A
Annemieke Kuil
Researcher at Netherlands Cancer Institute
Publications - 10
Citations - 1970
Annemieke Kuil is an academic researcher from Netherlands Cancer Institute. The author has contributed to research in topics: Multidrug resistance-associated protein 2 & Enterohepatic circulation. The author has an hindex of 10, co-authored 10 publications receiving 1891 citations.
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The human multidrug resistance protein MRP4 functions as a prostaglandin efflux transporter and is inhibited by nonsteroidal antiinflammatory drugs.
Glen Reid,Pieter Roeland Wielinga,Noam Zelcer,Ingrid van der Heijden,Annemieke Kuil,Marcel de Haas,Jan Wijnholds,Piet Borst +7 more
TL;DR: Investigation of the interaction between prostaglandins and members of the ATP-binding cassette (ABC) transporter ABCC [multidrug resistance protein (MRP)] family of membrane export pumps suggests that MRP4 can release prostaglandsins from cells, and that some nonsteroidal antiinflammatory drugs might also act by inhibiting this release.
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Steroid and bile acid conjugates are substrates of human multidrug-resistance protein (MRP) 4 (ATP-binding cassette C4)
Noam Zelcer,Glen Reid,Peter R. Wielinga,Annemieke Kuil,Ingrid van der Heijden,John D. Schuetz,Piet Borst +6 more
TL;DR: A physiological role for MRP1 and MRP4 in DHEAS transport and an involvement of MRp4 in transport of conjugated steroids and bile acids are suggested.
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Mice lacking multidrug resistance protein 3 show altered morphine pharmacokinetics and morphine-6-glucuronide antinociception
Noam Zelcer,Koen van de Wetering,Michel J.X. Hillebrand,Elise Sarton,Annemieke Kuil,Peter R. Wielinga,Thomas R. Tephly,Albert Dahan,Jos H. Beijnen,Piet Borst +9 more
TL;DR: Using morphine as a model aglycone, it is demonstrated that multidrug resistance protein 3 (MRP3/ABCC3), a protein present in the basolateral membrane of polarized cells, transports morphine-3-glucuronide (M3G) and morphine-6-glUCuronide in vitro.
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Evidence for Two Interacting Ligand Binding Sites in Human Multidrug Resistance Protein 2 (ATP Binding Cassette C2)
Noam Zelcer,Maarten T. Huisman,Glen Reid,Peter R. Wielinga,Pauline Breedveld,Annemieke Kuil,Puck Knipscheer,Jan H.M. Schellens,Alfred H. Schinkel,Piet Borst +9 more
TL;DR: It is proposed that MRP2 contains two similar but nonidentical ligand binding sites: one site from which substrate is transported and a second site that regulates the affinity of the transport site for the substrate.
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Thiopurine metabolism and identification of the thiopurine metabolites transported by MRP4 and MRP5 overexpressed in human embryonic kidney cells.
Pieter Roeland Wielinga,Glen Reid,E. E. Challa,I. van der Heijden,L. Van Deemter,M. De Haas,C. A. A. M. Mol,Annemieke Kuil,E. Groeneveld,John D. Schuetz,C. Brouwer,R.A. de Abreu,Jan Wijnholds,Jos H. Beijnen,Piet Borst +14 more
TL;DR: All major thiopurine monophosphates important in the efficacy of mercaptopurine treatment are transported by MRP4 and MRP5, although the substrate specificity of the two transporters differs in detail.