The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)
about
SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationFrom structure to redox: The diverse functional roles of disulfides and implications in disease.DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALSDestabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Aggregation modulating elements in mutant human superoxide dismutase 1.Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.The structural biochemistry of the superoxide dismutases.Superoxide dismutases and superoxide reductases.The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivoRole of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALSDirect magnetic resonance evidence for peroxymonocarbonate involvement in the cu,zn-superoxide dismutase peroxidase catalytic cycle.SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease.Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra- and intermolecular disulfide bonding in aggregation.Superoxide dismutases: ancient enzymes and new insights.An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis.A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.
P2860
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P2860
The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)
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2003 nî lūn-bûn
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2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
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2003年の論文
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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 perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@ast
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@en
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@nl
type
label
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@ast
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@en
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@nl
prefLabel
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@ast
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@en
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@nl
P1476
The perplexing role of copper- ...... lerosis (Lou Gehrig's disease)
@en
P2093
Joan Selverstone Valentine
Soshanna Zittin Potter
P2888
P304
P356
10.1007/S00775-003-0447-6
P407
P577
2003-04-01T00:00:00Z