Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis
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Multiple Drug Transport Pathways through Human P-Glycoprotein.Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegansRefined structures of mouse P-glycoproteinPredicting P-glycoprotein-mediated drug transport based on support vector machine and three-dimensional crystal structure of P-glycoproteinDevelopment of novel rifampicin-derived P-glycoprotein activators/inducers. synthesis, in silico analysis and application in the RBE4 cell model, using paraquat as substrateMultiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1)Catalytic transitions in the human MDR1 P-glycoprotein drug binding sites.Transmembrane helices 1 and 6 of the human breast cancer resistance protein (BCRP/ABCG2): identification of polar residues important for drug transport.Mutational analysis of threonine 402 adjacent to the GXXXG dimerization motif in transmembrane segment 1 of ABCG2.In silico screening for inhibitors of p-glycoprotein that target the nucleotide binding domains.Structural characterization of two metastable ATP-bound states of P-glycoprotein.P-glycoprotein induction in Caco-2 cells by newly synthetized thioxanthones prevents paraquat cytotoxicity.The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely togetherHuman P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface.What can naturally occurring mutations tell us about Ca(v)1.x channel function?Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoproteinCysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.Benzbromarone stabilizes ΔF508 CFTR at the cell surface.Homology modeling and binding site assessment of the human P-glycoprotein.Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein.Transmembrane helix 12 plays a pivotal role in coupling energy provision and drug binding in ABCB1.Comparison of the inward- and outward-open homology models and ligand binding of human P-glycoprotein.A promiscuous conformational switch in the secondary multidrug transporter MdfA.Drug rescue distinguishes between different structural models of human P-glycoproteinSitamaquine overcomes ABC-mediated resistance to miltefosine and antimony in Leishmania.Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein.In silico model for P-glycoprotein substrate prediction: insights from molecular dynamics and in vitro studies.Substrate versus inhibitor dynamics of P-glycoprotein.Allosteric Role of Substrate Occupancy Toward the Alignment of P-glycoprotein Nucleotide Binding Domains
P2860
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P2860
Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis
description
2009 nî lūn-bûn
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name
Identification of residues in ...... rotein by arginine mutagenesis
@en
Identification of residues in ...... otein by arginine mutagenesis.
@nl
type
label
Identification of residues in ...... rotein by arginine mutagenesis
@en
Identification of residues in ...... otein by arginine mutagenesis.
@nl
prefLabel
Identification of residues in ...... rotein by arginine mutagenesis
@en
Identification of residues in ...... otein by arginine mutagenesis.
@nl
P2093
P2860
P356
P1476
Identification of residues in ...... rotein by arginine mutagenesis
@en
P2093
David M Clarke
M Claire Bartlett
P2860
P304
24074-24087
P356
10.1074/JBC.M109.023267
P407
P577
2009-07-06T00:00:00Z