P
Pieter R. Cullis
Researcher at University of British Columbia
Publications - 472
Citations - 55317
Pieter R. Cullis is an academic researcher from University of British Columbia. The author has contributed to research in topics: Liposome & Vesicle. The author has an hindex of 113, co-authored 458 publications receiving 49522 citations. Previous affiliations of Pieter R. Cullis include Utrecht University & Princeton University.
Papers
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Patent
Fusogenic lipsomes and methods for making and using same
Austin Bailey,Pieter R. Cullis +1 more
TL;DR: In this paper, a fusion-promoting effective amount of an ionizable lipid having a protonatable, cationic headgroup and an unsaturated acyl chain was provided, which can be used to control the delivery of a biologically active agent entrapped in the liposome.
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Transbilayer transport of phosphatidic acid in response to transmembrane pH gradients.
TL;DR: It is shown that the kinetics of PA transport are consistent with the transport of the uncharged (protonated) form and is associated with a large activation energy similar to that observed for phosphatidylglycerol.
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Cation-dependent segregation phenomena and phase behavior in model membrane systems containing phosphatidylserine: influence of cholesterol and acyl chain composition.
TL;DR: The results are discussed with regard to the reliability of 31P NMR phase identifications of phospholipid structure in model and biological membranes and demonstrate that in mixed lipid systems the influence of divalent cations on lipid distribution and structure can be exquisitely sensitive to details of the local lipid composition.
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The influence of poly(L-lysine) on phospholipid polymorphism. Evidence that electrostatic polypeptide-phospholipid interactions can modulate bilayer/non-bilayer transitions.
B. de Kruijff,Pieter R. Cullis +1 more
TL;DR: 31P-NMR shows that poly(L-lysine) binding to cardiolipin, phosphatidylserine or phosph atidylglycerol does not affect the macroscopic structure or local order (in the phosphate region) of the phospholipids.
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A non-covalent method of attaching antibodies to liposomes
TL;DR: It is shown that anti-rat-erythrocyte IgG or F(ab')2 complexed to liposomes via the streptavidin linker bind specifically to rat erythroCytes but not to human ery Throatcytes.