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• W3027455652 abstract "Abstract One of the most common mutations in Cystic Fibrosis (CF) patients is the deletion of the amino acid phenylalanine at position 508. This mutation causes both the protein trafficking defect and an early degradation. Over time, small molecules, called correctors, capable of increasing the amount of mutated channel in the plasma membrane and causing an increase in its transport activity have been developed. This study shows that incubating in vitro cells permanently transfected with the mutated channel with the correctors VX809, VX661 and Corr4a, and the combination of VX809 and Corr4a, a recovery of anion transport activity is observed. Interestingly, the permeability of bicarbonate increases in the cells containing corrected p.F508del CFTR channels is greater than the increase of the halide permeability. These different increases of the permeability of bicarbonate and halides are consistent with the concept that the structural conformation of the pore of the corrector-rescued p.F508del channels would be different than the normal wild type CFTR protein." @default.
• W3027455652 created "2020-05-29" @default.
• W3027455652 creator A5038418968 @default.
• W3027455652 creator A5074009232 @default.
• W3027455652 creator A5079336753 @default.
• W3027455652 date "2020-05-21" @default.
• W3027455652 modified "2023-09-27" @default.
• W3027455652 title "Correctors modify the bicarbonate permeability of F508del-CFTR" @default.
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• W3027455652 doi "https://doi.org/10.1038/s41598-020-65287-4" @default.
• W3027455652 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7242338" @default.
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• W3027455652 hasPublicationYear "2020" @default.
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