Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.
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ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomesSOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesisMechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosisDestabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicityAn alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediateMolecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutaseStructural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsStructural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93ALigand binding and aggregation of pathogenic SOD1Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutaseThe rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosisSolid-state NMR studies of metal-free SOD1 fibrillar structures.Intermolecular transmission of superoxide dismutase 1 misfolding in living cells.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.Structural and functional analysis of human SOD1 in amyotrophic lateral sclerosis.Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy.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.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsMetal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Copper-based pulsed dipolar ESR spectroscopy as a probe of protein conformation linked to disease states.Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisAggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesCopper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.The megavirus chilensis Cu,Zn-superoxide dismutase: the first viral structure of a typical cellular copper chaperone-independent hyperstable dimeric enzymeFamilial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials.Superoxide dismutases and superoxide reductases.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.Arresting amyloid with coulomb's law: acetylation of ALS-linked SOD1 by aspirin impedes aggregationMetal-deficient SOD1 in amyotrophic lateral sclerosis.Protein aggregation in motor neurone disorders.Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant.
P2860
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P2860
Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@en
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@nl
type
label
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@en
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@nl
prefLabel
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@en
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@nl
P2093
P2860
P356
P1476
Familial amyotrophic lateral s ...... per/zinc superoxide dismutase.
@en
P2093
Daryl K Eggers
James A Roe
Joan S Valentine
Jorge A Rodriguez
Lawrence J Hayward
P2860
P304
15932-15937
P356
10.1074/JBC.M112088200
P407
P577
2002-02-19T00:00:00Z