Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein - Wikidata - awgldk - TriplyDB

Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein

Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein

http://www.wikidata.org/entity/Q30425734

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The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase Misfolded CuZnSOD and amyotrophic lateral sclerosis Engineering humoral immunity as prophylaxis or therapy Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site A faulty interaction between SOD1 and hCCS in neurodegenerative disease Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Accelerated s-nitrosothiol breakdown by amyotrophic lateral sclerosis mutant copper,zinc-superoxide dismutase.Regulation of CuZnSOD and its redox signaling potential: implications for amyotrophic lateral sclerosis Activated alpha 2-macroglobulin reverses the immunosuppressive activity in human breast cancer cell-conditioned medium by selectively neutralizing transforming growth factor-beta in the presence of interleukin-2.Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Expression of zinc-deficient human superoxide dismutase in Drosophila neurons produces a locomotor defect linked to mitochondrial dysfunction.Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability.Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state.Familial amyotrophic lateral sclerosis.Cu,Zn-superoxide dismutase without Zn is folded but catalytically inactive.Motor neuron trophic factors: therapeutic use in ALS?Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.A fruitful endeavor: modeling ALS in the fruit fly Metal-deficient SOD1 in amyotrophic lateral sclerosis.Serum choline activates mutant acetylcholine receptors that cause slow channel congenital myasthenic syndromes Current pharmacological management of amyotrophic [corrected] lateral sclerosis and a role for rational polypharmacy.Misfolded proteins, endoplasmic reticulum stress and neurodegeneration.Role of conserved glycine in zinc-dependent medium chain dehydrogenase/reductase superfamily The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1 Catalytic antioxidants to treat amyotropic lateral sclerosis.Role of zinc in ALS.Activation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS.Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis Gain in functions of mutant Cu,Zn-superoxide dismutases as a causative factor in familial amyotrophic lateral sclerosis: less reactive oxidant formation but high spontaneous aggregation and precipitation.Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis.Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg.Antioxidative and proapoptotic effects of riluzole on cultured cortical neurons.Bicarbonate enhances peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics.Thiol oxidase activity of copper, zinc superoxide dismutase.Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase.The structural analysis of the pro-oxidant copper-binding site of denatured apo-H43R SOD1 and the elucidation of the origin of the acquisition of the pro-oxidant activity.

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P2860

Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein

http://www.wikidata.org/entity/Q30425734

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1996 nî lūn-bûn

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1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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1996 թվականի հոտեմբերին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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Proceedings of the National Academy of Sciences of the United States of America

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Mutations in copper-zinc super ...... redox behavior of the protein

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A Nersissian

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P2860

Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase

Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

Rapid and efficient site-specific mutagenesis without phenotypic selection

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury

Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation

Crystal structure solution and refinement of the semisynthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0 A resolution.

Crystal structure of yeast Cu,Zn superoxide dismutase. Crystallographic refinement at 2.5 A resolution.

Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells.

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