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Journal Abstract Search

252 related items for PubMed ID: 7642618

  • 1. P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site.
    Urbatsch IL, Sankaran B, Weber J, Senior AE.
    J Biol Chem; 1995 Aug 18; 270(33):19383-90. PubMed ID: 7642618
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  • 2. Both P-glycoprotein nucleotide-binding sites are catalytically active.
    Urbatsch IL, Sankaran B, Bhagat S, Senior AE.
    J Biol Chem; 1995 Nov 10; 270(45):26956-61. PubMed ID: 7592942
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  • 4. Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity.
    Julien M, Gros P.
    Biochemistry; 2000 Apr 18; 39(15):4559-68. PubMed ID: 10758006
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  • 6. Functionally similar vanadate-induced 8-azidoadenosine 5'-[alpha-(32)P]Diphosphate-trapped transition state intermediates of human P-glycoprotin are generated in the absence and presence of ATP hydrolysis.
    Sauna ZE, Smith MM, Muller M, Ambudkar SV.
    J Biol Chem; 2001 Jun 15; 276(24):21199-208. PubMed ID: 11287418
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  • 8. Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotide at both sites.
    Urbatsch IL, Beaudet L, Carrier I, Gros P.
    Biochemistry; 1998 Mar 31; 37(13):4592-602. PubMed ID: 9521779
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  • 11. Drug binding and nucleotide hydrolyzability are essential requirements in the vanadate-induced inhibition of the human P-glycoprotein ATPase.
    Rao US.
    Biochemistry; 1998 Oct 20; 37(42):14981-8. PubMed ID: 9778376
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  • 13. Catalytic mechanism of P-glycoprotein.
    Senior AE.
    Acta Physiol Scand Suppl; 1998 Aug 20; 643():213-8. PubMed ID: 9789563
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  • 17. 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.
    Sauna ZE, Ambudkar SV.
    J Biol Chem; 2001 Apr 13; 276(15):11653-61. PubMed ID: 11154703
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