about
All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascadeThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter acetiOpen and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand bindingProperties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid ResidueProtein S-Thiolation by Glutathionylspermidine (Gsp): THE ROLE OF ESCHERICHIA COLI Gsp SYNTHETASE/AMIDASE IN REDOX REGULATIONDomain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Glutathione in Cellular Redox Homeostasis: Association with the Excitatory Amino Acid Carrier 1 (EAAC1)Cysteine scanning of MscL transmembrane domains reveals residues critical for mechanosensitive channel gating.Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxinMolecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: a [4Fe-4S] cluster co-ordinating protein disulphide reductaseA mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stressAuranofin exerts broad-spectrum bactericidal activities by targeting thiol-redox homeostasisCellular defenses against superoxide and hydrogen peroxideIntegration of time-resolved transcriptomics data with flux-based methods reveals stress-induced metabolic adaptation in Escherichia coli.The dithiol:disulfide oxidoreductases DsbA and DsbB of Rhodobacter capsulatus are not directly involved in cytochrome c biogenesis, but their inactivation restores the cytochrome c biogenesis defect of CcdA-null mutantsEngineering antibody fragments to fold in the absence of disulfide bonds.Relationship between recombinant protein expression and host metabolome as determined by two-dimensional NMR spectroscopyDisulfide bond formation in prokaryotes: history, diversity and designGene expression in Porphyromonas gingivalis after contact with human epithelial cells.Expression of three essential antioxidants of Helicobacter pylori in clinical isolates.Proteomics-based identification of differentially abundant proteins reveals adaptation mechanisms of Xanthomonas citri subsp. citri during Citrus sinensis infection.Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.Heme biosynthesis is coupled to electron transport chains for energy generation.Posttranslational protein modification in Archaea.Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomeraseThe parasite-specific trypanothione metabolism of trypanosoma and leishmania.In-cell NMR in E. coli to monitor maturation steps of hSOD1.An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signalsComplete pathway for protein disulfide bond formation encoded by poxvirusesMetabolism and virulence in Neisseria meningitidis.A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status.Molecular and physiological analysis of three Pseudomonas aeruginosa phages belonging to the "N4-like viruses".Formation and transfer of disulphide bonds in living cells.Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.Whole-genome transcriptional analysis of heavy metal stresses in Caulobacter crescentus.Thiol/Disulfide system plays a crucial role in redox protection in the acidophilic iron-oxidizing bacterium Leptospirillum ferriphilum.A connecter-like factor, CacA, links RssB/RpoS and the CpxR/CpxA two-component system in Salmonella.The diverse antioxidant systems of Helicobacter pylori.A novel component of the disulfide-reducing pathway required for cytochrome c assembly in plastids.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Roles of thiol-redox pathways in bacteria.
@ast
Roles of thiol-redox pathways in bacteria.
@en
Roles of thiol-redox pathways in bacteria.
@nl
type
label
Roles of thiol-redox pathways in bacteria.
@ast
Roles of thiol-redox pathways in bacteria.
@en
Roles of thiol-redox pathways in bacteria.
@nl
prefLabel
Roles of thiol-redox pathways in bacteria.
@ast
Roles of thiol-redox pathways in bacteria.
@en
Roles of thiol-redox pathways in bacteria.
@nl
P1476
Roles of thiol-redox pathways in bacteria.
@en
P2093
P356
10.1146/ANNUREV.MICRO.55.1.21
P577
2001-01-01T00:00:00Z