Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.
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Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisCopper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 MutationsCharacterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,The legs at odd angles (Loa) mutation in cytoplasmic dynein ameliorates mitochondrial function in SOD1G93A mouse model for motor neuron disease.Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.Redox susceptibility of SOD1 mutants is associated with the differential response to CCS over-expression in vivo.A role for copper in the toxicity of zinc-deficient superoxide dismutase to motor neurons in amyotrophic lateral sclerosisImmature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.Heat shock factor 1 over-expression protects against exposure of hydrophobic residues on mutant SOD1 and early mortality in a mouse model of amyotrophic lateral sclerosis.Superoxide dismutases and superoxide reductases.A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivoRole of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALSA common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosisMolecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.Study of mutation and misfolding of Cu-Zn SOD1 protein.
P2860
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P2860
Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.
description
2006 nî lūn-bûn
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2006年の論文
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name
Disease-associated mutations a ...... nd compromise dimer stability.
@en
Disease-associated mutations a ...... nd compromise dimer stability.
@nl
type
label
Disease-associated mutations a ...... nd compromise dimer stability.
@en
Disease-associated mutations a ...... nd compromise dimer stability.
@nl
prefLabel
Disease-associated mutations a ...... nd compromise dimer stability.
@en
Disease-associated mutations a ...... nd compromise dimer stability.
@nl
P2093
P2860
P356
P1476
Disease-associated mutations a ...... nd compromise dimer stability.
@en
P2093
Amy Caruano-Yzermans
Angela Rodriguez
David R Borchelt
Hilda H Slunt
Jonathan Gitlin
Jonathan P Scheurmann
P John Hart
Xiaohang Cao
P2860
P304
P356
10.1074/JBC.M604503200
P407
P577
2006-11-08T00:00:00Z