Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. - Wikidata - awgldk - TriplyDB

Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.

Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.

http://www.wikidata.org/entity/Q33897544

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Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations SOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesis Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis Structural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALS Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase The complex molecular biology of amyotrophic lateral sclerosis (ALS)Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS Metal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1 Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.The structural biochemistry of the superoxide dismutases.Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.Superoxide dismutases and superoxide reductases.Neutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Arresting amyloid with coulomb's law: acetylation of ALS-linked SOD1 by aspirin impedes aggregation Analysis of mutant SOD1 electrophoretic mobility by Blue Native gel electrophoresis; evidence for soluble multimeric assemblies Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1 Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.

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P2860

Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.

http://www.wikidata.org/entity/Q33897544

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2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Destabilization of apoprotein ...... utase-linked ALS pathogenesis.

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Destabilization of apoprotein ...... utase-linked ALS pathogenesis.

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type

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Destabilization of apoprotein ...... utase-linked ALS pathogenesis.

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Destabilization of apoprotein ...... utase-linked ALS pathogenesis.

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Destabilization of apoprotein ...... utase-linked ALS pathogenesis.

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Destabilization of apoprotein ...... utase-linked ALS pathogenesis.

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PNAS.0502515102

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

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Destabilization of apoprotein ...... mutase-linked ALS pathogenesis

@en

P2093

Aram M Nersissian

http://www.w3.org/2001/XMLSchema#string

Armando Durazo

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Bryan Francis Shaw

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Joan Selverstone Valentine

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Jorge A Rodriguez

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Kym F Faull

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Lawrence J Hayward

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Peter A Doucette

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Se Hui Sohn

http://www.w3.org/2001/XMLSchema#string

P2860

In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly

Misfolded CuZnSOD and amyotrophic lateral sclerosis

Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type

An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)

Primary structure effects on peptide group hydrogen exchange

Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.

Mechanisms and uses of hydrogen exchange.

Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry.

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10516-10521

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10.1073/PNAS.0502515102

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30

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102

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Ashutosh Tiwari

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2005-07-14T00:00:00Z

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7723283

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16020530

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amyotrophic lateral sclerosis

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1175580

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