ArticleComputational and structural biotechnology journal2024
Ion and water permeation through claudin-10b and claudin-15 paracellular channels.
Article in Computational and structural biotechnology journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- A multi-pore model of the blood-brain barrier tight junction strands recapitulates the permeability features of wild-type and mutant claudin-5.Protein science : a publication of the Protein Society · 2025Article
- MSF-CPMP: A novel multi-source feature fusion model for prediction of cyclic peptide membrane permeability.Computational and structural biotechnology journal · 2025Article
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4 authors.
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Abstract
The structural scaffold of epithelial and endothelial tight junctions (TJs) comprises multimeric strands of claudin (Cldn) proteins that anchor adjacent cells and control the paracellular flux of water and solutes. Based on the permeability properties they confer to the TJs, Cldns are classified as channel- or barrier-forming. For instance, Cldn10b, expressed in kidneys, lungs, and other tissues, displays high permeability for cations and low permeability for water. Along with its high sequence similarity to the cation- and water-permeable TJ protein Cldn15, this makes Cldn10b a valuable test case for investigating the molecular determinants of paracellular transport. In lack of high-resolution experimental information on TJ architectures, here we use molecular dynamics simulations to determine whether atomistic models recapitulate the differences in ion and water transport between of Cldn10b and Cldn15. Our data, based on extensive standard simulations and free energy calculations, reveal that Cldn10b models form cation-permeable pores narrower than Cldn15, which, together with the stable coordination of Na
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