Canhui Li

Studies of the molecular basis for cystic fibrosis using purified reconstituted CFTR protein.

CFTR directly mediates nucleotide-regulated glutathione flux.

Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore.

Phosphorylation-induced conformational changes of cystic fibrosis transmembrane conductance regulator monitored by attenuated total reflection-Fourier transform IR spectroscopy and fluorescence spectroscopy.

Methods to study CFTR protein in vitro.

The patch-clamp and planar lipid bilayer techniques: powerful and versatile tools to investigate the CFTR Cl- channel.

Determination of CFTR chloride channel activity and pharmacology using radiotracer flux methods.

Evaluation of the membrane-spanning domain of ClC-2.

Nucleotides bind to the C-terminus of ClC-5.

The intact CFTR protein mediates ATPase rather than adenylate kinase activity.

Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system.

Evidence for a superoxide permeability pathway in endosomal membranes.

Direct interaction of a small-molecule modulator with G551D-CFTR, a cystic fibrosis-causing mutation associated with severe disease.

A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability.

Structural basis for alginate secretion across the bacterial outer membrane.

Synthesis and properties of molecular probes for the rescue site on mutant cystic fibrosis transmembrane conductance regulator.

Cystic fibrosis transmembrane conductance regulator (CFTR) potentiator VX-770 (ivacaftor) opens the defective channel gate of mutant CFTR in a phosphorylation-dependent but ATP-independent manner.

VX-809 and related corrector compounds exhibit secondary activity stabilizing active F508del-CFTR after its partial rescue to the cell surface.