On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily
about
Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsAEffect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.Disulfide bond formation in prokaryotes: history, diversity and designA selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo.Mechanism of the electron transfer catalyst DsbB from Escherichia coli.Regulation of protein function by glutathionylation.Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231)Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Mechanisms of oxidative protein folding in the bacterial cell envelope.The biological roles of glutaredoxins.Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway.Insights into Trx1, TRP14, and Prx1 homologs of Paralichthys olivaceus: molecular profiles and transcriptional responses to immune stimulations.Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB.Protein folding drives disulfide formation.Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation.Prediction of pKa and redox properties in the thioredoxin superfamily.A small family of chloroplast atypical thioredoxins.Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant.A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation.
P2860
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P2860
On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2000 թվականի փետրվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
On the functional interchangea ...... of the thioredoxin superfamily
@ast
On the functional interchangea ...... of the thioredoxin superfamily
@en
type
label
On the functional interchangea ...... of the thioredoxin superfamily
@ast
On the functional interchangea ...... of the thioredoxin superfamily
@en
prefLabel
On the functional interchangea ...... of the thioredoxin superfamily
@ast
On the functional interchangea ...... of the thioredoxin superfamily
@en
P2860
P1476
On the functional interchangea ...... of the thioredoxin superfamily
@en
P2093
J Beckwith
P2860
P304
P356
10.1128/JB.182.3.723-727.2000
P407
P577
2000-02-01T00:00:00Z