The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
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Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivoStructures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisMolecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutaseStructural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALSRole of Conserved Tyrosine Residues in NiSOD Catalysis: A Case of Convergent Evolution †Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsStructural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93APurification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoanLeishmania tarentolaeStructures of mouse SOD1 and human/mouse SOD1 chimerasThe Role of Zn 2+ on the Structure and Stability of Murine Adenosine Deaminase †Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMRInsights into the role of the unusual disulfide bond in copper-zinc superoxide dismutaseCutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperatureZinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.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.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsAggregation of copper-zinc superoxide dismutase in familial and sporadic ALSSystematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutantsAggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesCommon dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changesCu,Zn-superoxide dismutase without Zn is folded but catalytically inactive.Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid diseaseThe E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.Superoxide dismutases and superoxide reductases.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation.Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomerDynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation.Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V.
P2860
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P2860
The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The structure of holo and meta ...... amyotrophic lateral sclerosis
@ast
The structure of holo and meta ...... amyotrophic lateral sclerosis
@en
The structure of holo and meta ...... amyotrophic lateral sclerosis
@nl
type
label
The structure of holo and meta ...... amyotrophic lateral sclerosis
@ast
The structure of holo and meta ...... amyotrophic lateral sclerosis
@en
The structure of holo and meta ...... amyotrophic lateral sclerosis
@nl
prefLabel
The structure of holo and meta ...... amyotrophic lateral sclerosis
@ast
The structure of holo and meta ...... amyotrophic lateral sclerosis
@en
The structure of holo and meta ...... amyotrophic lateral sclerosis
@nl
P2093
P1476
The structure of holo and meta ...... amyotrophic lateral sclerosis
@en
P2093
Joan S Valentine
Jorge A Rodriguez
Lawrence J Hayward
P John Hart
Peter A Doucette
Richard W Strange
S Samar Hasnain
P304
P356
10.1016/S0022-2836(03)00355-3
P407
P577
2003-05-01T00:00:00Z