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ATP-Binding Cassette Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-Throughput Screening.High-content screening of clinically tested anticancer drugs identifies novel inhibitors of human MRP1 (ABCC1).Biophysical Approaches Facilitate Computational Drug Discovery for ATP-Binding Cassette Proteins.Roles of the glycogen-binding domain and Snf4 in glucose inhibition of SNF1 protein kinase.Expression and function of human MRP1 (ABCC1) is dependent on amino acids in cytoplasmic loop 5 and its interface with nucleotide binding domain 2.Mutation of Glu521 or Glu535 in cytoplasmic loop 5 causes differential misfolding in multiple domains of multidrug and organic anion transporter MRP1 (ABCC1)Differential functional rescue of Lys(513) and Lys(516) processing mutants of MRP1 (ABCC1) by chemical chaperones reveals different domain-domain interactions of the transporter.Development of Novel Intramolecular FRET-Based ABC Transporter Biosensors to Identify New Substrates and ModulatorsCalcitriol and Calcipotriol Modulate Transport Activity of ABC Transporters and Exhibit Selective Cytotoxicity in MRP1-overexpressing CellsDoxorubicin as a fluorescent reporter identifies novel MRP1 (ABCC1) inhibitors missed by calcein-based high content screening of anticancer agents
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description
onderzoeker
@nl
researcher
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հետազոտող
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name
Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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type
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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Surtaj H. Iram
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15759935100
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0000-0002-0672-0936