Nucleotide triphosphatase activity of the N-terminal nucleotide-binding domains of the multidrug resistance proteins P-glycoprotein and MRP1. (Q44090300)

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scientific article published in August 2002

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English	Nucleotide triphosphatase activity of the N-terminal nucleotide-binding domains of the multidrug resistance proteins P-glycoprotein and MRP1.	scientific article published in August 2002

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scholarly article

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11 November 2019

Nucleotide triphosphatase activity of the N-terminal nucleotide-binding domains of the multidrug resistance proteins P-glycoprotein and MRP1 (English)

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11 November 2019

multiple drug resistance

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Guillermo A. Altenberg

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11 November 2019

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Denise M Wilkes

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11 November 2019

Changsen Wang

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11 November 2019

Patricia C Aristimuño

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11 November 2019

Ariel F Castro

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1 August 2002

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11 November 2019

Biochemical and Biophysical Research Communications

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11 November 2019

296

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11 November 2019

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11 November 2019

388-394

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11 November 2019

Biochemical, cellular, and pharmacological aspects of the multidrug transporter

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Multidrug transporters from bacteria to man: similarities in structure and function

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Effects of phosphorylation of P-glycoprotein on multidrug resistance.

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Protein kinase C-mediated phosphorylation of the human multidrug resistance P-glycoprotein regulates cell volume-activated chloride channels

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Phosphorylation of P-glycoprotein by PKA and PKC modulates swelling-activated Cl- currents.

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Characterization of phosphorylation-defective mutants of human P-glycoprotein expressed in mammalian cells

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Protein kinase C-mediated phosphorylation does not regulate drug transport by the human multidrug resistance P-glycoprotein

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Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport

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Mechanism of inhibition of P-glycoprotein-mediated drug transport by protein kinase C blockers

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Phosphorylation site mutations in the human multidrug transporter modulate its drug-stimulated ATPase activity

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Expression and characterization of the NBD1-R domain region of CFTR: evidence for subunit-subunit interactions

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A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases

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Expression and characterization of the N- and C-terminal ATP-binding domains of MRP1.

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Methods to estimate the conformation of proteins and polypeptides from circular dichroism data

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Drug binding and nucleotide hydrolyzability are essential requirements in the vanadate-induced inhibition of the human P-glycoprotein ATPase.

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

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Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells

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ATPase activity of purified multidrug resistance-associated protein.

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ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells

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Recombinant N-terminal nucleotide-binding domain from mouse P-glycoprotein. Overexpression, purification, and role of cysteine 430

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Stimulation of ATPase activity of purified multidrug resistance-associated protein by nucleoside diphosphates

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Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1.

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Nonequivalent nucleotide trapping in the two nucleotide binding folds of the human multidrug resistance protein MRP1

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10.1016/S0006-291X(02)00878-1

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11 November 2019

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11 November 2019

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