New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH.
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RfaH suppresses small RNA MicA inhibition of fimB expression in Escherichia coli K-12SigmaE-dependent small RNAs of Salmonella respond to membrane stress by accelerating global omp mRNA decayRelease of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress responseProtein quality control in the bacterial periplasmCrystal structure of a defective folding proteinCrystal structure of RseB and a model of its binding mode to RseAThe Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic ResiduesSome Like It Hot: Heat Resistance of Escherichia coli in FoodSystematic deletion of Salmonella small RNA genes identifies CyaR, a conserved CRP-dependent riboregulator of OmpX synthesisThe SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.Similarities between exogenously- and endogenously-induced envelope stress: the effects of a new antibacterial molecule, TPI1609-10PepD participates in the mycobacterial stress response mediated through MprAB and SigECharacterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coliLipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.The activity and specificity of the outer membrane protein chaperone SurA are modulated by a proline isomerase domain.Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.The 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.Folding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coliCharacterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics.The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domainsAssembly 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.SigmaE is an essential sigma factor in Escherichia coli.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 crescentusChaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Selection for a periplasmic factor improving phage display and functional periplasmic expression.The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.The extracytoplasmic stress factor, sigmaE, is required to maintain cell envelope integrity in Escherichia coli.The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasmAssembly of lipopolysaccharide in Escherichia coli requires the essential LapB heat shock proteinBivalent Formation 1, a plant-conserved gene, encodes an OmpH/coiled-coil motif-containing protein required for meiotic recombination in rice.Role of the Escherichia coli SurA protein in stationary-phase survival.Potential of a novel protein, OMP26, from nontypeable Haemophilus influenzae to enhance pulmonary clearance in a rat model.Temporal transcriptomic response during arsenic stress in Herminiimonas arsenicoxydans.Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB.A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
P2860
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P2860
New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
New components of protein fold ...... coli SurA, FkpA and Skp/OmpH.
@en
type
label
New components of protein fold ...... coli SurA, FkpA and Skp/OmpH.
@en
prefLabel
New components of protein fold ...... coli SurA, FkpA and Skp/OmpH.
@en
P2093
P1476
New components of protein fold ...... coli SurA, FkpA and Skp/OmpH.
@en
P2093
P304
P356
10.1046/J.1365-2958.1996.561412.X
P407
P577
1996-08-01T00:00:00Z