Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.
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Deficiency of disulfide bonds facilitating fibrillogenesis of endostatinIntracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosisRedox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linkingALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomesMechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosisCharacterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutaseProtein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosisA faulty interaction between SOD1 and hCCS in neurodegenerative diseaseZinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Disulfide bond as a switch for copper-zinc superoxide dismutase activity in asthma.Lipid-associated aggregate formation of superoxide dismutase-1 is initiated by membrane-targeting loops.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.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric speciesAggregation of copper-zinc superoxide dismutase in familial and sporadic ALSSystematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutantsDestabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS.The crucial role of caspase-9 in the disease progression of a transgenic ALS mouse model.Exposure 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.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1Cytotoxicity of superoxide dismutase 1 in cultured cells is linked to Zn2+ chelation.Aggregation modulating elements in mutant human superoxide dismutase 1.Zinc: indications in brain disorders.Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondriaDecreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.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.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.SOD1 oxidation and formation of soluble aggregates in yeast: relevance to sporadic ALS development.Metal-deficient SOD1 in amyotrophic lateral sclerosis.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1
P2860
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P2860
Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@ast
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@en
type
label
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@ast
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@en
prefLabel
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@ast
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@en
P2860
P356
P1476
Familial amyotrophic lateral s ...... ptible to disulfide reduction.
@en
P2093
Lawrence J Hayward
P2860
P304
P356
10.1074/JBC.M210419200
P407
P577
2002-11-27T00:00:00Z