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- W1149440014 abstract "Publisher Summary Claudins are tight junction membrane proteins that form both the paracellular pore and barrier. This chapter reviews current knowledge about the structure and function of the claudin pore and the types of methods that are used to address this. The chapter presents the evidence that the first extracellular domains of multiple claudin monomers fold to enclose a charge-selective paracellular ion pore with a diameter of 6.5–8 Ǻ. The location of specific amino acid residues relative to the pore and their role in determining charge selectivity is also discussed. The general approach to elucidating the paracellular properties of claudins is to overexpress it by transfection into a host cell line. The cells are then grown to a confluent monolayer. Ideally, they are mounted in Ussing chambers and transepithelial permeabilities are determined either from the measurements of diffusion potentials at steady state or from the kinetic measurements of conductance or unidirectional radiotracer fluxes." @default.
- W1149440014 created "2016-06-24" @default.
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- W1149440014 date "2010-01-01" @default.
- W1149440014 modified "2023-09-27" @default.
- W1149440014 title "Structure–Function Studies of the Claudin Pore" @default.
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- W1149440014 doi "https://doi.org/10.1016/s1063-5823(10)65004-1" @default.
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