The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
about
Protein quality control in the bacterial periplasmThe Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic ResiduesThe prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activityStructural Basis for Two-component System Inhibition and Pilus Sensing by the Auxiliary CpxP ProteinThe yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress.PpiA, a surface PPIase of the cyclophilin family in Lactococcus lactisA Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.How does a β-barrel integral membrane protein insert into the membrane?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 activity and specificity of the outer membrane protein chaperone SurA are modulated by a proline isomerase domain.Dissecting 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.Roles 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.Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics.Protein secretion and outer membrane assembly in AlphaproteobacteriaKinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment.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.Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.The 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.Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.The bacterial cell envelope.Characterization of six lipoproteins in the sigmaE regulon.Suppression of bladder epithelial cytokine responses by uropathogenic Escherichia coli.The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactisPeriplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coliMicrobial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its captureSelf-association of unfolded outer membrane proteins.Mealybugs nested endosymbiosis: going into the 'matryoshka' system in Planococcus citri in depth.Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Interaction of Rickettsia felis with histone H2B facilitates the infection of a tick cell line.Maturation of intracellular Escherichia coli communities requires SurA.Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence.
P2860
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P2860
The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The SurA periplasmic PPIase la ...... ivo and has chaperone activity
@nl
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@ast
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@en
type
label
The SurA periplasmic PPIase la ...... ivo and has chaperone activity
@nl
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@ast
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@en
prefLabel
The SurA periplasmic PPIase la ...... ivo and has chaperone activity
@nl
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@ast
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@en
P2093
P2860
P3181
P356
P1433
P1476
The SurA periplasmic PPIase la ...... vo and has chaperone activity.
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/20.1.285
P407
P577
2001-01-01T00:00:00Z