Stephanie van Hoppe

165 The impact of OATPs on disposition and toxicity of antitumor drugs; insights from KO and humanized mice H. Yamaguchi, M. Kobayashi, M. Okada, T. Takeuchi, M. Unno, T. Abe, J. Goto, T. Hishinuma and N. Mano, Rapid screening of antineoplastic candidates for the human organic anion transporter OATP1B3 substrates using fluorescent probes, Cancer Lett 260 (2008), pp. 163-169. H. Zaher, H.E. Meyer zu Schwabedissen, R.G. Tirona, M.L. Cox, L.A. Obert, N. Agrawal, J. Palandra, J.L. Stock, R.B. Kim and J.A. Ware, Targeted disruption of murine organic anion-transporting polypeptide 1b2 (Oatp1b2/ Slco1b2) significantly alters disposition of prototypical drug substrates pravastatin and rifampin, Mol Pharmacol 74 (2008), pp. 320-329. N. Zelcer, M.T. Huisman, G. Reid, P. Wielinga, P. Breedveld, A. Kuil, P. Knipscheer, J.H. Schellens, A.H. Schinkel and P. Borst, Evidence for two interacting ligand binding sites in human multidrug resistance protein 2 (ATP binding cassette C2), J Biol Chem 278 (2003), pp. 23538-23544. S. Zhou, E. Chan, W. Duan, M. Huang andY.Z. Chen, Drug bioactivation, covalent binding to target proteins and toxicity relevance, Drug Metab Rev 37 (2005), pp. 41-213. E.I. Zimmerman, S. Hu, J.L. Roberts, A.A. Gibson, S.J. Orwick, L. Li, A. Sparreboom and S.D. Baker, Contribution of OATP1B1 and OATP1B3 to the disposition of sorafenib and sorafenib-glucuronide, Clin Cancer Res 19 (2013), pp. 1458-1466.