Requirement for YaeT in the outer membrane assembly of autotransporter proteins. - Wikidata - wikimedia - TriplyDB

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

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Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence Autotransporter structure reveals intra-barrel cleavage followed by conformational changes A novel virulence strategy for Pseudomonas aeruginosa mediated by an autotransporter with arginine-specific aminopeptidase activity The TamB ortholog of Borrelia burgdorferi interacts with the β-barrel assembly machine (BAM) complex protein BamA Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA.Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.The passenger-associated transport repeat promotes virulence factor secretion efficiency and delineates a distinct autotransporter subtype.The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate.Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins.Translocation path of a substrate protein through its Omp85 transporter.The bacterial outer membrane β-barrel assembly machinery.Characterization of Esterase A, a Pseudomonas stutzeri A15 Autotransporter.Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries.Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membrane The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli The essential β-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis.Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein.Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters Importance of conserved residues of the serine protease autotransporter beta-domain in passenger domain processing and beta-barrel assembly Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.Folding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coli Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB.Protein secretion and outer membrane assembly in Alphaproteobacteria Intramolecular interactions between the protease and structural domains are important for the functions of serine protease autotransporters A genome-scale proteomic screen identifies a role for DnaK in chaperoning of polar autotransporters in Shigella.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters.Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.Identification of Shigella flexneri IcsA residues affecting interaction with N-WASP, and evidence for IcsA-IcsA co-operative interaction.Autotransporter-based cell surface display in Gram-negative bacteria.Secretome of obligate intracellular Rickettsia.Genetic reporter system for positioning of proteins at the bacterial pole.VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli.Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria Mutagenesis of the Shigella flexneri autotransporter IcsA reveals novel functional regions involved in IcsA biogenesis and recruitment of host neural Wiscott-Aldrich syndrome protein Molecular Characterization of the Vacuolating Autotransporter Toxin in Uropathogenic Escherichia coli.

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Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

http://www.wikidata.org/entity/Q30157971

description

2007 nî lūn-bûn

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2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2007 թվականի մայիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

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Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

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type

label

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

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Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

@en

prefLabel

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

@ast

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

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Journal of Bacteriology

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Requirement for YaeT in the outer membrane assembly of autotransporter proteins.

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Marcia B Goldberg

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Sumita Jain

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P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.

Role of a highly conserved bacterial protein in outer membrane protein assembly

A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR

Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.

Kinetic 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.

YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli.

Molecular architecture and function of the Omp85 family of proteins.

Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA

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5393-5398

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scholarly article

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10.1128/JB.00228-07

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14

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189

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2007-05-18T00:00:00Z

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6319988

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17513479

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1951886

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