These mutations cause a wide variety of molecular defects ranging from the disruption of transcription and splicing of the CFTR transcript to functional defects in the channel protein.1 However, most CF mutations enhance CFTR misfolding, which promotes aberrant interactions with endogenous molecular chaperones that trigger its retention and premature degradation within the endoplasmic reticulum (ER).2 The folding defects caused by certain CF variants can be suppressed by small molecule “correctors” that bind and stabilize the CFTR protein. The gene discussed is CFTR; the disease is cystic fibrosis.