The C-terminal region of Bacteroides fragilis toxin is essential to its biological activity - Wikidata - wikimedia - TriplyDB

The C-terminal region of Bacteroides fragilis toxin is essential to its biological activity

The C-terminal region of Bacteroides fragilis toxin is essential to its biological activity

http://www.wikidata.org/entity/Q35073983

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Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog Structural and functional diversity of metalloproteinases encoded by theBacteroides fragilispathogenicity island Enterotoxigenic Bacteroides fragilis: a rogue among symbiotes.Substrate cleavage profiling suggests a distinct function of Bacteroides fragilis metalloproteinases (fragilysin and metalloproteinase II) at the microbiome-inflammation-cancer interface.Peptide Sequence Region That is Essential for the Interactions of the Enterotoxigenic Bacteroides fragilis Metalloproteinase II with E-cadherin.Bacteroides fragilis toxin stimulates intestinal epithelial cell shedding and gamma-secretase-dependent E-cadherin cleavage.Enterotoxigenic and nontoxigenic Bacteroides fragilis strains isolated in Brazil.

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The C-terminal region of Bacteroides fragilis toxin is essential to its biological activity

http://www.wikidata.org/entity/Q35073983

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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The C-terminal region of Bacte ...... ial to its biological activity

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Infection and Immunity

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The C-terminal region of Bacte ...... ial to its biological activity

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Augusto A Franco

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

Cynthia L Sears

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Jai W Shin

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Simy L Buckwold

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed

A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation

The enterotoxin of Bacteroides fragilis is a metalloprotease

Heterologous gene expression in Bacteroides fragilis.

Matrix metalloproteinases in wound repair (review).

Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing.

Molecular evolution of the pathogenicity island of enterotoxigenic Bacteroides fragilis strains.

Identification of a third metalloprotease toxin gene in extraintestinal isolates of Bacteroides fragilis.

Human intestinal epithelial cells swell and demonstrate actin rearrangement in response to the metalloprotease toxin of Bacteroides fragilis.

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5595-5601

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scholarly article

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10.1128/IAI.00135-06

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10

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74

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2006-10-01T00:00:00Z

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6806657

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16988234

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1594940

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