Quantitative proteomic analysis of type III secretome of enteropathogenic Escherichia coli reveals an expanded effector repertoire for attaching/effacing bacterial pathogens.
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From ingestion to colonization: the influence of the host environment on regulation of the LEE encoded type III secretion system in enterohaemorrhagic Escherichia coliType Three Secretion System in Attaching and Effacing PathogensRecent advances in understanding enteric pathogenic Escherichia coli.Effective identification of Gram-negative bacterial type III secreted effectors using position-specific residue conservation profiles.Metalloprotease NleC suppresses host NF-κB/inflammatory responses by cleaving p65 and interfering with the p65/RPS3 interactionThe Serine Protease EspC from Enteropathogenic Escherichia coli Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System.Shotgun proteomics of bacterial pathogens: advances, challenges and clinical implications.Novel Host Proteins and Signaling Pathways in Enteropathogenic E. coli Pathogenesis Identified by Global Phosphoproteome Analysis.Role of EscP (Orf16) in injectisome biogenesis and regulation of type III protein secretion in enteropathogenic Escherichia coliComparative Secretome Analysis of Ralstonia solanacearum Type 3 Secretion-Associated Mutants Reveals a Fine Control of Effector Delivery, Essential for Bacterial PathogenicityBiophysical Characterization and Activity of Lymphostatin, a Multifunctional Virulence Factor of Attaching and Effacing Escherichia coli.The Aeromonas salmonicida subsp. salmonicida exoproteome: determination of the complete repertoire of Type-Three Secretion System effectors and identification of other virulence factors.Citrobacter Infection and Wnt signaling.Exoproteomics: exploring the world around biological systems.In vitro and in vivo model systems for studying enteropathogenic Escherichia coli infections.Inhibition of Antigen-Specific and Nonspecific Stimulation of Bovine T and B Cells by Lymphostatin from Attaching and Effacing Escherichia coli.Sharpening Host Defenses during Infection: Proteases Cut to the Chase.Functional Characterization of EscK (Orf4), a Sorting Platform Component of the Enteropathogenic Escherichia coli Injectisome.Quantitative proteomic analysis of Burkholderia pseudomallei Bsa type III secretion system effectors using hypersecreting mutants.Identification of a novel Salmonella type III effector by quantitative secretome profiling.Secretome analysis of diarrhea-inducing strains of Escherichia coliA quantitative proteomic screen of the Campylobacter jejuni flagellar-dependent secretome.The Ruler Protein EscP of the Enteropathogenic Escherichia coli Type III Secretion System Is Involved in Calcium Sensing and Secretion Hierarchy Regulation by Interacting with the Gatekeeper Protein SepL.SepD/SepL-dependent secretion signals of the type III secretion system translocator proteins in enteropathogenic Escherichia coli.Synergism Between Bacterial GAPDH and OMVs: Disparate Mechanisms but Co-Operative Action.A distinct regulatory sequence is essential for the expression of a subset of nle genes in attaching and effacing Escherichia coli.Dynamics of the type III secretion system activity of enteropathogenic Escherichia coli.Engineering the Controlled Assembly of Filamentous Injectisomes in E. coli K-12 for Protein Translocation into Mammalian Cells.Identification of novel substrates of Shigella T3SA through analysis of its virulence plasmid-encoded secretome.Attaching and effacing (A/E) lesion formation by enteropathogenic E. coli on human intestinal mucosa is dependent on non-LEE effectors.Proteogenomics in Aid of Host-Pathogen Interaction Studies: A Bacterial Perspective.Novel insights into the mechanism of SepL-mediated control of effector secretion in enteropathogenic Escherichia coli.Jump transition observed in translocation time for ideal poly-X proteinogenic chains as a result of competing folding and anchoraging contributions.
P2860
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P2860
Quantitative proteomic analysis of type III secretome of enteropathogenic Escherichia coli reveals an expanded effector repertoire for attaching/effacing bacterial pathogens.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
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2012年學術文章
@zh-hant
name
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@ast
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@en
type
label
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@ast
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@en
prefLabel
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@ast
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@en
P2093
P2860
P356
P1476
Quantitative proteomic analysi ...... /effacing bacterial pathogens.
@en
P2093
B Brett Finlay
Carmen L de Hoog
Leonard J Foster
Nikolay Stoynov
Wanyin Deng
P2860
P304
P356
10.1074/MCP.M111.013672
P577
2012-06-01T00:00:00Z