Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone

A recombinant peptide model of the first nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: Comparison of wild-type and ΔF508 mutant forms

(2010) Iwona Yike et al.   PROTEIN SCIENCE

Correctors promote folding of the CFTR in the endoplasmic reticulum

(2008) Tip W. Loo et al.   BIOCHEMICAL JOURNAL

Solubilizing Mutations Used to Crystallize One CFTR Domain Attenuate the Trafficking and Channel Defects Caused by the Major Cystic Fibrosis Mutation

(2008) Luísa S. Pissarra et al.   CHEMISTRY & BIOLOGY

Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia

(2008) Fei Sun et al.   FASEB JOURNAL

ΔF508 mutation increases conformational flexibility of CFTR protein

(2008) G. Wieczorek et al.   Journal of Cystic Fibrosis

Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function

(2008) A. W. R. Serohijos et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA