The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.
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Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM.Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins.Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pyloriTwo-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membraneAssembly of Outer Membrane β-Barrel Proteins: the Bam Complex.The Bam machine: a molecular cooper.Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.PpiD is a player in the network of periplasmic chaperones in Escherichia coli.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 domainsAssembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.Refolding of Escherichia coli outer membrane protein F in detergent creates LPS-free trimers and asymmetric dimersFolding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.Dynamic interaction of the sec translocon with the chaperone PpiDRole of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Detecting folding intermediates of a protein as it passes through the bacterial translocation channelBacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin.Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.Interactions between folding factors and bacterial outer membrane proteins.Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes.Advances in understanding bacterial outer-membrane biogenesis.Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane ProteinsRole for Skp in LptD assembly in Escherichia coli.Protein disorder is positively correlated with gene expression in Escherichia coli.Integrating protein homeostasis strategies in prokaryotes.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.The lipopolysaccharide export pathway in Escherichia coli: structure, organization and regulated assembly of the Lpt machineryMechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?The Sec translocon mediated protein transport in prokaryotes and eukaryotes.The β-Barrel Assembly Machinery Complex.Skp is a multivalent chaperone of outer-membrane proteinsMisfolding of a bacterial autotransporter.The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation.Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding.The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization.Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System.Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism.Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture.
P2860
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P2860
The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
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2001年学术文章
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2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
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2001年學術文章
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name
The early interaction of the o ...... s at the cytoplasmic membrane.
@en
The early interaction of the o ...... s at the cytoplasmic membrane.
@nl
type
label
The early interaction of the o ...... s at the cytoplasmic membrane.
@en
The early interaction of the o ...... s at the cytoplasmic membrane.
@nl
prefLabel
The early interaction of the o ...... s at the cytoplasmic membrane.
@en
The early interaction of the o ...... s at the cytoplasmic membrane.
@nl
P2093
P2860
P356
P1476
The early interaction of the o ...... s at the cytoplasmic membrane.
@en
P2093
Koningstein G
P2860
P304
18804-18811
P356
10.1074/JBC.M011194200
P407
P577
2001-03-05T00:00:00Z