Fixing cystic fibrosis by correcting CFTR domain assembly.
For cystic fibrosis (CF) patients most therapies focus on alleviating the disease symptoms. Yet the cellular basis of the disease has been well studied; mutations in the CF gene can impair folding, secretion, cell surface stability, and/or function of the CFTR chloride channel. Correction of these basic defects has been a challenge, but indicates that a deeper understanding of the molecular and cellular mechanism of mutations is a prerequisite for developing more efficient therapies.
Department of Physiology, McGill University, Montréal, Quebec, Canada.
Tsukasa
T
Okiyoneda
Gergely L
GL
Lukacs
D018118:Chloride Channels / Q000235:genetics; D003550:Cystic Fibrosis / Q000235:genetics* / Q000628:therapy*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009154:Mutation; D017510:Protein Folding; D017434:Protein Structure, Tertiary
C505032:CFTR protein, human; D018118:Chloride Channels; D019005:Cystic Fibrosis Transmembrane Conductance Regulator