Corrector VX-809 promotes interactions between cytoplasmic loop one and the first nucleotide-binding domain of CFTR
Author:
Funder
Cystic Fibrosis Canada
Canadian Institutes for Health Research
Publisher
Elsevier BV
Subject
Pharmacology,Biochemistry
Reference45 articles.
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2. Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR);Loo;J. Biol. Chem.,2008
3. The ΔF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator;Chen;J. Biol. Chem.,2004
4. The cystic fibrosis V232D mutation inhibits CFTR maturation by disrupting a hydrophobic pocket rather than formation of aberrant interhelical hydrogen bonds;Loo;Biochem. Pharmacol.,2014
5. Revertants, low temperature, and correctors reveal the mechanism of F508del-CFTR rescue by VX-809 and suggest multiple agents for full correction;Farinha;Chem. Biol.,2013
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