Study of mutation and misfolding of Cu-Zn SOD1 protein.

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Dynamic properties of SOD1 mutants can predict survival time of patients carrying familial amyotrophic lateral sclerosis.Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.

P2860

Q40885460-A57D2870-CAE0-4668-A7AE-93D60BD22109 Q47382895-1ED13AFB-F950-4512-BF7F-681487AE6D29

P2860

Study of mutation and misfolding of Cu-Zn SOD1 protein.

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http://www.wikidata.org/entity/Q51134892

description

2013 nî lūn-bûn

@nan

2013年の論文

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2013年学术文章

@wuu

2013年学术文章

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2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

2013年學術文章

@zh-hant

name

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@en

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@nl

type

Item

label

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@en

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@nl

prefLabel

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@en

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@nl

P1476

Study of mutation and misfolding of Cu-Zn SOD1 protein.

@en

P2093

P Kolandaivel

http://www.w3.org/2001/XMLSchema#string

S P Keerthana

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P2860

Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal

Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutase

Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A

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

Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1

Protein misfolding, functional amyloid, and human disease

Structure and dynamics of amyloid-β segmental polymorphisms

ALS-causing SOD1 mutations promote production of copper-deficient misfolded species.

Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.

Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.

P304

167-183

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P31

scholarly article

P356

10.1080/07391102.2013.865104

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P433

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P478

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P577

2013-12-10T00:00:00Z

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P698

24320678

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Study of mutation and misfolding of Cu-Zn SOD1 protein.

about

P2860

P2860

Study of mutation and misfolding of Cu-Zn SOD1 protein.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698