These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

138 related articles for article (PubMed ID: 24766073)

  • 1. Role of protons in the pump cycle of KdpFABC investigated by time-resolved kinetic experiments.
    Damnjanovic B; Apell HJ
    Biochemistry; 2014 May; 53(19):3218-28. PubMed ID: 24766073
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase.
    Damnjanovic B; Weber A; Potschies M; Greie JC; Apell HJ
    Biochemistry; 2013 Aug; 52(33):5563-76. PubMed ID: 23930894
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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; 46(48):13920-8. PubMed ID: 17994765
    [TBL] [Abstract][Full Text] [Related]  

  • 4. The KdpFABC complex from Escherichia coli: a chimeric K+ transporter merging ion pumps with ion channels.
    Greie JC
    Eur J Cell Biol; 2011 Sep; 90(9):705-10. PubMed ID: 21684627
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 278(17):3041-53. PubMed ID: 21711450
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 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; 44(23):8260-6. PubMed ID: 15938615
    [TBL] [Abstract][Full Text] [Related]  

  • 7. KdpFABC reconstituted in Escherichia coli lipid vesicles: substrate dependence of the transport rate.
    Damnjanovic B; Apell HJ
    Biochemistry; 2014 Sep; 53(35):5674-82. PubMed ID: 25144826
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 45(36):11038-46. PubMed ID: 16953591
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 47(11):3564-75. PubMed ID: 18298081
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.
    Silberberg JM; Corey RA; Hielkema L; Stock C; Stansfeld PJ; Paulino C; Hänelt I
    Nat Commun; 2021 Aug; 12(1):5098. PubMed ID: 34429416
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Structural basis for potassium transport in prokaryotes by KdpFABC.
    Sweet ME; Larsen C; Zhang X; Schlame M; Pedersen BP; Stokes DL
    Proc Natl Acad Sci U S A; 2021 Jul; 118(29):. PubMed ID: 34272288
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The KdpFABC complex - K
    Pedersen BP; Stokes DL; Apell HJ
    Mol Membr Biol; 2019 Dec; 35(1):21-38. PubMed ID: 31259644
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Amino acid substitutions in putative selectivity filter regions III and IV in KdpA alter ion selectivity of the KdpFABC complex from Escherichia coli.
    Bertrand J; Altendorf K; Bramkamp M
    J Bacteriol; 2004 Aug; 186(16):5519-22. PubMed ID: 15292155
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Characterization of amino acid substitutions in KdpA, the K+-binding and -translocating subunit of the KdpFABC complex of Escherichia coli.
    van der Laan M; Gassel M; Altendorf K
    J Bacteriol; 2002 Oct; 184(19):5491-4. PubMed ID: 12218037
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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; 342(5):1547-58. PubMed ID: 15364580
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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; 166(3):295-302. PubMed ID: 19285138
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Serine phosphorylation regulates the P-type potassium pump KdpFABC.
    Sweet ME; Zhang X; Erdjument-Bromage H; Dubey V; Khandelia H; Neubert TA; Pedersen BP; Stokes DL
    Elife; 2020 Sep; 9():. PubMed ID: 32955430
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli.
    Bramkamp M; Altendorf K
    Biochemistry; 2004 Sep; 43(38):12289-96. PubMed ID: 15379567
    [TBL] [Abstract][Full Text] [Related]  

  • 19. The Kdp-ATPase of Escherichia coli mediates an ATP-dependent, K+-independent electrogenic partial reaction.
    Fendler K; Dröse S; Epstein W; Bamberg E; Altendorf K
    Biochemistry; 1999 Feb; 38(6):1850-6. PubMed ID: 10026265
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Crystal structure of the potassium-importing KdpFABC membrane complex.
    Huang CS; Pedersen BP; Stokes DL
    Nature; 2017 Jun; 546(7660):681-685. PubMed ID: 28636601
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.