4-E, Sir Charles Tupper Medical Building, 5850 College Street, Halifax, Nova Scotia, Canada, B3H 4R2Research Topics:
- Ion channel structure and function
- 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.
- Negoda, A., Hogan, M.S., Cowley, E.A., and Linsdell, P. (2019). Contribution of the eighth transmembrane segment to the function of the CFTR chloride channel pore. Cellular and Molecular Life Sciences, DOI : 10.1007/s00018-019-03043-2.
- Linsdell, P. (2018). Cystic fibrosis transmembrane conductance regulator (CFTR): Making an ion channel out of an active transporter structure. Channels 12, 284-290.
- Li, M.-S., Cowley, E.A., El Hiani, Y., and Linsdell, P. (2018). Functional organization of cytoplasmic portals controlling access to the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel pore. Journal of Biological Chemistry 293, 5649-5658.
- Linsdell, P. (2017). Architecture and functional properties of the CFTR channel pore. Cellular and Molecular Life Sciences 74, 67-83.
- El Hiani, Y., and Linsdell, P. (2015). Functional architecture of the cytoplasmic entrance to the cystic fibrosis transmembrane conductance regulator chloride channel pore. Journal of Biological Chemistry 290, 15855-15865.
- 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.
- Site-directed mutagenesis
- Mammalian cell transfection
- Patch clamp electrophysiology (single channel and macroscopic current recording)