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Superoxide dismutase 2 gene

Ceballos-Picot, I., Nicole, A., Briand, P., Grimber, G., Delacourte, A., Defossez, A., Javoy-Agid, F., Lafon, M., Blouin, J.L. and Sinet, P.M. (1991). Neuronal-specific expression of human copper-zinc superoxide dismutase gene in transgenic mice animal model of gene dosage effects in Down s syndrome. Brain Res, 552, 198-214. [Pg.81]

Rosen, D. R., Siddique, T., Patterson, D. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362 59-62, 1993. [Pg.665]

Das KC, Guo X, White CW (1998) Protein kinase C8-dependent induction of Manganese superoxide dismutase gene e q>ression by microtubule-active anticancer drugs. J Biol Chem 273 34639-34645... [Pg.67]

R., Morrison, J. H. and Gordon, J. W. (1995) Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 92, 689-693. [Pg.388]

Andersen PM, Sims KB, Xin WW, Kiely R, O Neill G, Ravits J, Pioro E, Harati Y, Brower RD, Levine JS, Heinicke HU, Seltzer W, Boss M, Brown RH Jr. (2003) Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis a decade of discoveries, defects and disputes. Amyotroph Lateral Scler Other Motor Neuron Disord 4 62-73... [Pg.39]

Morita, S., Kaminaka, H., Yokoi, H., Masumara, T., and Tanaka, K., 1997, Differential responses of two cytosolic superoxide dismutase genes and two cytosolic ascorbate peroxidase genes in rice to environmental stresses. Plant Physiol. 114 102. [Pg.347]

Nettleton CJ, Bull C, Baldwin TO, Fee JA. (1984). Isolation of the Escherichia coli iron superoxide dismutase gene Evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase. Proc Nat Acad Sci USA 81 4970-4973. [Pg.507]

Rosen DR, Siddique T, Patterson D, Eiglewicz DA, Sapp P, Hentad A, Donaldson D, Goto J, O Regan JP, Deng HX, et al. (1993) Mutadons in Cu/Zn superoxide dismutase genes are associated widi familial amyotrophic lateral sclerosis. Nature 362 59—62. [Pg.387]

Yoo, H.Y., M.S. Chang and H.M. Rho. The activation of the rat copper/zinc superoxide dismutase gene by hydrogen peroxide through the hydrogen peroxide-responsive element and by paraquat and heat shock through the same heat shock element. J. Biol. Chem. 21 A 23887—23892, 1999. [Pg.394]

Dl. Danciger, E., Dafni, N., Bernstein, Y., Laver-Rudich, Z., Neer, A., and Groner, Y., Human Cu,Zn superoxide dismutase gene family Molecular stmcture and characterization of four Cu,Zn superoxide dismutase-related pseudogenes. Proc. Natl. Acad. Sci. U.SA. 83,3619-3623... [Pg.50]

Gralla EB, Thiele DJ, Silar P, Valentine JS. ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc Natl Acad Sci USA 88 8558-8562, 1991. [Pg.471]

Zhong Z, Connor HD, Yin M, Wheeler MD, Mason RP, Thurman RG. Viral delivery of superoxide dismutase gene reduces cyclosporine A-induced nephrotoxicity. Kidney Int 2001 59 1397-1404. [Pg.442]

Mossman BT, Surinrut P, Brinton BT, et al. 1996. Transfection of a manganese-containing superoxide dismutase gene into hamster tracheal epithelial cells ameliorates asbestos-mediated cytotoxicity. Free Radical Biol Med 21 125-131 [Retrieval in progress]. [Pg.472]

Honda, Y. and Honda, S. The daf-2 gene network for longevity regulates oxidative stress resistance and Mn-superoxide dismutase gene expression in Caenorhabditis elegans. FASEB Journal 13 1385-1393 1999. [Pg.354]

Antras-Ferry J, Maheo K, Chevanne M, Dubos MP, Morel F, GuUlouzo A, CiUard P, CUlard J. Oltipraz stimulates the transcription of the manganese superoxide dismutase gene in rat hepatocytes. Carcinogenesis 1997 18 2113-2117. [Pg.291]

G115 extract protects rat heart from ischemia>reperfuslon injury G115 extract protects rabbits pulmonary artery from free radical injury G115 extract inhibits dose-dependently lipid peroxidation in rats Activation of the superoxide dismutase gene by Rb2 Scavenging effect of hydroxyl radicals, protection of fatty acids Anti free radical action of Ginsenostdes Rbl, Rb2, Rb3, Rc, Rd In rats Antioxidant action in rats (SOD, catalase, glutathionperoxidase) Activation of superoxide dismutase... [Pg.218]

Mo Y, Barnett ME, Takemoto D et al (2007) Human serum albumin nanoparticles fw efficient delivery of Cu, Zn superoxide dismutase gene. Mol Vis 13 746-757... [Pg.82]

BEAS 2 B cells, a human bronchial epitheUal cell line, exposed to various concentrations of crocidolite showed an increase of DNA strand breaks as follows (% positive cells) after 2h exposure (2% at 10" g/cm and 3 % at 5 x 10" g/cm ), after 24 h exposure (16% at 10" g/cm and 20% at 5xl0" g/ cm ) (Gillissen et al. 1996). In contrast, even at highest concentrations (24 h exposure) man-made mineral fibre basalt wool did not cause any increase of DNA strand breaks. Scanning electron microscopy confirmed that both fibre types were in part incorporated into the cells. Manganese superoxide dismutase gene expression was induced by 2ji UICC crocidolite/cm (Jaworska et al. 1997). [Pg.192]


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See also in sourсe #XX -- [ Pg.385 , Pg.476 , Pg.485 , Pg.486 , Pg.518 ]




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