Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae. - Wikidata - awgldk - TriplyDB

Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.

Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.

http://www.wikidata.org/entity/Q34489246

about

Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence Serine protease EspP from enterohemorrhagic Escherichia coli is sufficient to induce shiga toxin macropinocytosis in intestinal epithelium.Recent advances in understanding enteric pathogenic Escherichia coli.The Serine Protease EspC from Enteropathogenic Escherichia coli Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System.Animal models of enteroaggregative Escherichia coli infection.Pathogenesis of human enterovirulent bacteria: lessons from cultured, fully differentiated human colon cancer cell lines EspC promotes epithelial cell detachment by enteropathogenic Escherichia coli via sequential cleavages of a cytoskeletal protein and then focal adhesion proteins.Atypical enteropathogenic Escherichia coli secretes plasmid encoded toxin.Actin cytoskeleton manipulation by effector proteins secreted by diarrheagenic Escherichia coli pathotypes.

P2860

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P2860

Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.

http://www.wikidata.org/entity/Q34489246

description

2010 nî lūn-bûn

@nan

2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մայիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Host-Toxin Interactions Involv ...... ers of the Enterobacteriaceae.

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Host-Toxin Interactions Involv ...... ers of the Enterobacteriaceae.

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Host-Toxin Interactions Involv ...... ers of the Enterobacteriaceae.

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Fernando Navarro-Garcia

http://www.w3.org/2001/XMLSchema#string

Ken Teter

http://www.w3.org/2001/XMLSchema#string

Michael Sonnested

http://www.w3.org/2001/XMLSchema#string

P2860

Diarrheagenic Escherichia coli

The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome

Ricin A chain insertion into endoplasmic reticulum membranes is triggered by a temperature increase to 37 {degrees}C

One step at a time: endoplasmic reticulum-associated degradation

Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells

Pathogenic Escherichia coli

Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.

Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.

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

Pet, an autotransporter enterotoxin from enteroaggregative Escherichia coli.

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1134-1147

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scholarly article

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10.3390/TOXINS2051134

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5

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2

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2010-05-01T00:00:00Z

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49763201

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21243083

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3020798

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