Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein - Wikidata - wikimedia - TriplyDB

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

http://www.wikidata.org/entity/Q36589430

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Synergy in a medicinal plant: antimicrobial action of berberine potentiated by 5'-methoxyhydnocarpin, a multidrug pump inhibitor Providing a molecular mechanism for P-glycoprotein; why would I bother?Polymers influencing transportability profile of drug Molecular properties of bacterial multidrug transporters Antimonite regulation of the ATPase activity of ArsA, the catalytic subunit of the arsenical pump Predicting binding to p-glycoprotein by flexible receptor docking Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1)The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism Small molecules that dramatically alter multidrug resistance phenotype by modulating the substrate specificity of P-glycoprotein Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein. The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes.Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site.Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains.Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites.Design and synthesis of human ABCB1 (P-glycoprotein) inhibitors by peptide coupling of diverse chemical scaffolds on carboxyl and amino termini of (S)-valine-derived thiazole amino acid.Human immunodeficiency virus protease inhibitors serve as substrates for multidrug transporter proteins MDR1 and MRP1 but retain antiviral efficacy in cell lines expressing these transporters Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis.Studies of human MDR1-MDR2 chimeras demonstrate the functional exchangeability of a major transmembrane segment of the multidrug transporter and phosphatidylcholine flippase ABC drug transporters: hereditary polymorphisms and pharmacological impact in MDR1, MRP1 and MRP2.A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.Multidrug transporters in prokaryotic and eukaryotic cells: physiological functions and transport mechanisms.Exploring the P-glycoprotein binding cavity with polyoxyethylene alkyl ethers.Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters In silico screening for inhibitors of p-glycoprotein that target the nucleotide binding domains.Polymorphisms in the ABC drug transporter gene MDR1.Novel suicide ligands of tubulin arrest cancer cells in S-phase.Overcoming multidrug resistance in taxane chemotherapy.Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein.Functional polymorphisms of the human multidrug-resistance gene: multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo Snapshots of ligand entry, malleable binding and induced helical movement in P-glycoprotein.Structure and function of efflux pumps that confer resistance to drugs Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy.Toward eradicating HIV reservoirs in the brain: inhibiting P-glycoprotein at the blood-brain barrier with prodrug abacavir dimers P glycoprotein in human immunodeficiency virus type 1 infection and therapy.Stereoselective Modulation of P-Glycoprotein by Chiral Small Molecules.PK11195, a peripheral benzodiazepine receptor (pBR) ligand, broadly blocks drug efflux to chemosensitize leukemia and myeloma cells by a pBR-independent, direct transporter-modulating mechanism A review of selected anti-tumour therapeutic agents and reasons for multidrug resistance occurrence.The ABC transporters MDR1 and MRP2: multiple functions in disposition of xenobiotics and drug resistance.Revealing the fate of cell surface human P-glycoprotein (ABCB1): The lysosomal degradation pathway.Structure of a multidrug transporter.Rhodamine inhibitors of P-glycoprotein: an amide/thioamide "switch" for ATPase activity.

P2860

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P2860

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

http://www.wikidata.org/entity/Q36589430

description

1997 nî lūn-bûn

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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1997年论文

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1997年论文

@zh-cn

name

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@ast

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@en

type

label

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@ast

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@en

prefLabel

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@ast

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@en

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PNAS.94.20.10594

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein

@en

P2093

Ambudkar SV

http://www.w3.org/2001/XMLSchema#string

Dey S

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Gottesman MM

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Pastan I

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Ramachandra M

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P2860

Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease

ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells

Biochemistry of multidrug resistance mediated by the multidrug transporter

Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase.

The catalytic cycle of P-glycoprotein.

Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells.

Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance.

Partial purification and reconstitution of the human multidrug-resistance pump: characterization of the drug-stimulatable ATP hydrolysis.

Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system.

A single amino acid substitution strongly modulates the activity and substrate specificity of the mouse mdr1 and mdr3 drug efflux pumps.

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10594-10599

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10.1073/PNAS.94.20.10594

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9380680

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23414

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