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Journal Abstract Search

300 related items for PubMed ID: 15379567

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  • 2. ATP binding properties of the soluble part of the KdpC subunit from the Escherichia coli K(+)-transporting KdpFABC P-type ATPase.
    Ahnert F, Schmid R, Altendorf K, Greie JC.
    Biochemistry; 2006 Sep 12; 45(36):11038-46. PubMed ID: 16953591
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  • 4. FITC binding site and p-nitrophenyl phosphatase activity of the Kdp-ATPase of Escherichia coli.
    Bramkamp M, Gassel M, Altendorf K.
    Biochemistry; 2004 Apr 20; 43(15):4559-67. PubMed ID: 15078102
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  • 6. Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes.
    Haupt M, Bramkamp M, Coles M, Altendorf K, Kessler H.
    J Mol Biol; 2004 Oct 01; 342(5):1547-58. PubMed ID: 15364580
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  • 9. The conserved dipole in transmembrane helix 5 of KdpB in the Escherichia coli KdpFABC P-type ATPase is crucial for coupling and the electrogenic K+-translocation step.
    Becker D, Fendler K, Altendorf K, Greie JC.
    Biochemistry; 2007 Dec 04; 46(48):13920-8. PubMed ID: 17994765
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  • 12. The KdpFABC complex from Escherichia coli: a chimeric K+ transporter merging ion pumps with ion channels.
    Greie JC.
    Eur J Cell Biol; 2011 Sep 04; 90(9):705-10. PubMed ID: 21684627
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  • 16. The structure and function of heavy metal transport P1B-ATPases.
    Argüello JM, Eren E, González-Guerrero M.
    Biometals; 2007 Jun 04; 20(3-4):233-48. PubMed ID: 17219055
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  • 17. Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.
    Papanikolau Y, Papadovasilaki M, Ravelli RB, McCarthy AA, Cusack S, Economou A, Petratos K.
    J Mol Biol; 2007 Mar 09; 366(5):1545-57. PubMed ID: 17229438
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  • 18. The structure of Mg-ATPase nucleotide-binding domain at 1.6 A resolution reveals a unique ATP-binding motif.
    Håkansson KO.
    Acta Crystallogr D Biol Crystallogr; 2009 Nov 09; 65(Pt 11):1181-6. PubMed ID: 19923713
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  • 20. The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP.
    Okkeri J, Laakkonen L, Haltia T.
    Biochem J; 2004 Jan 01; 377(Pt 1):95-105. PubMed ID: 14510639
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