Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis. - Test2 - elhamkhani - TriplyDB

Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis.

Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis.

http://www.wikidata.org/entity/Q37326811

about

Artifacts to avoid while taking advantage of top-down mass spectrometry based detection of protein S-thiolation.Acetylation at lysine 71 inactivates superoxide dismutase 1 and sensitizes cancer cells to genotoxic agents.Non-native soluble oligomers of Cu/Zn superoxide dismutase (SOD1) contain a conformational epitope linked to cytotoxicity in amyotrophic lateral sclerosis (ALS).A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.Cysteine Modifications in the Pathogenesis of ALS.Cysteines as Redox Molecular Switches and Targets of Disease.Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity.Addition of exogenous SOD1 aggregates causes TDP-43 mislocalisation and aggregation.The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation.Minimotifs dysfunction is pervasive in neurodegenerative disorders Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cells

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Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis.

http://www.wikidata.org/entity/Q37326811

description

2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年學術文章

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2013年學術文章

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2013年學術文章

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name

Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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type

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Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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Scientific Reports

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Glutathionylation potentiates ...... amyotrophic lateral sclerosis.

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J Andrew Aquilina

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

P2860

Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase

Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis

Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS.

Aggregation of ALS mutant superoxide dismutase expressed in Escherichia coli.

Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.

Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.

Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species

Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients

The structural biochemistry of the superoxide dismutases.

Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.

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10.1038/SREP03275

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Justin J Yerbury

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amyotrophic lateral sclerosis

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