Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. - Wikidata - awgldk - TriplyDB

Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.

Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.

http://www.wikidata.org/entity/Q35162930

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SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis The genetic epidemiology of neurodegenerative disease.Deficiency of disulfide bonds facilitating fibrillogenesis of endostatin Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosis Alsin, the product of ALS2 gene, suppresses SOD1 mutant neurotoxicity through RhoGEF domain by interacting with SOD1 mutants The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Ultrafast colorimetric determination of predominant protein structure evolution with gold nanoplasmonic particles.Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening.Differential effects of phytotherapic preparations in the hSOD1 Drosophila melanogaster model of ALS.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.The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.A role for copper in the toxicity of zinc-deficient superoxide dismutase to motor neurons in amyotrophic lateral sclerosis Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Direct observation of defects and increased ion permeability of a membrane induced by structurally disordered Cu/Zn-superoxide dismutase aggregates.The contrasting effect of macromolecular crowding on amyloid fibril formation.Copper-based pulsed dipolar ESR spectroscopy as a probe of protein conformation linked to disease states.Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model Cupric ions induce the oxidation and trigger the aggregation of human superoxide dismutase 1 Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease The effect of SOD1 mutation on cellular bioenergetic profile and viability in response to oxidative stress and influence of mutation-type.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Sensitive and molecular size-selective detection of proteins using a chip-based and heteroliganded gold nanoisland by localized surface plasmon resonance spectroscopy Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant.

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Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.

http://www.wikidata.org/entity/Q35162930

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2003 nî lūn-bûn

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Cu/Zn superoxide dismutase mut ...... mation of aggregates in vitro.

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Cu/Zn superoxide dismutase mut ...... mation of aggregates in vitro.

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

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Cu/Zn superoxide dismutase mut ...... mation of aggregates in vitro.

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E M Meiering

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G A Scholz

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H E Frey

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J R Lepock

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R A Hallewell

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R A Irani

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P2860

Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

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

From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS

Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Amyotrophic lateral sclerosis

Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1 beta point mutant modified in a surface loop.

Evolutionary aspects of superoxide dismutase: the copper/zinc enzyme.

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amyotrophic lateral sclerosis

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