A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
about
Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeThe Escherichia coli proteome: past, present, and future prospectsProtein quality control in the bacterial periplasmMechanism to control the cell lysis and the cell survival strategy in stationary phase under heat stressThe prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activityStructure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27Some Like It Hot: Heat Resistance of Escherichia coli in FoodRegulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stressStructural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerasesThe SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refoldingA Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.Outer membrane protein biogenesis in Gram-negative bacteriaIdentification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditionsThe Bam machine: a molecular cooper.Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein.PpiD is a player in the network of periplasmic chaperones in Escherichia coli.Involvement and necessity of the Cpx regulon in the event of aberrant beta-barrel outer membrane protein assembly.Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase.The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines.Isolation and characterization of NaCl-sensitive mutants of Caulobacter crescentusCombining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin.Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Protein complexes of the Escherichia coli cell envelope.Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli.Characterization of the Cpx regulon in Escherichia coli strain MC4100.Microbial interactions and differential protein expression in Staphylococcus aureus -Candida albicans dual-species biofilms.Assembly of lipopolysaccharide in Escherichia coli requires the essential LapB heat shock proteinThe acetate switch.Serodiagnosis of human granulocytic ehrlichiosis by using novel combinations of immunoreactive recombinant proteins.Dynamic interaction of the sec translocon with the chaperone PpiDThe CpxRA signal transduction system of Escherichia coli: growth-related autoactivation and control of unanticipated target operons.Cpx two-component signal transduction in Escherichia coli: excessive CpxR-P levels underlie CpxA* phenotypes.Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated.Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilisComplex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene.
P2860
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P2860
A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@ast
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@en
type
label
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@ast
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@en
prefLabel
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@ast
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@en
P2860
P356
P1433
P1476
A new heat-shock gene, ppiD, e ...... e proteins in Escherichia coli
@en
P2093
Dartigalongue C
P2860
P304
P356
10.1093/EMBOJ/17.14.3968
P407
P577
1998-07-01T00:00:00Z