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Reducing systems protecting the bacterial cell envelope from oxidative damageMolecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulenceStructure and multistate function of the transmembrane electron transporter CcdALegionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerizationBacterial thiol oxidoreductases - from basic research to new antibacterial strategiesStructure of a DsbF homologue from Corynebacterium diphtheriae.Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive BacteriaFunctional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domainThioredoxin-like proteins in F and other plasmid systemsEngineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231)Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis.The 'captain of the men of death', Streptococcus pneumoniae, fights oxidative stress outside the 'city wall'.A new role for Escherichia coli DsbC protein in protection against oxidative stressRepairing oxidized proteins in the bacterial envelope using respiratory chain electrons.Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants.Solution structure and elevator mechanism of the membrane electron transporter CcdA.Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.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.Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase.
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Many roles of the bacterial envelope reducing pathways
@ast
Many roles of the bacterial envelope reducing pathways
@en
Many roles of the bacterial envelope reducing pathways
@nl
type
label
Many roles of the bacterial envelope reducing pathways
@ast
Many roles of the bacterial envelope reducing pathways
@en
Many roles of the bacterial envelope reducing pathways
@nl
prefLabel
Many roles of the bacterial envelope reducing pathways
@ast
Many roles of the bacterial envelope reducing pathways
@en
Many roles of the bacterial envelope reducing pathways
@nl
P2860
P3181
P356
P1476
Many roles of the bacterial envelope reducing pathways
@en
P2093
Seung-Hyun Cho
P2860
P304
P3181
P356
10.1089/ARS.2012.4962
P407
P577
2013-05-01T00:00:00Z