Reactions of Hydrogen Peroxide with Familial Amyotrophic Lateral Sclerosis Mutant Human Copper-Zinc Superoxide Dismutases Studied by Pulse Radiolysis*
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J S Valentine | J. Valentine | J. J. Goto | E. B. Gralla | E B Gralla | J J Goto | D E Cabelli | D. Cabelli
[1] J. Holcman,et al. The interaction between Cu(I) superoxide dismutase and hydrogen peroxide. , 1989, The Journal of biological chemistry.
[2] D. Richardson,et al. Metal sites of copper-zinc superoxide dismutase. , 1977, Biochemistry.
[3] D. Price,et al. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[4] D. Bredesen,et al. Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis , 1996, Science.
[5] E. Stadtman,et al. Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[6] E. Stadtman,et al. A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[7] P. B. Roberts,et al. Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis. , 1974, The Biochemical journal.
[8] L. Ellerby,et al. Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[9] F. Poccia,et al. Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH‐SY5Y cells , 1997, FEBS letters.
[10] I. Fridovich,et al. Superoxide-dependent peroxidase activity of H48Q: a superoxide dismutase variant associated with familial amyotrophic lateral sclerosis. , 1997, Archives of biochemistry and biophysics.
[11] D. Borchelt,et al. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[12] C. Bull,et al. Steady-state kinetic studies of superoxide dismutases. Saturative behavior of the copper- and zinc-containing protein. , 1986, The Journal of biological chemistry.
[13] P. B. Roberts,et al. Mechanism and Inactivation of Superoxide Dismutase Activity , 1973 .
[14] I. Fridovich,et al. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. , 1975, Biochemistry.
[15] I. Fridovich,et al. The familial amyotrophic lateral sclerosis-associated amino acid substitutions E100G, G93A, and G93R do not influence the rate of inactivation of copper- and zinc-containing superoxide dismutase by H2O2. , 1998, Archives of biochemistry and biophysics.
[16] R. Mason,et al. Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H2O2. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[17] G. Rotilio,et al. A pulse radiolysis study of superoxide dismutase. , 1972, Biochimica et biophysica acta.
[18] M. Gurney,et al. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. , 1994, Science.
[19] E. Stadtman,et al. A Familial Amyotrophic Lateral Sclerosis-associated A4V Cu,Zn-Superoxide Dismutase Mutant Has a Lower Km for Hydrogen Peroxide , 1997, The Journal of Biological Chemistry.
[20] Robert H. Brown,et al. Increased 3‐nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis , 1997, Annals of neurology.
[21] Matteo Pellegrini,et al. Subunit asymmetry in the three‐dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis , 1998, Protein science : a publication of the Protein Society.
[22] M. Gurney,et al. The Copper Chelator d‐Penicillamine Delays Onset of Disease and Extends Survival in a Transgenic Mouse Model of Familial Amyotrophic Lateral Sclerosis , 1997, The European journal of neuroscience.
[23] E. Stadtman,et al. Enzyme function of copper, zinc superoxide dismutase as a free radical generator. , 1993, The Journal of biological chemistry.
[24] M. Carson,et al. ALS, SOD and peroxynitrite , 1993, Nature.
[25] R. Bray,et al. Trapping of Short-Lived Intermediates in Enzymic Reactions by Rapid Freezing: Combination of Electron Paramagnetic Resonance with Pulse Radiolysis , 1973 .
[26] I. Fridovich,et al. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. , 1975, Biochemistry.
[27] R. Casareno,et al. The Copper Chaperone for Superoxide Dismutase* , 1997, The Journal of Biological Chemistry.
[28] M. Gurney,et al. A low expressor line of transgenic mice carrying a mutant human Cu,Zn superoxide dismutase (SOD1) gene develops pathological changes that most closely resemble those in human amyotrophic lateral sclerosis , 1997, Acta Neuropathologica.
[29] J. Fee,et al. Studies on the reconstitution of bovine erythrocyte superoxide dismutase. V. Preparation and properties of derivatives in which both zinc and copper sites contain copper. , 1975, Biochimica et biophysica acta.
[30] J. Valentine,et al. Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[31] I. Fridovich,et al. A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. , 1972, The Journal of biological chemistry.
[32] V. Culotta,et al. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[33] M. Beal,et al. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury , 1996, Nature Genetics.
[34] C. M. Mcewen. [230] Monoamine oxidase [rabbit serum] , 1971 .
[35] I. Fridovich,et al. Pulse radiolytic investigations of superoxide catalyzed disproportionation. Mechanism for bovine superoxide dismutase. , 1973, Journal of the American Chemical Society.
[36] R. Nalbandyan,et al. Interaction of hydrogen peroxide with superoxide dismutase from erythrocytes , 1972, FEBS letters.
[37] J. Haines,et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis , 1993, Nature.