx.doi.org/10.15760/honors.168.

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Mozgovaya, E. E., S. A. Bedina, I. A. Zborovskaya, A. S. Trofimenko, M. A. Mamus, E. A. Tikhomirova, and S. S. Spitsina. XANTHINE OXIDOREDUCTASE AND SUPEROXIDE DISMUTASE ACTIVITIES OF BLOOD PLASMA DEPENDING ON TYPE OF SYSTEMIC SCLEROSIS. "PLANET", 2019. http://dx.doi.org/10.18411/978-5-907192-54-6-2019-xxxvi-120-127.

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สุขหร่อง, สุชาดา, and วรวุฒิ จุฬาลักษณานุกูล. โครงการ การศึกษาคุณสมบัติการกระตุ้นทางชีวภาพของน้ำหมักชีวภาพจากพืชต่อความทนทานภายใต้สภาวะเครียดจากออกซิเดชันในข้าว : รายงานวิจัยฉบับสมบูรณ์. คณะเภสัชศาสตร์ จุฬาลงกรณ์มหาวิทยาลัย, 2009. http://dx.doi.org/10.58837/chula.res.2009.3.

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งานวิจัยนี้สามารถแยกเชื้อแบคทีเรียกลุ่มที่สังเคราะห์แสงจากดินและน้ำหมักจากฟางข้าวในแปลงเกษตรอินทรีย์ได้ ซึ่งได้แก่เชื้อ Rhodopseudomanas palustris ไอโซเลทที่ 59 ที่สามารถสร้างสาร 5-aminolevulinic acid (ALA) ที่มีรายงานว่าเป็นสารที่มีประโยชน์กับพืช และนำไปใช้ในการผลิตน้ำหมักชีวภาพจากพืช โดยสามารถใช้สาร ALA นี้เป็นสารเครื่องหมาย (marker) ในการควบคุมคุณภาพของน้ำหมักชีวภาพ การเจือจางน้ำหมักชีวภาพที่ความเข้มข้น 1:500 เป็นสัดส่วนที่เหมาะสมที่สุดในการเป็นตัวกระตุ้นทางชีวภาพซึ่งทำให้ข้าวมีความสูง การเจริญเติบโต การงอก ความยาวราก และดัชนีการงอกของเมล็ดข้าวดีกว่ากลุ่มควบคุมที่ใช้น้ำเปล่า ผลของน้ำหมักชีวภาพที่มีต่อความทนทานของข้าวภายใต้สภาวะเครียดจากออกซิเดชันโดยการเหนี่ยวนำจากสารเคมี aminotriazole (AT) buthionine sulfoximine (BSO) และ methyl viologen (MV) โดยวัดการทำงานของเอนไซม์แอนติออกซิแดนท์และการเปลี่ยนแปลงของการแสดงออกของยีน superoxide dismutase (SOD), ascorbate peroxidase (APX), และ catalase (CAT) พบว่าสามารถเหนี่ยวนำต้นข้าวอ่อนให้เกิดสภาวะเครียดจากออกซิเดชันสารเคมีได้โดยการใช้สารเคมี ถึงแม้ว่าจะสังเกตเห็นลักษณะที่ทนทานทาง phenotype ได้ไม่ชัดเจนในต้นข้าวอ่อนกลุ่มที่ได้รับและไม่ได้รับการ pretreat ด้วยน้ำหมักชีวภาพเมื่อถูกเหนี่ยวนำให้เกิดความเครียด แต่ได้มีการเปลี่ยนแปลงในระดับของยีนและเอนไซม์กลุ่มต้านออกซิเดชัน ต้นข้าวอ่อนกลุ่มที่ได้รับการ pretreat ด้วยน้ำหมักชีวภาพก่อนพบว่ามีระดับ transcript ของยีนและการทำงานของเอนไซม์ SOD APX และ CAT สูงอยู่ก่อนแล้ว ต้นข้าวอ่อนกลุ่มนี้มีการตอบสนองต่อสารเคมีที่ใช้เหนี่ยวนำให้เกิดความเครียดได้ไวกว่ากลุ่มที่ไม่ได้รับการ pretreat ด้วยน้ำหมักชีวภาพ เหมือนเป็นการเตรียมพร้อมให้กับต้นข้าวอ่อน เมื่อเวลาผ่านไประดับของ transcript และการทำงานของเอนไซม์จะลดลงสู่สภาวะปกติได้เร็วกว่า ชี้ให้เห็นว่าเมื่อต้นข้าวอ่อนกลุ่มที่ได้รับการ pretreat ด้วยน้ำหนักชีวภาพสามารถที่จะกระตุ้นกลไกการป้องกันตนเองให้จัดการกับภาวะเครียดได้อย่างรวดเร็วและลดลงสู่สภาวะปกติได้เร็ว
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Bedina, S. A., E. E. Mozgovaya, I. A. Zborovskaya, A. S. Trofimenko, and E. G. Korenskaya. ENZYMATIC PROFILE OF BLOOD PLASMA IN RHEUMATOID ARTHRITIS: ACTIVITY OF XANTHINE OXIDASE, XANTHINE DEHYDROGENASE AND SUPEROXIDE DISMUTASE. Планета, 2018. http://dx.doi.org/10.18411/978-5-907109-24-7-2018-xxxv-54-61.

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Bedina, S. A., E. E. Mozgovaya, A. S. Trofimenko, S. S. Spitsina, M. A. Mamus, and E. A. Tikhomirova. ENZYMATIC PROFILE OF BLOOD PLASMA IN SYSTEMIC SCLEROSIS: ACTIVITY OF XANTHINE OXIDASE, XANTHINE DEHYDROGENASE AND SUPEROXIDE DISMUTASE. "PLANET", 2019. http://dx.doi.org/10.18411/978-5-907192-54-6-2019-xxxvi-38-45.

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Bedina, S. A., E. E. Mozgovaya, A. S. Trofimenko, N. M. Devyataeva, M. A. Mamus, S. S. Spitsyna, and E. A. Tikhomirova. XANTHINE OXIDASE, XANTHINE DEHYDROGENASE AND SUPEROXIDE DISMUTASE ACTIVITIES OF BLOOD PLASMA DEPENDING ON CLINICAL FEATURES OF SYSTEMIC SCLEROSIS. Academy of Natural Knowledge, 2019. http://dx.doi.org/10.18411/1996-3955-2019-10-268-272.

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Plymate, Stephen R. Superoxide Dismutase and Transcription Factor sox9 as Mediators of Tumor Suppression by mac25 (IGFBP-rp1) in Prostate Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, October 2006. http://dx.doi.org/10.21236/ada463476.

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Zilinskas, Barbara A., Doron Holland, Yuval Eshdat, and Gozal Ben-Hayyim. Production of Stress Tolerant Plants by Overproduction of Enzymatic Oxyradical Scavengers. United States Department of Agriculture, May 1993. http://dx.doi.org/10.32747/1993.7568751.bard.

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Most of the objectives that were outlined in the original proposal have been met with two exceptions. Briefly, our goals were to: (1) constract transgenic tobacco plants which overproduce one or more of the enzymatic oxyradical scavengers and associated ancillary enzymes, including superoxide dismutase, ascorbate peroxidase, glutathione peroxidase, glutathione reductase, and monodehydrascorbate reductase; (2) evaluate the tolerance of these transgenic plants to oxidative stress; and (3) extend these studies to an agronomically important crop such as citrus. As can be seen i the following pages, our objectives (1) and (2) have been achieved, although transgenic lines overexpressing phospholipid hydroperoxidase glutathione peroxidase (PHGPX) were not obtained and our evidence to date suggests that constitutive overexpressing of the enzyme is probably lethal. Howeever, transgenic tobacco expressing the antisense construct for PHGPX were obtained. Tobacco plants overexpressing ascorbate peroxidase and those sensesuppressing monodehydroascorbate reductase are more tolerant to oxidative stress, as mediated by the redox-cycling agent paraquant; in contrast, plants expressing the PHGPX-antisense construct are more sensitive to paraquat. Additional research is warranted on each of the six types of transgenic lines which we generated with regard to their tolerance to saline stress. Until recently, attempts to transform citrus were not very successful, and thus additional attention is currently being directed at objective (3). We are optimistic that use of the plant transformation vector, pBIN, will lead to stable transgenic citrus, as preliminary experiments demonstrate stable expression of the GUS reporter gene. Other important contributions resulting from this BARD project include the biochemical characterization of the first plant phospholipid glutathione peroxidase and the biochemical and molecular analysis of another key antioxidant enzyme, monodehydroascorbate reductase. Overall this BARD-supported project was quite successful, and the biological resource of numerous transgenic lines which have altered levels of antioxidant enzymes should be valuable for years to come.
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Pesis, Edna, Elizabeth J. Mitcham, Susan E. Ebeler, and Amnon Lers. Application of Pre-storage Short Anaerobiosis to Alleviate Superficial Scald and Bitter Pit in Granny Smith Apples. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7593394.bard.

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There is increased demand for high quality fruit produced and marketed with reduced chemical inputs to minimize toxic effects on human health and the environment. Granny Smith (GS) apple quality is reduced by two major physiological disorders, superficial scald and bitter pit (BP). These disorders cause great loss to apple growers worldwide. Superficial scald is commonly controlled by chemical treatments, mainly the antioxidant diphenylamine (DPA) and/or the ethylene action inhibitor, 1-methylcyclopropene (1–MCP). Both chemicals are ineffective in controlling bitter pit incidence. We proposed to investigate the beneficial use of non-chemical, abiotic stress with low O2 (LO2) applied for 10d at 20°C on GS apple fruit. During the project we expanded the treatment to more apple cultivars, Golden Delicious (GD) and Starking Delicious (SD) and another pome fruit, the pear. Apple and pear have similar physiological disorders that develop during cold storage and we examined if the LO2 treatment would also be effective on pear. Application of 0.5% LO2 atmosphere for 10d at 20°C or 500ppb 1-MCP at 20°C prior to cold storage at 0°C, was effective in reducing superficial scald in GS apple. Moreover, LO2 pretreatment was also effective in reducing bitter pit (BP) development in California GS and Israeli GD and SD apples The BP symptoms in GS from California were much more prominent, so the effect of LO2 was more dramatic than the effect on the Israeli cvs. GD and SD, nevertheless the LO2 treatment showed the same trend in all cultivars in reducing BP. The LO2 and 1-MCP -treated fruit exhibited lower levels of ethylene, - farnesene and its oxidation product, 6-methyl-5-hepten-2-one (MHO), as determined by SPME/GC-MS analysis. In addition, LO2 pretreatment applied to California Bartlett or Israeli Spadona pears was effective in reducing superficial scald, senescent scald and internal breakdown after 4 m of cold storage at 0°C. For GS apple, low-temperature storage resulted in oxidative stress and chilling injury, caused by increased production of superoxide anions which in turn led to the generation of other dangerous reactive oxygen species (ROS). Using confocal laser-scanning microscopy and H2O2 measurements of apple peel, we observed ROS accumulation in control fruit, while negligible amounts were found in LO2 and 1-MCP treated fruit. Gene-expression levels of ROS-scavenging enzymes were induced by the various pretreatments: catalase was induced by LO2 treatment, whereas Mn superoxide dismutase was induced by 1-MCP treatment. We assume that LO2 and 1-MCP pretreated fruit remained healthier due to reduced production of ethylene and reactive oxygen substances, such as MHO, during cold storage. The LO2-treated apple exhibited greener peel and firmer fruit after 6 m of cold storage, and the fruit had high crispiness leading to high taste preference. In both pear cultivars, the LO2 treatment led to a reduction in internal breakdown and browning around the seed cavity. We tested the LO2 pre-storage treatment on a semi-commercial scale that would be applicable to a small organic grower by sealing the fruit within the plastic field bins. The treatment was most effective with a continuous flow of nitrogen through the bins; however, a single 6 hour flush of nitrogen was also fairly effective. In addition, we determined that it was very important to have the oxygen levels below 0.5% for approximately 10 days to achieve good scald control, not counting the time required to reduce the oxygen concentration. Our LO2 technology has been proven in this project to be effective in reducing several physiological disorders developed in pome fruit during cold storage. We hope that our non-chemical treatment which is friendly to the environment will be used in the near future for the organic apple and pear industry. The next step should be an analysis of the cost-benefits and commercial feasibility.
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Kanner, Joseph, Dennis Miller, Ido Bartov, John Kinsella, and Stella Harel. The Effect of Dietary Iron Level on Lipid Peroxidation of Muscle Food. United States Department of Agriculture, January 1995. http://dx.doi.org/10.32747/1995.7604282.bard.

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Biological oxidations are almost exclusively metal ion-promoted reactions and in ths respect iron, being the most abundant, is the commonly involved. The effect of dietary iron levels on pork, turkey and chick muscle lipid peroxidation and various other related compounds were evaluated. Crossbred feeder pigs were fed to market weight on corn-soy rations containing either 62, 131 or 209 ppm iron. After slaughter, the muscles were dissected, cooked and stored at 4°C. Heavily fortifying swine rations with iron (>200 ppm) increase nn-heme iron (NHI), thiobarbituric acid reactive substances (TBARS), and decrease a-tocopherol in cooked stored pork but did not increase warmed-over aroma (WOA). NHI and TBARS were higher in cooked pork from pigs fed high-iron diets. Liver iron correlated with muscle iron. TBARS were strongly related with WOA. The role of dietary vitamin E and ascorbic acid on Fe-induced in vivo lipid peroxidation in swine was also evaluated. Moderate elevation in iron stores had a marked effect on oxidative stress, especially as indicated by liver TBARS. Supplemental vitamin E, and to a lesser extent vitamin C, protect against this oxidative stress. Unsupplementation of Fe in the regular diet of turkeys did not affect body weight, blood hemoglobin level, or iron pool in the liver or muscle. The reason being that it contained "natural" ~120 mg Fe/kg feed, and this amount is high enough to keep constant the pool of iron in the body, liver or muscle tissues. Only Fe-supplementation with high amounts of Fe (500 ppm) significantly increased turkey blood hemoglobin and total iron in the liver, in 1 out of 3 experiments, but only slightly affects iron pool in the muscles. It seems that the liver accumulates very high concentations of iron and significantly regulates iron concentration in skeletal muscles. For this reason, it was very difficult to decrease muscle stability in turkeys through a diet containing high levels of Fe-supplementation. It was shown that the significant increase in the amount of iron (total and "free") in the muscle by injections with Fe-dextran accelerated its lipid peroxidation rate and decreased its a-tocopherol concentration. The level and metabolism of iron in the muscles affects the intensity of in vivo lipid peroxidation. This process was found to ifluence the turnover and accumulation of a-tocopherol in turkey and chick muscles. Treatments which could significantly decrease the amount and metabolism of iron pool in muscle tissues (or other organs) may affect the rate of lipid peroxidation and the turnover of a-tocopherol. Several defense enzymes were determined and found in the turkey muscle, such as superoxide dismutase, catalase, and glutathione peroxidase. Glutathione peroxidase was more active in muscles with a high trend of lipid peroxidation, lmore so in drumsticks than in breast muscles, or muscles with a low a-tocopherol content. The activity of glutathione peroxidase increased several fold in muscle stored at 4°C. Our work demonstrated that it will be much more practical to increase the stability of muscle tissues in swine, turkeys and chickens during storage and processing by increasing the amount of vitamin E in the diet than by withdrawing iron supplementation.
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