Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa. - Test2 - elhamkhani - TriplyDB

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

http://www.wikidata.org/entity/Q37907307

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Animal Enterotoxigenic Escherichia coli.Small Intestinal Infections.Clarification of linaclotide pharmacology presented in a recent clinical study of plecanatide.Modulating the Global Response Regulator, LuxO of V. cholerae Quorum Sensing System Using a Pyrazine Dicarboxylic Acid Derivative (PDCApy): An Antivirulence Approach Staphylococcus aureus enterotoxins A- and B: binding to the enterocyte brush border and uptake by perturbation of the apical endocytic membrane traffic.Clostridium Bacteria and Autism Spectrum Conditions: A Systematic Review and Hypothetical Contribution of Environmental Glyphosate Levels.Bacterial Toxins - Structure, Properties and Mode of Action

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Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

http://www.wikidata.org/entity/Q37907307

description

article científic

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article scientifique

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articol științific

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articolo scientifico

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artigo científico

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artigo científico

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artigo científico

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artikel ilmiah

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artículo científico

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name

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

@en

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

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type

label

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

@en

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

@nl

prefLabel

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

@en

Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

@nl

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Future Microbiology

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Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.

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M R Popoff

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Development of the human infant intestinal microbiota

Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum

CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin

Clostridium difficile toxins: mechanism of action and role in disease.

Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins

Toxin B is essential for virulence of Clostridium difficile

Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria

Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1

Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity

Structure of the claudin-binding domain of Clostridium perfringens enterotoxin

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763-797

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scholarly article

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10.2217/FMB.11.58

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7

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