Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator.

@article{Pind1994ParticipationOT,
  title={Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator.},
  author={Steven Pind and John R. Riordan and David B. Williams},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 17},
  pages={12784-8}
}
Deletion of phenylalanine at position 508 (delta F508) in the first nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator (CFTR) is the most common mutation in patients with cystic fibrosis. Although retaining functional Cl- channel activity, this mutant is recognized as abnormal by the cellular "quality control" machinery and is retained within the endoplasmic reticulum (ER). We have used human epithelial cells and recombinant Chinese hamster ovary cells to… CONTINUE READING

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