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Current treatments for cystic fibrosis target the secondary effects of dysfunction of the cystic fibrosis transmembrane conductance regulator protein. The CFTR protein is an epithelial ion channel adding to the regulation of absorption and secretion of salt and water in a variety of tissues, including the lung, sweat glands, pancreas, and gastrointestinal tract.4,5 Cystic fibrosis is due to mutations in CFTR that affect the quantity of the proteins that gets to the cell surface or that affect the function of CFTR stations at the cell surface area.6,7 The missense mutation G551D may be the most prevalent example of the latter.8 Approximately 4 to 5 percent of individuals with cystic fibrosis have the G551D mutation on at least one allele. Ivacaftor was proven to augment the chloride-transport activity of G551D-CFTR proteins in vitro.10 A small, randomized, controlled study of subjects with cystic fibrosis and at least one G551D-CFTR allele evaluated the safety profile of ivacaftor over the course of 14 to 28 times of treatment.