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Article

Mutated C-terminal fragments of Clostridium perfringens enterotoxin have increased affinity to claudin-4 and reversibly modulate tight junctions in vitro.

Biochemical and biophysical research communications - 8 Jul 2011

Takahashi Azusa, Kondoh Masuo, Uchida Hiroshi, Kakamu Yohei, Hamakubo Takao, Yagi Kiyohito

Abstract excerpt

Passage across epithelial cell sheets is the first step in drug absorption. Tight junctions (TJs) are located between adjacent epithelial cells and seal the intercellular space preventing leakage of solutes. Claudin, a tetra-transmembrane protein family, is a pivotal functional and structural component of the TJ barrier. Modulation of the claudin-based TJ seal is a strategy for mucosal drug absorption. We...

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PMID: 21672529
DOI: 10.1016/j.bbrc.2011.05.161

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CPE

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutated C-terminal fragments of Clostridium perfringens enterotoxin have increased affinity to claudin-4 and reversibly modulate tight junctions in vitro.PMID 21672529Read ↗

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