Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
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Four decades of neurodegenerative disease research: how far we have come!SOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesisResveratrol: A Focus on Several Neurodegenerative DiseasesProtein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applicationsMechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosisRedox regulation in amyotrophic lateral sclerosisStructural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93AThe complex molecular biology of amyotrophic lateral sclerosis (ALS)A faulty interaction between SOD1 and hCCS in neurodegenerative diseaseSuppressing mutation-induced protein aggregation in mammalian cells by mutating residues significantly displaced upon the original mutationCis-suppression to arrest protein aggregation in mammalian cells.Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts.Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutantsOxidative stress and mitochondrial dysfunction across broad-ranging pathologies: toward mitochondria-targeted clinical strategies.DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Identification of compounds protective against G93A-SOD1 toxicity for the treatment of amyotrophic lateral sclerosis.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.Using theoretical protein isotopic distributions to parse small-mass-difference post-translational modifications via mass spectrometryExposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability.Bim links ER stress and apoptosis in cells expressing mutant SOD1 associated with amyotrophic lateral sclerosis.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1Oligomerization of Cysteine String Protein alpha mutants causing adult neuronal ceroid lipofuscinosis.Huntingtin fragments and SOD1 mutants form soluble oligomers in the cellAn examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1Aggregation modulating elements in mutant human superoxide dismutase 1.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisRole of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.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 effect of SOD1 mutation on cellular bioenergetic profile and viability in response to oxidative stress and influence of mutation-type.TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin/IGF-1 signalingGlial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis.Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregationMeasuring copper and zinc superoxide dismutase from spinal cord tissue using electrospray mass spectrometry.Proteins that bind to misfolded mutant superoxide dismutase-1 in spinal cords from transgenic amyotrophic lateral sclerosis (ALS) model mice.Biochemical properties and in vivo effects of the SOD1 zinc-binding site mutant (H80G)Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice.Analysis of mutant SOD1 electrophoretic mobility by Blue Native gel electrophoresis; evidence for soluble multimeric assemblies
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Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 30 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Role of mutant SOD1 disulfide ...... e pathogenesis of familial ALS
@en
Role of mutant SOD1 disulfide ...... pathogenesis of familial ALS.
@nl
type
label
Role of mutant SOD1 disulfide ...... e pathogenesis of familial ALS
@en
Role of mutant SOD1 disulfide ...... pathogenesis of familial ALS.
@nl
prefLabel
Role of mutant SOD1 disulfide ...... e pathogenesis of familial ALS
@en
Role of mutant SOD1 disulfide ...... pathogenesis of familial ALS.
@nl
P2093
P2860
P356
P1476
Role of mutant SOD1 disulfide ...... e pathogenesis of familial ALS
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P2093
David R Borchelt
Duane D Winkler
P John Hart
P2860
P304
P356
10.1073/PNAS.0902505106
P407
P577
2009-04-30T00:00:00Z