Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.
about
DJ-1 is a copper chaperone acting on SOD1 activationStatistical analysis of interface similarity in crystals of homologous proteinsReducing systems protecting the bacterial cell envelope from oxidative damageMolecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu Zn superoxide dismutaseStructural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93ADisrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80RStructures of mouse SOD1 and human/mouse SOD1 chimerasPost-translational modification of Cu/Zn superoxide dismutase under anaerobic conditions.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.S-glutathionylation: from molecular mechanisms to health outcomesThe endosymbiont Wolbachia pipientis induces the expression of host antioxidant proteins in an Aedes albopictus cell line.Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.The impact of growth hormone on proteomic profiles: a review of mouse and adult human studies.A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase.Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS.The megavirus chilensis Cu,Zn-superoxide dismutase: the first viral structure of a typical cellular copper chaperone-independent hyperstable dimeric enzymeSuperoxide dismutases and superoxide reductases.Biochemical properties and in vivo effects of the SOD1 zinc-binding site mutant (H80G)Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1Activation of superoxide dismutases: putting the metal to the pedal.Purification and characterization of thermostable monomeric chloroplastic Cu/Zn superoxide dismutase from Chenopodium murale.Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomerSelenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase.Regulation of superoxide dismutase genes: implications in disease.The right to choose: multiple pathways for activating copper,zinc superoxide dismutase.Proteomic tools for the analysis of transient interactions between metalloproteins.Disulfide bonds in amyloidogenesis diseases related proteins.Species-specific activation of Cu/Zn SOD by its CCS copper chaperone in the pathogenic yeast Candida albicans.Knockdown of SOD1 sensitizes the CD34+ CML cells to imatinib therapy.Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosisPathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis.Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants.Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1.Trifluoroethanol-induced changes in activity and conformation of manganese-containing superoxide dismutase.Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.
P2860
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P2860
Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Posttranslational modification ...... amyotrophic lateral sclerosis.
@ast
Posttranslational modification ...... amyotrophic lateral sclerosis.
@en
type
label
Posttranslational modification ...... amyotrophic lateral sclerosis.
@ast
Posttranslational modification ...... amyotrophic lateral sclerosis.
@en
prefLabel
Posttranslational modification ...... amyotrophic lateral sclerosis.
@ast
Posttranslational modification ...... amyotrophic lateral sclerosis.
@en
P2860
P356
P1476
Posttranslational modification ...... amyotrophic lateral sclerosis
@en
P2093
Thomas V O'Halloran
P2860
P304
P356
10.1089/ARS.2006.8.847
P577
2006-05-01T00:00:00Z