Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS
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SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationSuperoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosisDJ-1 is a copper chaperone acting on SOD1 activationStructural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsFunctional features cause misfolding of the ALS-provoking enzyme SOD1Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assemblyLigand binding and aggregation of pathogenic SOD1Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferasesThe complex molecular biology of amyotrophic lateral sclerosis (ALS)Modification of superoxide dismutase 1 (SOD1) properties by a GFP tag--implications for research into amyotrophic lateral sclerosis (ALS)A faulty interaction between SOD1 and hCCS in neurodegenerative diseaseSolid-state NMR studies of metal-free SOD1 fibrillar structures.Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols.Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts.Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutantsWild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensityLoss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric speciesAtomic-resolution monitoring of protein maturation in live human cells by NMRConformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases.Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALSImmature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.A high-throughput screen to identify inhibitors of SOD1 transcription.In-cell NMR in E. coli to monitor maturation steps of hSOD1.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Direct observation of defects and increased ion permeability of a membrane induced by structurally disordered Cu/Zn-superoxide dismutase aggregates.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1Cytotoxicity of superoxide dismutase 1 in cultured cells is linked to Zn2+ chelation.Huntingtin fragments and SOD1 mutants form soluble oligomers in the cellNonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisAggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesRole of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation
P2860
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P2860
Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@ast
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@en
type
label
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@ast
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@en
prefLabel
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@ast
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@en
P2093
P2860
P50
P921
P356
P1476
Metal-free superoxide dismutas ...... ral mechanism for familial ALS
@en
P2093
Armando Durazo
Edith Butler Gralla
Joan Selverstone Valentine
Manuele Martinelli
Miguela Vieru
Stefania Girotto
P2860
P304
11263-11267
P356
10.1073/PNAS.0704307104
P407
P577
2007-06-25T00:00:00Z