- BSc (University College London)
- PhD (University of Leicester)
- PDF (University of Washington)
- PDF (McGill University)
Dr. Linsdell's lab is carrying out research to understand the structure and function of CFTR, the chloride channel that is mutated in cystic fibrosis. We are using electrophysiological recording techniques to study the detailed function of normal and mutant forms of the protein.
- Linsdell, P. (2014). Functional architecture of the CFTR chloride channel. Molecular Membrane Biology 31, 1-16.
- El Hiani, Y., and Linsdell, P. (2014). Metal bridges illuminate transmembrane domain movements during gating of the cystic fibrosis transmembrane conductance regulator chloride channel. Journal of Biological Chemistry 289, 28149-28159.
- Wang, W., and Linsdell, P. (2012). Alternating access to the transmembrane domain of the ATP-binding cassette protein cystic fibrosis transmembrane conductance regulator (ABCC7). Journal of Biological Chemistry 287, 10156-10165.
- El Hiani, Y., and Linsdell, P. (2012). Tuning of CFTR chloride channel function by location of positive charges within the pore. Biophysical Journal 103, 1719-1726.
- Zhou, J.-J., Li, M.-S., Qi, J., and Linsdell, P. (2010). Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore. Journal of General Physiology 135, 229-245.
- Site-directed mutagenesis
- Mammalian cell transfection
- Patch clamp electrophysiology (single channel and macroscopic current recording)