Claudins and epithelial paracellular transport.

By C. V. Van Itallie, James M. Anderson. Annual Review of Physiology, 2006

1,133 citations recorded by the source corpus.

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Citations in the corpus

Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. (2008, background): “Although claudins do not share sequence similarity with the occludin family, they also comprise a tetra-span transmembrane protein [92] with two extracellular loops [5,91].”
Tight Junction Pore and Leak Pathways: A Dynamic Duo (2011, background): “As briefly described above and reviewed in detail elsewhere (43), the claudin residues responsible for ion selectivity and modulation of pore pathway permeability by changes in claudin protein expression have been well documented in cell culture (34, 37, 38, 40, 137–141), animal models (16, 32), and”
Regulation of the intestinal barrier by nutrients: The role of tight junctions (2020, background): “Claudins 3, 4, 7, and 14 form a selective barrier to macromolecules and ions, whereas claudins 2, 12, and 15 form selective pores to ions and water and thereby increase the intestinal permeability (Van Itallie & Anderson, 2006).”
Intestinal Permeability Regulation by Tight Junction: Implication on Inflammatory Bowel Diseases (2015, background): “The extracellular loops of claudin molecules make hemophilic and heterophilic interactions with adjacent cells and the interactions create either barriers against or pores for the passage of selective molecules in the paracellular pathways.(12,28) Numerous studies have demonstrated that claudins are”
Endothelial adherens junctions control tight junctions by VE-cadherin-mediated upregulation of claudin-5 (2008, background): “Claudins are a multigene family of at least 24 members, each of which has a specific tissue expression patter”
Intestinal barrier function: molecular regulation and disease pathogenesis. (2009, background): “The intracellular C-terminal domain of claudin possesses multiple regulatory sites, including potential serine and threonine phosphorylation sites and PDZ-binding domains.(7) Phosphorylation of claudin-3 and 4 in ovarian cancer cells is linked to the regulation of paracellular permeability.”
Regulation of intestinal epithelial permeability by tight junctions (2012, background): “The extracellular loops of claudin molecules make homophilic and heterophilic interactions with adjacent cells, and the interactions create either barriers against or pores for the passage of selective molecules in the paracellular pathways [5, 44].”