Enteropathogenic Escherichia coli infection leads to appearance of aberrant tight junctions strands in the lateral membrane of intestinal epithelial cells

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Cellular Microbiology

• Publication date

  2004-08-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1111/j.1462-5822.2004.00404.xPMID 15236645
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Tight junction proteins.

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• Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion.

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• Tight Junctions and Cell Surface Lipid Polarity

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• Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin‐3, a tight junction integral membrane protein

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• Enteropathogenic E. coli secreted protein F is required for alteration of host intestinal epithelial barrier function

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• Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions

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• Clostridium perfringens Enterotoxin Fragment Removes Specific Claudins from Tight Junction Strands

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• Protein Interactions at the Tight Junction

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• Redistribution and Phosphorylation of Occludin During Opening and Resealing of Tight Junctions in Cultured Epithelial Cells

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• Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins

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