Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
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Disulfide bond formation in the bacterial periplasm: major achievements and challenges aheadCytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Many roles of the bacterial envelope reducing pathwaysReducing systems protecting the bacterial cell envelope from oxidative damageA strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome cCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEProtein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid PhosphorylationStructural Plasticity of the Thioredoxin Recognition Site of Yeast Methionine S-Sulfoxide Reductase Mxr1Oxidation State-dependent Protein-Protein Interactions in Disulfide CascadesAn Extended Active-site Motif Controls the Reactivity of the Thioredoxin FoldThioredoxin-like protein TlpA from Bradyrhizobium japonicum is a reductant for the copper metallochaperone ScoILegionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerizationThe Vibrio cholerae Cpx envelope stress response senses and mediates adaptation to low iron.A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelopeGenomic island genes in a coastal marine Synechococcus strain confer enhanced tolerance to copper and oxidative stress.The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.Thioredoxin-like proteins in F and other plasmid systemsCytochrome c biogenesis: the Ccm system.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.The active-site cysteinyls and hydrophobic cavity residues of ResA are important for cytochrome c maturation in Bacillus subtilisBiochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability.The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli.1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli.Genetic analysis of activation of the Vibrio cholerae Cpx pathway.Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.Control of periplasmic interdomain thiol:disulfide exchange in the transmembrane oxidoreductase DsbD.Helix swapping leads to dimerization of the N-terminal domain of the c-type cytochrome maturation protein CcmH from Escherichia coli.(1)H, (13)C and (15)N backbone and side-chain resonance assignments of reduced CcmG from Escherichia coli.The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome c maturation.Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase.The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.Molecular Mechanisms of the Methionine Sulfoxide Reductase System fromMolecular Basis for Specificity of the Extracytoplasmic Thioredoxin ResA
P2860
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P2860
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@en
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@nl
type
label
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@en
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@nl
prefLabel
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@en
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@nl
P2093
P1433
P1476
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
@en
P2093
Anna Rozhkova
Christian U Stirnimann
Guido Capitani
Markus G Grütter
Rudi Glockshuber
Ulla Grauschopf
P304
P356
10.1016/J.STR.2005.04.014
P577
2005-07-01T00:00:00Z