How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
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Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosisDynamics, stability and iron-binding activity of frataxin clinical mutantsA Potential Alternative against Neurodegenerative Diseases: PhytodrugsTempol moderately extends survival in a hSOD1(G93A) ALS rat model by inhibiting neuronal cell loss, oxidative damage and levels of non-native hSOD1(G93A) formsFunctional features cause misfolding of the ALS-provoking enzyme SOD1Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assemblyTrimming Down a Protein Structure to Its Bare Foldons: SPATIAL ORGANIZATION OF THE COOPERATIVE UNITInsights into the role of the unusual disulfide bond in copper-zinc superoxide dismutaseThe complex molecular biology of amyotrophic lateral sclerosis (ALS)Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperatureStructural and functional analysis of human SOD1 in amyotrophic lateral sclerosis.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.The legs at odd angles (Loa) mutation in cytoplasmic dynein ameliorates mitochondrial function in SOD1G93A mouse model for motor neuron disease.Genome-wide association analysis reveals a SOD1 mutation in canine degenerative myelopathy that resembles amyotrophic lateral sclerosis.Proteasomes remain intact, but show early focal alteration in their composition in a mouse model of amyotrophic lateral sclerosis.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.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsDNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALSAxonal mitochondrial clusters containing mutant SOD1 in transgenic models of ALS.Metal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.Stem cell-derived motor neurons: applications and challenges in amyotrophic lateral sclerosis.Immunological detection of N-formylkynurenine in oxidized proteins.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Direct observation of defects and increased ion permeability of a membrane induced by structurally disordered Cu/Zn-superoxide dismutase aggregates.Cu, Zn-superoxide dismutase 1 (SOD1) is a novel target of Puromycin-sensitive aminopeptidase (PSA/NPEPPS): PSA/NPEPPS is a possible modifier of amyotrophic lateral sclerosis.Bim links ER stress and apoptosis in cells expressing mutant SOD1 associated with amyotrophic lateral sclerosis.Huntingtin fragments and SOD1 mutants form soluble oligomers in the cellIL-17A is increased in the serum and in spinal cord CD8 and mast cells of ALS patients.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisCopper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol.The structural biochemistry of the superoxide dismutases.Superoxide dismutases and superoxide reductases.The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder.Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis.
P2860
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P2860
How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
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
How do ALS-associated mutation ...... te aggregation of the protein?
@ast
How do ALS-associated mutation ...... te aggregation of the protein?
@en
type
label
How do ALS-associated mutation ...... te aggregation of the protein?
@ast
How do ALS-associated mutation ...... te aggregation of the protein?
@en
prefLabel
How do ALS-associated mutation ...... te aggregation of the protein?
@ast
How do ALS-associated mutation ...... te aggregation of the protein?
@en
P1476
How do ALS-associated mutation ...... te aggregation of the protein?
@en
P2093
Bryan F Shaw
Joan Selverstone Valentine
P356
10.1016/J.TIBS.2006.12.005
P577
2007-01-05T00:00:00Z