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pro vyhledávání: '"Paul Linsdell"'
Publikováno v:
Cellular and Molecular Life Sciences. 80
The recent elucidation of atomistic structures of Cl− channel CFTR provides opportunities for understanding the molecular basis of cystic fibrosis. Despite having been activated through phosphorylation and provided with ATP ligands, several near-at
Autor:
Paul Linsdell
Publikováno v:
Cell Biochemistry and Biophysics. 79:863-871
The cystic fibrosis transmembrane conductance regulator (CFTR) Cl− channel shows only weak selectivity between different small monovalent anions, however, little is known about its ability to discriminate between monovalent and divalent anions. The
Electrostatic Tuning of Anion Attraction from the Cytoplasm to the Pore of the CFTR Chloride Channel
Publikováno v:
Cell Biochemistry and Biophysics. 78:15-22
Anions enter from the cytoplasm into the channel pore of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel not via a central pathway but via a single lateral portal or fenestration. High Cl- conductance is dependent on electr
Publikováno v:
The Journal of biological chemistry. 298(3)
Ion channels use charged amino-acid residues to attract oppositely charged permeant ions into the channel pore. In the cystic fibrosis transmembrane conductance regulator (CFTR) Cl
Publikováno v:
Cellular and Molecular Life Sciences.
Positively charged amino acid side-chains play important roles in anion binding and permeation through the CFTR chloride channel. One pore-lining lysine residue in particular (K95) has been shown to be indispensable for anion binding, conductance, an
Publikováno v:
Cellular and Molecular Life Sciences. 76:2411-2423
Our molecular understanding of the cystic fibrosis transmembrane conductance regulator (CFTR)-the chloride channel that is mutated in cystic fibrosis-has been greatly enhanced by a number of recent atomic-level structures of the protein in different
Publikováno v:
Cellular and molecular life sciences : CMLS. 78(12)
Positively charged amino acid side-chains play important roles in anion binding and permeation through the CFTR chloride channel. One pore-lining lysine residue in particular (K95) has been shown to be indispensable for anion binding, conductance, an
Autor:
Paul Linsdell
Publikováno v:
Biochimica et biophysica acta. Biomembranes. 1863(4)
Mutations at many sites within the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel pore region result in changes in chloride conductance. Although chloride binding in the pore – as well as interactions between concurrent
Publikováno v:
Cellular and Molecular Life Sciences. 75:3027-3038
Cystic fibrosis can be treated by potentiators, drugs that interact directly with the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel to increase its open probability. These substances likely target key conformational changes o
Autor:
Paul Linsdell
Publikováno v:
Channels
Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is a member of the ATP-binding cassette (ABC) family of membrane transport proteins, most members of which function as ATP-dependent pumps.