The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.
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The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic ResiduesCrystal Structure of YaeT: Conformational Flexibility and Substrate RecognitionStructural Basis of Outer Membrane Protein Biogenesis in BacteriaFrom Chaperones to the Membrane with a BAM!Outer membrane protein biogenesis in Gram-negative bacteriaA mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditionsDissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagPAssembly of Outer Membrane β-Barrel Proteins: the Bam Complex.The Bam machine: a molecular cooper.PpiD is a player in the network of periplasmic chaperones in Escherichia coli.Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransportersReconstitution of outer membrane protein assembly from purified componentsRoles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence.The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domainsProtein secretion and outer membrane assembly in AlphaproteobacteriaThe periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli.Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization.The bacterial cell envelope.Suppression of bladder epithelial cytokine responses by uropathogenic Escherichia coli.Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coliReconstruction and modeling protein translocation and compartmentalization in Escherichia coli at the genome-scale.A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters.Identification of Shigella flexneri IcsA residues affecting interaction with N-WASP, and evidence for IcsA-IcsA co-operative interaction.Maturation of intracellular Escherichia coli communities requires SurA.Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence.The virulence factor PEB4 (Cj0596) and the periplasmic protein Cj1289 are two structurally related SurA-like chaperones in the human pathogen Campylobacter jejuniDiverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA.NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.Interactions between folding factors and bacterial outer membrane proteins.Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane ProteinsProteomic methods unravel the protein quality control in Escherichia coli.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?The β-Barrel Assembly Machinery Complex.Protein folding in the cell envelope of Escherichia coli.
P2860
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P2860
The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The periplasmic molecular chap ...... egral outer membrane proteins.
@ast
The periplasmic molecular chap ...... egral outer membrane proteins.
@en
type
label
The periplasmic molecular chap ...... egral outer membrane proteins.
@ast
The periplasmic molecular chap ...... egral outer membrane proteins.
@en
prefLabel
The periplasmic molecular chap ...... egral outer membrane proteins.
@ast
The periplasmic molecular chap ...... egral outer membrane proteins.
@en
P2860
P356
P1476
The periplasmic molecular chap ...... egral outer membrane proteins.
@en
P2093
David B McKay
Eduard Bitto
P2860
P304
49316-49322
P356
10.1074/JBC.M308853200
P407
P577
2003-09-23T00:00:00Z