about
Unexpected vascular enrichment of SCO1 over SCO2 in mammalian tissues: implications for human mitochondrial diseaseSco proteins are involved in electron transfer processesA new structural paradigm in copper resistance in Streptococcus pneumoniaeStructural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividansThe CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding ProteinsCopper metallochaperonesThioredoxin-like protein TlpA from Bradyrhizobium japonicum is a reductant for the copper metallochaperone ScoIAnalysis of mouse models of cytochrome c oxidase deficiency owing to mutations in Sco2H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco.Disparate pathways for the biogenesis of cytochrome oxidases in Bradyrhizobium japonicum.Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation.The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis ScoHuman SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1.A targetable fluorescent sensor reveals that copper-deficient SCO1 and SCO2 patient cells prioritize mitochondrial copper homeostasis.Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze-quench EPR study.Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of CuA in human cytochrome oxidaseThe roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidasesFlexibility of the metal-binding region in apo-cupredoxinsCharacterization of the PIB-Type ATPases present in Thermus thermophilus.Copper starvation-inducible protein for cytochrome oxidase biogenesis in Bradyrhizobium japonicumLumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase.Binuclear Cu(A) Formation in Biosynthetic Models of Cu(A) in Azurin Proceeds via a Novel Cu(Cys)2His Mononuclear Copper Intermediate.Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus.Electronic structure of the ground and excited states of the Cu(A) site by NMR spectroscopy.Mechanisms of copper homeostasis in bacteria.The coiled coil-helix-coiled coil-helix proteins may be redox proteins.Divergent functions of the Arabidopsis mitochondrial SCO proteins: HCC1 is essential for COX activity while HCC2 is involved in the UV-B stress response.Seeking the determinants of the elusive functions of Sco proteins.Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatusCopper chaperones. The concept of conformational control in the metabolism of copper.Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the assembly of Cu(B) of cytochrome c oxidase.A novel heme a insertion factor gene cotranscribes with the Thermus thermophilus cytochrome ba3 oxidase locusThe ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.Copper trafficking in biology: an NMR approach.Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein.Analysis of copper-ligand bond lengths in X-ray structures of different types of copper sites in proteins.Functional analysis of the copy 1 of the fixNOQP operon of Ensifer meliloti under free-living micro-oxic and symbiotic conditions.Mono-nuclear copper complexes mimicking the intermediates for the binuclear copper center of the subunit II of cytochrome oxidase: a peptide based approach.
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Mechanism of CuA assembly
@ast
Mechanism of CuA assembly
@en
Mechanism of CuA assembly
@nl
type
label
Mechanism of CuA assembly
@ast
Mechanism of CuA assembly
@en
Mechanism of CuA assembly
@nl
prefLabel
Mechanism of CuA assembly
@ast
Mechanism of CuA assembly
@en
Mechanism of CuA assembly
@nl
P2093
P2860
P50
P356
P1476
Mechanism of CuA assembly
@en
P2093
Alejandro J Vila
Georgios A Spyroulias
Luciano A Abriata
Petros Gkazonis
P2860
P2888
P304
P356
10.1038/NCHEMBIO.110
P577
2008-10-01T00:00:00Z
P5875
P6179
1047312266