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Journal Abstract Search

104 related items for PubMed ID: 9789551

  • 1. Structural changes associated with the coupling of ATP hydrolysis and cation transport by the Na pump.
    Kaplan JH, Gatto C, Holden JP, Thornewell SJ.
    Acta Physiol Scand Suppl; 1998 Aug; 643():99-105. PubMed ID: 9789551
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  • 3. Conformational changes in the alpha-subunit, and cation transport by Na+, K+-ATPase.
    Jørgensen PL.
    Ciba Found Symp; 1983 Aug; 95():253-72. PubMed ID: 6303721
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  • 4. Na+,K+-ATPase: structure, mechanism, and regulation.
    Lopina OD.
    Membr Cell Biol; 2000 Aug; 13(6):721-44. PubMed ID: 10963432
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  • 5. The dynamics of the cell membrane coupling of the reaction of the Na, K-ATPase with ATP to the reaction with the cations.
    Skou JC.
    Tokai J Exp Clin Med; 1982 Aug; 7 Suppl():1-6. PubMed ID: 6310820
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  • 6. Chemical modification with dihydro-4,4'-diisothiocyanostilbene-2,2'-disulfonate reveals the distance between K480 and K501 in the ATP-binding domain of the Na,K-ATPase.
    Gatto C, Lutsenko S, Kaplan JH.
    Arch Biochem Biophys; 1997 Apr 01; 340(1):90-100. PubMed ID: 9126281
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  • 7. Structure-function relationships based on ATP binding and cation occlusion at equilibrium in Na,K-ATPase.
    Jorgensen PL, Nielsen JM, Rasmussen JH, Pedersen PA.
    Acta Physiol Scand Suppl; 1998 Aug 01; 643():79-87. PubMed ID: 9789549
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  • 8. Residues within transmembrane domains 4 and 6 of the Na,K-ATPase alpha subunit are important for Na+ selectivity.
    Sánchez G, Blanco G.
    Biochemistry; 2004 Jul 20; 43(28):9061-74. PubMed ID: 15248763
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  • 9. Crystal structure of the sodium-potassium pump.
    Morth JP, Pedersen BP, Toustrup-Jensen MS, Sørensen TL, Petersen J, Andersen JP, Vilsen B, Nissen P.
    Nature; 2007 Dec 13; 450(7172):1043-9. PubMed ID: 18075585
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  • 10. Identification of the cation binding domain of Na/K-ATPase.
    Karlish SJ, Goldshleger R, Tal DM, Capasso JM, Hoving S, Stein WD.
    Acta Physiol Scand Suppl; 1992 Dec 13; 607():69-76. PubMed ID: 1333162
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  • 11. Structure and mechanism of Na,K-ATPase: functional sites and their interactions.
    Jorgensen PL, Hakansson KO, Karlish SJ.
    Annu Rev Physiol; 2003 Dec 13; 65():817-49. PubMed ID: 12524462
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  • 13. Evidence for tryptophan residues in the cation transport path of the Na(+),K(+)-ATPase.
    Yudowski GA, Bar Shimon M, Tal DM, González-Lebrero RM, Rossi RC, Garrahan PJ, Beaugé LA, Karlish SJ.
    Biochemistry; 2003 Sep 02; 42(34):10212-22. PubMed ID: 12939149
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  • 14. Glutamic acid 472 and lysine 480 of the sodium pump alpha 1 subunit are essential for activity. Their conservation in pyrophosphatases suggests their involvement in recognition of ATP phosphates.
    Scheiner-Bobis G, Schreiber S.
    Biochemistry; 1999 Jul 20; 38(29):9198-208. PubMed ID: 10413494
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  • 15. D443 of the N domain of Na+,K+-ATPase interacts with the ATP-Mg2+ complex, possibly via a second Mg2+ ion.
    Strugatsky D, Gottschalk KE, Goldshleger R, Karlish SJ.
    Biochemistry; 2005 Dec 13; 44(49):15961-9. PubMed ID: 16331955
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  • 16. The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.
    Lánský Z, Kubala M, Ettrich R, Kutý M, Plásek J, Teisinger J, Schoner W, Amler E.
    Biochemistry; 2004 Jul 06; 43(26):8303-11. PubMed ID: 15222743
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  • 18. Nucleotide-binding kinetics of Na,K-ATPase: cation dependence.
    Fedosova NU, Esmann M.
    Biochemistry; 2004 Apr 13; 43(14):4212-8. PubMed ID: 15065865
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  • 19. New evidence for ATP binding induced catalytic subunit interactions in pig kidney Na/K-ATPase.
    Tanoue K, Kaya S, Hayashi Y, Abe K, Imagawa T, Taniguchi K, Sakaguchi K.
    J Biochem; 2006 Oct 13; 140(4):599-607. PubMed ID: 16987945
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  • 20. E2P phosphoforms of Na,K-ATPase. II. Interaction of substrate and cation-binding sites in Pi phosphorylation of Na,K-ATPase.
    Cornelius F, Fedosova NU, Klodos I.
    Biochemistry; 1998 Nov 24; 37(47):16686-96. PubMed ID: 9843437
    [Abstract] [Full Text] [Related]

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