Karin Pleban
University of Vienna
8 Papers
114 Citations
Karin Pleban is an academic researcher from University of Vienna. The author has contributed to research in topics: P-glycoprotein & Lipophilicity. The author has an hindex of 8, co-authored 8 publications. Previous affiliations of Karin Pleban include Medical University of Vienna.
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Papers
P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: a combined photoaffinity labeling-protein homology modeling approach.
Karin Pleban,Stephan Kopp,Edina Csaszar,Michael Peer,Thomas Hrebicek,Andreas Rizzi,Gerhard F. Ecker,Peter Chiba +7 more
TL;DR: A set of propafenonetype substrate photoaffinity ligands has been used in this study in conjunction with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to define the substrate binding domain(s) of P-gp in more detail, and binding at domain interfaces may be a general feature of polyspecific drug efflux pumps.
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Inhibitors of p-glycoprotein--lead identification and optimisation.
Karin Pleban,Gerhard F. Ecker +1 more
TL;DR: This review highlights concepts for identification and optimization of new inhibitors of P-glycoprotein, which represents a promising approach for treatment of multidrug resistant tumours.
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Targeting drug-efflux pumps -- a pharmacoinformatic approach.
TL;DR: On LmrA, a bacterial homologue of P-gp, the authors were able to identify distinct regions on transmembrane helices 3, 5 and 6 which show significant changes in the labeling pattern during different steps of the catalytic cycle.
A three-dimensional model for the substrate binding domain of the multidrug ATP binding cassette transporter LmrA.
Gerhard F. Ecker,Karin Pleban,Stephan Kopp,Edina Csaszar,Gerrit J. Poelarends,M Putman,Dominik Kaiser,Wil N. Konings,Peter Chiba +8 more
TL;DR: Inverse changes in the reactivity of TM segments 5 and 6 suggest that substrate binding and release involves a repositioning of these helices during the catalytic cycle, suggesting substrate-binding at the monomer/monomer interface.
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Homology model of the multidrug transporter LmrA from Lactococcus lactis.
Karin Pleban,Antonio Macchiarulo,Gabriele Costantino,Roberto Pellicciari,Peter Chiba,Gerhard F. Ecker +5 more
TL;DR: Two homology models are built from the dimeric crystal structure of Vc-MsbA, with NBD:NBD interfaces reflecting the nonenergized and energized state, respectively, suggesting binding of substrates at the TMD:TMD interface involving helix 3 of one monomer and helices 5 and 6 of the other monomer.
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