Functional activation of the cystic fibrosis trafficking mutant delta F508-CFTR by overexpression.

@article{Cheng1995FunctionalAO,
  title={Functional activation of the cystic fibrosis trafficking mutant delta F508-CFTR by overexpression.},
  author={S. H. Cheng and S L Fang and Joseph Zabner and John Marshall and Susan Piraino and Susan C. Schiavi and Douglas M. Jefferson and Michael J. Welsh and A. E. Smith},
  journal={The American journal of physiology},
  year={1995},
  volume={268 4 Pt 1},
  pages={
          L615-24
        }
}
The most common mutation in the gene associated with cystic fibrosis (CF) causes deletion of phenylalanine at residue 508 (delta F508) of the gene product called CFTR. This mutation results in the synthesis of a variant CFTR protein that is defective in its ability to traffic to the plasma membrane. Because earlier studies showed delta F508-CFTR retains significant phosphorylation-regulated chloride (Cl-) channel activity, processes capable of restoring the mislocalized delta F508-CFTR to the… 
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