Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.
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Dysregulation of glutathione homeostasis in neurodegenerative diseasesSumoylation of critical proteins in amyotrophic lateral sclerosis: emerging pathways of pathogenesisRedox regulation in amyotrophic lateral sclerosisThe complex molecular biology of amyotrophic lateral sclerosis (ALS)Biological Chemistry and Functionality of Protein Sulfenic Acids and Related Thiol ModificationsParsing Disease-relevant Protein Modifications from Epiphenomena: Perspective on the Structural Basis of SOD1-Mediated ALS.Disulfide bond as a switch for copper-zinc superoxide dismutase activity in asthma.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesGenotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis.Artifacts to avoid while taking advantage of top-down mass spectrometry based detection of protein S-thiolation.Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis.Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damageSOD1 Lysine 123 Acetylation in the Adult Central Nervous System.Computational approaches to understanding protein aggregation in neurodegeneration.Non-native soluble oligomers of Cu/Zn superoxide dismutase (SOD1) contain a conformational epitope linked to cytotoxicity in amyotrophic lateral sclerosis (ALS).Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis.A cysteine residue affects the conformational state and neuronal toxicity of mutant SOD1 in mice: relevance to the pathogenesis of ALS.Cysteine Modifications in the Pathogenesis of ALS.Cysteines as Redox Molecular Switches and Targets of Disease.Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzymeRedox regulation of cysteine-dependent enzymes in neurodegeneration.The involvement of GSH in the activation of human Sod1 linked to FALS in chronologically aged yeast cells.A hidden aggregation-prone structure in the heart of hypoxia inducible factor prolyl hydroxylase.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human-A Discrete Molecular Dynamics Study.Large SOD1 aggregates, unlike trimeric SOD1, do not impact cell viability in a model of amyotrophic lateral sclerosis
P2860
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P2860
Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@ast
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@en
type
label
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@ast
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@en
prefLabel
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@ast
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@en
P2093
P2860
P356
P1433
P1476
Glutathionylation at Cys-111 i ...... e and FALS mutant SOD1 dimers.
@en
P2093
Kyle C Wilcox
Lanette Fee
Michael Caplow
Rachel L Redler
P2860
P304
P356
10.1021/BI200614Y
P407
P577
2011-07-18T00:00:00Z