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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

http://www.wikidata.org/entity/Q27662078

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Structures of mouse SOD1 and human/mouse SOD1 chimeras Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense Metal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis Superoxide dismutases and superoxide reductases.Biochemical properties and in vivo effects of the SOD1 zinc-binding site mutant (H80G)Analysis of mutant SOD1 electrophoretic mobility by Blue Native gel electrophoresis; evidence for soluble multimeric assemblies Mutant SOD1 forms ion channel: implications for ALS pathophysiology.The Phylogeny and Active Site Design of Eukaryotic Copper-only Superoxide Dismutases.The role of solvent exclusion in the interaction between D124 and the metal site in SOD1: implications for ALS.A solution 17O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase.Synergistic oxygen atom transfer by ruthenium complexes with non-redox metal ions.Redox-inactive metal ions promoted the catalytic reactivity of non-heme manganese complexes towards oxygen atom transfer.Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.Eukaryotic Cu-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains.Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.Study of mutation and misfolding of Cu-Zn SOD1 protein.Destabilization of the metal site as a hub for the pathogenic mechanism of five ALS-linked mutants of copper, zinc superoxide dismutase.Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1).

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

http://www.wikidata.org/entity/Q27662078

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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Alexander B Taylor

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Duane D Winkler

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Joan S Valentine

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Lisa J Whitson

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Mark C Carroll

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P John Hart

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Peter A Doucette

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Sai V Seetharaman

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Valeria C Culotta

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Virgil Schirf

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P2860

The copper chaperone for superoxide dismutase

Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis

Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

Structural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALS

Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †

Functional features cause misfolding of the ALS-provoking enzyme SOD1

Characterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,

Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase

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10.1021/BI100314N

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27

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44642093

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