Detailed characterization of cysteine-less P-glycoprotein reveals subtle pharmacological differences in function from wild-type protein (Q28366017)

2

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L Soceneantu

3

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K J Linton

4

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M Gabriel

5

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C Martin

6

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J Woodhouse

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E Blott

8

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C F Higgins

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R Callaghan

British Journal of Pharmacology

10

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language of work or name

English

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publication date

December 2001

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published in

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volume

134

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issue

8

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page(s)

1609-18

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Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity

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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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Covalent inhibitors of P-glycoprotein ATPase activity

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Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exterior

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Communication between multiple drug binding sites on P-glycoprotein

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Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysis

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Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase

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