Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.
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A pathway for disulfide bond formation in vivoTwo cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaEfficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasmStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneThe complete general secretory pathway in gram-negative bacteriaLegionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerizationMutational analysis of the disulfide catalysts DsbA and DsbB.An export-specific reporter designed for gram-positive bacteria: application to Lactococcus lactis.The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasmElectron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris.XC_0531 encodes a c-type cytochrome biogenesis protein and is required for pathogenesis in Xanthomonas campestris pv. campestris.Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membraneEvidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbABradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosisIdentification and functional analysis of an immunoreactive DsbA-like thio-disulfide oxidoreductase of Ehrlichia spp.Structure and mechanism of RND-type multidrug efflux pumpsReduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin.The OmpL porin does not modulate redox potential in the periplasmic space of Escherichia coli.Detecting folding intermediates of a protein as it passes through the bacterial translocation channelSecretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements.Protein folding in the bacterial periplasmTransduction of envelope stress in Escherichia coli by the Cpx two-component system.NlpI-mediated modulation of outer membrane vesicle production through peptidoglycan dynamics in Escherichia coli.PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbAMutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.Cytochromes c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like proteinIdentification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivoBiogenesis of respiratory cytochromes in bacteria.Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cellsOverproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbAAn in vivo pathway for disulfide bond isomerization in Escherichia coliPeptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogensProtein secretion in Bacillus species.Functions of the gene products of Escherichia coli.Synthetic effect between envelope stress and lack of outer membrane vesicle production in Escherichia coli.A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae RdTranslocation of a folded protein across the outer membrane in Escherichia coli.
P2860
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P2860
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Identification and characteriz ...... phatase, a periplasmic enzyme.
@ast
Identification and characteriz ...... phatase, a periplasmic enzyme.
@en
type
label
Identification and characteriz ...... phatase, a periplasmic enzyme.
@ast
Identification and characteriz ...... phatase, a periplasmic enzyme.
@en
prefLabel
Identification and characteriz ...... phatase, a periplasmic enzyme.
@ast
Identification and characteriz ...... phatase, a periplasmic enzyme.
@en
P2093
P2860
P1433
P1476
Identification and characteriz ...... phatase, a periplasmic enzyme.
@en
P2093
P2860
P407
P577
1992-01-01T00:00:00Z