The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
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Human CCS gene: genomic organization and exclusion as a candidate for amyotrophic lateral sclerosis (ALS).XIAP: cell death regulation meets copper homeostasisThe Silver syndrome variant of hereditary spastic paraplegia maps to chromosome 11q12-q14, with evidence for genetic heterogeneity within this subtypeInteraction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasisHuman copper transporter 2 is localized in late endosomes and lysosomes and facilitates cellular copper uptakeMolecular mediators governing iron-copper interactionsPurification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assemblyRole of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasisCopper ion-sensing transcription factor Mac1p post-translationally controls the degradation of its target gene product Ctr1p.Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase.Transcriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutaseThe neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activityThe copper toxicosis gene product Murr1 directly interacts with the Wilson disease proteinCharacterization of mouse embryonic cells deficient in the ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport systemCopper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutaseDevelopmental changes in murine brain antioxidant enzymesCu,Zn superoxide dismutase in Rhodotorula and Udeniomyces spp. isolated from sea water: cloning and sequencing the encoding region.Cloning and sequencing the genomic encoding region of copper-zinc superoxide dismutase enzyme from several marine strains of the genus Debaryomyces (Lodder & Kreger-van Rij).Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Abeta production in APP23 transgenic miceMetallochaperones, an intracellular shuttle service for metal ions.Colocalization of 14-3-3 proteins with SOD1 in Lewy body-like hyaline inclusions in familial amyotrophic lateral sclerosis cases and the animal modelEvaluation of higher plant virus resistance genes in the green alga, Chlorella variabilis NC64A, during the early phase of infection with Paramecium bursaria chlorella virus-1Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS.Copper modulates the degradation of copper chaperone for Cu,Zn superoxide dismutase by the 26 S proteosome.Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP.Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase.Familial amyotrophic lateral sclerosis.Mechanisms of liver injury relevant to pediatric hepatology.Hepatic transport systems.Transcuprein is a macroglobulin regulated by copper and iron availabilityProteins that bind to misfolded mutant superoxide dismutase-1 in spinal cords from transgenic amyotrophic lateral sclerosis (ALS) model mice.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Biochemical properties and in vivo effects of the SOD1 zinc-binding site mutant (H80G)The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase.Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development.Effects of Cu/Zn superoxide dismutase on estrogen responsiveness and oxidative stress in human breast cancer cellsMetabolic crossroads of iron and copper.Copper transport into the secretory pathway is regulated by oxygen in macrophages.Featured Article: Effect of copper on nuclear translocation of copper chaperone for superoxide dismutase-1.
P2860
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P248
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P2860
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@ast
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en-gb
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@nl
type
label
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@ast
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en-gb
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@nl
prefLabel
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@ast
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en-gb
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@nl
P2093
P2860
P921
P356
P1476
The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
@en
P2093
D Waggoner
J D Gitlin
R L Casareno
P2860
P304
P356
10.1074/JBC.273.37.23625
P407
P577
1998-09-11T00:00:00Z