Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.
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Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosisRegulation of the copper chaperone CCS by XIAP-mediated ubiquitinationStructures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisMisfolded CuZnSOD and amyotrophic lateral sclerosisCopper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 MutationsSynthetic fluorescent probes for studying copper in biological systemsDestabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicityAn alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediateMolecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutaseSuperoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosisStructural Evidence for a Copper-Bound Carbonate Intermediate in the Peroxidase and Dismutase Activities of Superoxide DismutaseStructural Consequences of Cysteinylation of Cu/Zn-Superoxide DismutaseInhibition of fast axonal transport by pathogenic SOD1 involves activation of p38 MAP kinaseSolid-state NMR studies of metal-free SOD1 fibrillar structures.Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperatureZinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.S-nitrosothiol depletion in amyotrophic lateral sclerosis.Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS.Discovery of molecular mechanisms of neuroprotection using cell-based bioassays and oligonucleotide arrays.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.Loss 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 methodsMutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric speciesModulation of mutant superoxide dismutase 1 aggregation by co-expression of wild-type enzyme.Application of external-cavity quantum cascade infrared lasers to nanosecond time-resolved infrared spectroscopy of condensed-phase samples following pulse radiolysis.A role for copper in the toxicity of zinc-deficient superoxide dismutase to motor neurons in amyotrophic lateral sclerosisMetal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.X-ray fluorescence imaging reveals subcellular biometal disturbances in a childhood neurodegenerative disorder.Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.The potential for transition metal-mediated neurodegeneration in amyotrophic lateral sclerosisInsights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Using theoretical protein isotopic distributions to parse small-mass-difference post-translational modifications via mass spectrometryThe crucial role of caspase-9 in the disease progression of a transgenic ALS mouse model.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.
P2860
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P2860
Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Decreased metallation and acti ...... amyotrophic lateral sclerosis.
@en
type
label
Decreased metallation and acti ...... amyotrophic lateral sclerosis.
@en
prefLabel
Decreased metallation and acti ...... amyotrophic lateral sclerosis.
@en
P2093
P2860
P356
P1476
Decreased metallation and acti ...... amyotrophic lateral sclerosis
@en
P2093
Diane E Cabelli
Joan Selverstone Valentine
Jorge A Rodriguez
Joy J Goto
Lawrence J Hayward
P2860
P304
15923-15931
P356
10.1074/JBC.M112087200
P407
P577
2002-02-19T00:00:00Z