Protein folding is a complex, error-prone process that often results in an irreparable protein
by-product. These by-products can be recognized by cellular quality control machineries …

Mutations in the gene coding for the cystic fibrosis transmembrane conductance regulator
(CFTR) epithelial anion channel cause cystic fibrosis (CF). The multidomain integral …

A complex involving Derlin-1 and p97 mediates the retrotranslocation and endoplasmic
reticulum (ER)-associated degradation of misfolded proteins in yeast and is used by certain …

Over one-third of all newly synthesized polypeptides in eukaryotes interact with or insert into
the membrane or the lumenal space of the ER (endoplasmic reticulum), an event that is …

Small heat shock proteins (sHsps) bind destabilized proteins during cell stress and disease,
but their physiological functions are less clear. We evaluated the impact of Hsp27, an sHsp …

The most common cause of cystic fibrosis (CF) is defective folding of a cystic fibrosis
transmembrane conductance regulator (CFTR) mutant lacking Phe 508 (ΔF508). The ΔF508 …

Cystic fibrosis (CF) is the most common lethal inherited disease among Caucasians in North
America and a significant portion of Europe. The disease arises from one of many mutations …

Most proteins in the secretory pathway are translated, folded, and subjected to quality
control at the endoplasmic reticulum (ER). These processes must be flexible enough to …

Secreted proteins that fail to achieve their native conformations, such as cystic fibrosis
transmembrane conductance regulator (CFTR) and particularly the ΔF508-CFTR variant can …

The role of the cystic fibrosis transmembrane conductance regulator (CFTR) as a cAMP-
dependent chloride channel on the apical membrane of epithelia is well established …