Keith Poole
University of British Columbia
9 Papers
168 Citations
Keith Poole is an academic researcher from University of British Columbia. The author has contributed to research in topics: Bacterial outer membrane & Membrane. The author has an hindex of 9, co-authored 9 publications.
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Papers
Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli.
TL;DR: Gentamicin, kanamycin, and polymyxin B increased E. coli outer membrane permeability to the hydrophobic fluorescent compound 1-N-phenyl-naphthylamine (NPN) and the peptidoglycan-degrading enzyme lysozyme and added addition of Mg2+ blocked these permeabilizing activities.
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Outer membrane protein P of Pseudomonas aeruginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes.
TL;DR: A new major outer membrane protein, P, was induced in Pseudomonas aeruginosa PAO1 upon growth in medium containing 0.2 mM or less inorganic phosphate and was found to be highly specific for anions.
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Secretion of alkaline phosphatase and phsopholipase C in Pseudomonas aeruginosa is specific and does not involve an increase in outer membrane permeability
Keith Poole,Robert E. W. Hancock +1 more
TL;DR: It is reported that secretion of the enzymes is indeed specific and does not involve increased outer membrane permeability, as well as the specificity of the release of alkaline phosphatase and phospholipase C.
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An anion-selective channel from the Pseudomonas aeruginosa outer membrane
TL;DR: The reconstitution of protein P from Pseudomonas aeruginosa outer membrane was reconstituted in lipid bilayer membranes from diphytanoylphosphatidylcholine resulted in the formation of anion-selective channels with a conductance at least 100-times more selective for anions than for cations as judged from zero-current membrane potentials.
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Modification of the conductance, selectivity and concentration-dependent saturation of Pseudomonas aeruginosa protein P channels by chemical acetylation.
TL;DR: Data suggested that the basis of anion selectivity for native protein P channels is fixed amino groups, and could demonstrate a 2.5-fold decrease in single-channel conductance between pH 7 and pH 9, between which pH values the epsilon-amino groups of amino acids would start to become deprotonated.
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