Allosteric transition, defined as conformational changes induced by ligand binding, is one of
the fundamental properties of proteins. Allostery has been observed and characterized in …

Defective epithelial ion transport is the hallmark of the life-limiting genetic disease cystic
fibrosis (CF). This abnormality is caused by mutations in the cystic fibrosis transmembrane …

The most common cystic fibrosis mutation, ΔF508 in nucleotide binding domain 1 (NBD1),
impairs cystic fibrosis transmembrane conductance regulator (CFTR)-coupled domain …

Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator
(CFTR). Newly developed “correctors” such as lumacaftor (VX-809) that improve CFTR …

The folding and misfolding mechanism of multidomain proteins remains poorly understood.
Although thermodynamic instability of the first nucleotide-binding domain (NBD1) of ΔF508 …

Most cystic fibrosis is caused by the deletion of a single amino acid (F508) from CFTR and
the resulting misfolding and destabilization of the protein. Compounds identified by high …

CFTR (cystic fibrosis transmembrane conductance regulator) is a member of the ATP-
binding cassette family of membrane proteins. Although almost all members of this family …

The ABCG2 protein has a key role in the transport of a wide range of structurally dissimilar
endo‐and xenobiotics in the human body, especially in the tissue barriers and the …

Relative contributions of folding kinetics versus protein quality control (QC) activity in the
partitioning of non-native proteins between life and death are not clear. Cystic fibrosis …

In the past decade much has been learned about how Cystic Fibrosis Transmembrane
Conductance Regulator (CFTR) folds and misfolds as the etiologic cause of cystic fibrosis …