Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.
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Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidCThe crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleftA cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli--expression and characterization of cytochrome-tagged Complex I subunitsReconstruction and modeling protein translocation and compartmentalization in Escherichia coli at the genome-scale.Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Mutation of the maturase lipoprotein attenuates the virulence of Streptococcus equi to a greater extent than does loss of general lipoprotein lipidationCharacterization of the secretion pathway of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans.Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial SurfaceNew Escherichia coli outer membrane proteins identified through prediction and experimental verificationSecretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyondTranscriptome analysis of Cronobacter sakazakii ATCC BAA-894 after interaction with human intestinal epithelial cell line HCT-8.Protein secretion in Corynebacterium glutamicum.YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease.Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family.The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential.Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA.The Sec System: Protein Export in Escherichia coli.Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins.Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane.Recombinant Protein Expression System in and Its Application
P2860
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P2860
Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.
description
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name
Targeting and translocation of ...... via the SRP/Sec/YidC pathway.
@en
Targeting and translocation of ...... via the SRP/Sec/YidC pathway.
@nl
type
label
Targeting and translocation of ...... via the SRP/Sec/YidC pathway.
@en
Targeting and translocation of ...... via the SRP/Sec/YidC pathway.
@nl
prefLabel
Targeting and translocation of ...... via the SRP/Sec/YidC pathway.
@en
Targeting and translocation of ...... via the SRP/Sec/YidC pathway.
@nl
P2093
P2860
P356
P1476
Targeting and translocation of ...... i via the SRP/Sec/YidC pathway
@en
P2093
Jan-Willem de Gier
Linda Fröderberg
Louise Baars
P2860
P304
31026-31032
P356
10.1074/JBC.M403229200
P407
P577
2004-05-12T00:00:00Z