Title : Analysis of amino acid residues in the predicted transmembrane pore influencing transport kinetics of the hepatic drug transporter organic anion transporting polypeptide 1B1 (OATP1B1).

Pub. Date : 2016 Nov

PMID : 27594653






3 Functional Relationships(s)
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1 Based on a computational analysis we established HEK293 cell lines overexpressing the mutant OATP1B1 proteins HEK-OATP1B1p.H54Q, -p.H54A, -p.Y169H and -p.Y169A and analyzed protein expression, localization and transport kinetics of the four OATP1B1 substrates bromosulfophthalein, estradiaol-17beta-glucuronide, taurocholate and pravastatin. Taurocholic Acid solute carrier organic anion transporter family member 1B1 Homo sapiens
2 Based on a computational analysis we established HEK293 cell lines overexpressing the mutant OATP1B1 proteins HEK-OATP1B1p.H54Q, -p.H54A, -p.Y169H and -p.Y169A and analyzed protein expression, localization and transport kinetics of the four OATP1B1 substrates bromosulfophthalein, estradiaol-17beta-glucuronide, taurocholate and pravastatin. Taurocholic Acid solute carrier organic anion transporter family member 1B1 Homo sapiens
3 Based on a computational analysis we established HEK293 cell lines overexpressing the mutant OATP1B1 proteins HEK-OATP1B1p.H54Q, -p.H54A, -p.Y169H and -p.Y169A and analyzed protein expression, localization and transport kinetics of the four OATP1B1 substrates bromosulfophthalein, estradiaol-17beta-glucuronide, taurocholate and pravastatin. Taurocholic Acid solute carrier organic anion transporter family member 1B1 Homo sapiens