Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants - Wikidata - awgldk - TriplyDB

Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants

Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants

http://www.wikidata.org/entity/Q33895940

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SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization SOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesis Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis Regulation of protein quality control by UBE4B and LSD1 through p53-mediated transcription An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans RNA-Seq profiling of spinal cord motor neurons from a presymptomatic SOD1 ALS mouse Functional features cause misfolding of the ALS-provoking enzyme SOD1 RNA-binding protein is involved in aggregation of light neurofilament protein and is implicated in the pathogenesis of motor neuron degeneration Parsing Disease-relevant Protein Modifications from Epiphenomena: Perspective on the Structural Basis of SOD1-Mediated ALS.Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Structural and functional analysis of human SOD1 in amyotrophic lateral sclerosis.Correlating protein function and stability through the analysis of single amino acid substitutions.SDM--a server for predicting effects of mutations on protein stability and malfunction.Correlating disease-related mutations to their effect on protein stability: a large-scale analysis of the human proteome.A structural systems biology approach for quantifying the systemic consequences of missense mutations in proteins.Amyotrophic lateral sclerosis: an emerging era of collaborative gene discovery Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm.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.Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species Transfer of pathogenic and nonpathogenic cytosolic proteins between spinal cord motor neurons in vivo in chimeric mice Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells 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 Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Cytotoxicity of superoxide dismutase 1 in cultured cells is linked to Zn2+ chelation.Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na+-Activated K+ Channels in Aplysia Neurons 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 Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease The structural biochemistry of the superoxide dismutases.Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.Motor neuron trophic factors: therapeutic use in ALS?Superoxide dismutases and superoxide reductases.

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P2860

Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants

http://www.wikidata.org/entity/Q33895940

description

2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005年の論文

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Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

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Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

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Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

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Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

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Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

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Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

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PNAS.0501957102

P1433

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

P1476

Systematically perturbed foldi ...... (ALS)-associated SOD1 mutants

@en

P2093

Mikael J Lindberg

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Mikael Oliveberg

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Niklas Boknäs

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Roberth Byström

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P2860

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

The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly

Unspecific hydrophobic stabilization of folding transition states

The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis

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

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

Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?

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

Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding

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scholarly article

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10.1073/PNAS.0501957102

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28

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102

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Peter M Andersen

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7755800

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15987780

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amyotrophic lateral sclerosis

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1174986

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