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540 related items for PubMed ID: 16953591

  • 1. 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
    [Abstract] [Full Text] [Related]

  • 2. The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone.
    Irzik K, Pfrötzschner J, Goss T, Ahnert F, Haupt M, Greie JC.
    FEBS J; 2011 Sep 12; 278(17):3041-53. PubMed ID: 21711450
    [Abstract] [Full Text] [Related]

  • 3. Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli.
    Bramkamp M, Altendorf K.
    Biochemistry; 2004 Sep 28; 43(38):12289-96. PubMed ID: 15379567
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  • 4. Single amino acid substitution in the putative transmembrane helix V in KdpB of the KdpFABC complex of Escherichia coli uncouples ATPase activity and ion transport.
    Bramkamp M, Altendorf K.
    Biochemistry; 2005 Jun 14; 44(23):8260-6. PubMed ID: 15938615
    [Abstract] [Full Text] [Related]

  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. 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
    [Abstract] [Full Text] [Related]

  • 7. Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis.
    Heitkamp T, Böttcher B, Greie JC.
    J Struct Biol; 2009 Jun 20; 166(3):295-302. PubMed ID: 19285138
    [Abstract] [Full Text] [Related]

  • 8. 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
    [Abstract] [Full Text] [Related]

  • 9. 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
    [Abstract] [Full Text] [Related]

  • 10. K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer.
    Heitkamp T, Kalinowski R, Böttcher B, Börsch M, Altendorf K, Greie JC.
    Biochemistry; 2008 Mar 18; 47(11):3564-75. PubMed ID: 18298081
    [Abstract] [Full Text] [Related]

  • 11. Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review).
    Bramkamp M, Altendorf K, Greie JC.
    Mol Membr Biol; 2007 Mar 18; 24(5-6):375-86. PubMed ID: 17710642
    [Abstract] [Full Text] [Related]

  • 12. 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
    [Abstract] [Full Text] [Related]

  • 13. Probing the nucleotide-binding site of Escherichia coli succinyl-CoA synthetase.
    Joyce MA, Fraser ME, Brownie ER, James MN, Bridger WA, Wolodko WT.
    Biochemistry; 1999 Jun 01; 38(22):7273-83. PubMed ID: 10353839
    [Abstract] [Full Text] [Related]

  • 14. Analysis of KdpC of the K(+)-transporting KdpFABC complex of Escherichia coli.
    Gassel M, Altendorf K.
    Eur J Biochem; 2001 Mar 01; 268(6):1772-81. PubMed ID: 11248697
    [Abstract] [Full Text] [Related]

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  • 17. 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 01; 65(Pt 11):1181-6. PubMed ID: 19923713
    [Abstract] [Full Text] [Related]

  • 18. Differentiation of catalytic sites on Escherichia coli F1ATPase by laser photoactivated labeling with [3H]-2-Azido-ATP using the mutant beta Glu381Cys:epsilonSer108Cys to identify different beta subunits by their interactions with gamma and epsilon subunits.
    Grüber G, Capaldi RA.
    Biochemistry; 1996 Apr 02; 35(13):3875-9. PubMed ID: 8672416
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