Mechanism-based corrector combination restores ΔF508-CFTR folding and function

Compounds that restore function to the cystic fibrosis–linked ΔF508 allele of CFTR can be classified on the basis of three corrector functions, representing different targets within the five domains of the channel protein. Combinations of individual compounds in the three classes can restore conside...

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Veröffentlicht in:	Nature chemical biology 2013-07, Vol.9 (7), p.444-454
Hauptverfasser:	Okiyoneda, Tsukasa, Veit, Guido, Dekkers, Johanna F, Bagdany, Miklos, Soya, Naoto, Xu, Haijin, Roldan, Ariel, Verkman, Alan S, Kurth, Mark, Simon, Agnes, Hegedus, Tamas, Beekman, Jeffrey M, Lukacs, Gergely L
Format:	Artikel
Sprache:	eng
Schlagworte:	631/92/269 Aminopyridines - pharmacology Animals Benzodioxoles - pharmacology Binding Sites Biochemical Engineering Biochemistry Bioorganic Chemistry Bronchi - cytology Cell Biology Cell Membrane - metabolism Chemistry Chemistry/Food Science Cricetinae Cystic fibrosis Cystic Fibrosis - genetics Cystic Fibrosis - therapy Cystic Fibrosis Transmembrane Conductance Regulator - chemistry Cystic Fibrosis Transmembrane Conductance Regulator - physiology Defects Drug development Endoplasmic Reticulum - metabolism Epithelial cells Epithelial Cells - metabolism Epithelium Folding Genetic suppression Glycosylation Humans Interfaces Membranes Missense mutation Mutation Nucleotides Nucleotides - chemistry Organoids Protein Folding Protein Structure, Tertiary Recombinant Proteins - chemistry Recovery of function Stability
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