Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. - Wikidata - awgldk - TriplyDB

Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.

Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.

http://www.wikidata.org/entity/Q36512177

about

Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis Sumoylation of critical proteins in amyotrophic lateral sclerosis: emerging pathways of pathogenesis The complex molecular biology of amyotrophic lateral sclerosis (ALS)Solid-state NMR studies of metal-free SOD1 fibrillar structures.Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature Regulation of CuZnSOD and its redox signaling potential: implications for amyotrophic lateral sclerosis Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis.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.Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.Modulation of mutant superoxide dismutase 1 aggregation by co-expression of wild-type enzyme.DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.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.Autophagy defends pancreatic β cells from human islet amyloid polypeptide-induced toxicity Aggregation modulating elements in mutant human superoxide dismutase 1.Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.Impairment of mitochondria in adult mouse brain overexpressing predominantly full-length, N-terminally acetylated human α-synuclein Characterization of Protein Structural Changes in Living Cells Using Time-Lapsed FTIR Imaging Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.FTIR spectroscopic imaging of protein aggregation in living cells.Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis Intraneuronal β-amyloid and its interactions with proteins and subcellular organelles.RNA metabolism in ALS: when normal processes become pathological.A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability.Cellular Chaperones As Therapeutic Targets in ALS to Restore Protein Homeostasis and Improve Cellular Function Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells.Detection of a novel frameshift mutation and regions with homozygosis within ARHGEF28 gene in familial amyotrophic lateral sclerosis.Six SQSTM1 mutations in a Chinese amyotrophic lateral sclerosis cohort.Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice.Poloxamer 188 decreases membrane toxicity of mutant SOD1 and ameliorates pathology observed in SOD1 mouse model for ALS.Parkin is a disease modifier in the mutant SOD1 mouse model of ALS Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification Isotopic Evidence for Disrupted Copper Metabolism in Amyotrophic Lateral Sclerosis

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P2860

Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.

http://www.wikidata.org/entity/Q36512177

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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name

Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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P2860

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P1433

Journal of Biological Chemistry

P1476

Detergent-insoluble aggregates ...... dified superoxide dismutase-1.

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P2093

Aram M Nersissian

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Armando Durazo

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Bryan F Shaw

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David R Borchelt

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Edith B Gralla

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Guillan Xu

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

Herman L Lelie

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Joan S Valentine

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

Lawrence J Hayward

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Pik K Chan

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P2860

Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1

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

ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization

Protein misfolding, functional amyloid, and human disease

Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria

A specific amyloid-beta protein assembly in the brain impairs memory

A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids

Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.

P304

8340-8350

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scholarly article

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10.1074/JBC.M707751200

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P407

P433

13

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P478

283

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Ashutosh Tiwari

Julian P Whitelegge

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2008-01-11T00:00:00Z

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18192269

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P921

amyotrophic lateral sclerosis

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2276386

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