B
B. de Kruijff
Researcher at Utrecht University
Publications - 204
Citations - 17134
B. de Kruijff is an academic researcher from Utrecht University. The author has contributed to research in topics: Bilayer & Vesicle. The author has an hindex of 71, co-authored 204 publications receiving 16788 citations. Previous affiliations of B. de Kruijff include ETH Zurich & Laboratory of Molecular Biology.
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Journal ArticleDOI
Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization.
TL;DR: In order to obtain more insight in the initial steps of the process of protein translocation across membranes, biophysical investigations were undertaken on the lipid specificity and structural consequences of penetration of the PhoE signal peptide into lipid model membranes and on the conformation of the signal peptides adopted upon interaction with the lipids.
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Protein-mediated transbilayer movement of lysophosphatidylcholine in glycophorin-containing vesicles
TL;DR: The transbilayer distribution of palmitoyl lysophosphatidylcholine in these vesicles is such that they have a significantly higher content of the lyso-compound in the inner monolayer when compared with vesicle without glycophorin.
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The interaction of adriamycin with cardiolipin in model and rat liver mitochondrial membranes
Klaas Nicolay,R.J.M. Timmers,Ellen C. Spoelstra,R. van der Neut,J.J. Fok,Y.M. Huigen,Arie J. Verkleij,B. de Kruijff +7 more
TL;DR: It is proposed that endogenous RNA present in mitochondria and mitoplasts is not accessible for adriamycin at low concentrations of the drug due to the presence of an intact lipid barrier, and the evidence for the potential importance of RNA as a target comes from experiments on outer membranes and microsomes.
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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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Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organization
TL;DR: In these fused structures freeze-fracture electron microscopy reveals the appearance of particles, which is accompanied by the induction of an isotropic component in 31P NMR, and the localization of the cardiotoxin molecule in these structures is discussed.