Photoaffinity labels for characterizing drug interaction sites of P-glycoprotein (Q41015261)

25 September 2017

title

Photoaffinity labels for characterizing drug interaction sites of P-glycoprotein (English)

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25 September 2017

Safa AR

1

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25 September 2017

language of work or name

English

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publication date

1 January 1998

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25 September 2017

published in

Methods in Enzymology

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25 September 2017

volume

292

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25 September 2017

page(s)

289-307

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The biochemistry of P-glycoprotein-mediated multidrug resistance

25 September 2017

cites work

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Radioiodination of a photoactivatable heterobifunctional reagent

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Photoaffinity labeling of P-glycoprotein in multidrug resistant cells with photoactive analogs of colchicine.

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N-(p-azido-3-[125I]iodophenethyl)spiperone binds to specific regions of P-glycoprotein and another multidrug binding protein, spiperophilin, in human neuroblastoma cells

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Photoaffinity substrates for P-glycoprotein

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Interaction of forskolin with the P-glycoprotein multidrug transporter

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Benzimidazoles, potent anti-mitotic drugs: substrates for the P-glycoprotein transporter in multidrug-resistant cells.

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P-glycoprotein binding and modulation of the multidrug-resistant phenotype by estramustine

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Studies on Ca2+ channel antagonists. 5-[(3,4-Dimethoxyphenethyl)methylamino]-2-(3,4-dimethoxyphenyl)-2- isopropylpentyl isothiocyanate, a chemoaffinity ligand derived from verapamil

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A Film Detection Method for Tritium-Labelled Proteins and Nucleic Acids in Polyacrylamide Gels

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Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies

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Photoaffinity labeling of P-glycoprotein in multidrug-resistant cells

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7 January 2021

The alpha 1-adrenergic photoaffinity probe [125I]arylazidoprazosin binds to a specific peptide of P-glycoprotein in multidrug-resistant cells

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7 January 2021

P-glycoprotein transports corticosterone and is photoaffinity-labeled by the steroid

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7 January 2021

P-glycoprotein possesses a 1,4-dihydropyridine-selective drug acceptor site which is alloserically coupled to a vinca-alkaloid-selective binding site

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Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site.

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Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein

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Megestrol acetate reverses multidrug resistance and interacts with P-glycoprotein

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7 January 2021

10.1016/S0076-6879(98)92023-7

Identifiers

DOI

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25 September 2017

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