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Volumn 53, Issue 4, 2014, Pages 746-754

Molecular mechanism of Na+,K+-ATPase malfunction in mutations characteristic of adrenal hypertension

Author keywords

[No Author keywords available]

Indexed keywords

ION GRADIENTS; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR MECHANISM; PHYSIOLOGICAL CONDITION; SODIUM BINDING; STRUCTURAL BEHAVIORS; TRANSMEMBRANE HELICES; WATER-PATHWAY;

EID: 84893641602     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401425g     Document Type: Article
Times cited : (24)

References (53)
  • 1
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • Skou, J. C. (1957) The influence of some cations on an adenosine triphosphatase from peripheral nerves Biochim. Biophys. Acta 23, 439-446
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 439-446
    • Skou, J.C.1
  • 2
    • 0036196950 scopus 로고    scopus 로고
    • A hundred years of sodium pumping
    • DOI 10.1146/annurev.physiol.64.081501.130716
    • Glynn, I. M. (2002) A hundred years of sodium pumping Annu. Rev. Physiol. 64, 1-18 (Pubitemid 34259223)
    • (2002) Annual Review of Physiology , vol.64 , pp. 1-18
    • Glynn, I.M.1
  • 4
    • 0000760057 scopus 로고
    • The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane
    • Post, R. L. and Jolly, P. C. (1957) The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane Biochim. Biophys. Acta 25, 118-128
    • (1957) Biochim. Biophys. Acta , vol.25 , pp. 118-128
    • Post, R.L.1    Jolly, P.C.2
  • 5
    • 84893648590 scopus 로고    scopus 로고
    • Sodium/potassium homeostasis in the cell
    • Clausen, M. J. and Poulsen, H. (2013) Sodium/potassium homeostasis in the cell Met. Ions Life Sci. 12, 41-67
    • (2013) Met. Ions Life Sci. , vol.12 , pp. 41-67
    • Clausen, M.J.1    Poulsen, H.2
  • 6
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post, R. L., Hegyvary, C., and Kume, S. (1972) Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase J. Biol. Chem. 247, 6530-6540
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 7
    • 0000770960 scopus 로고
    • Biochemical aspects of active transport
    • Albers, R. W. (1967) Biochemical aspects of active transport Annu. Rev. Biochem. 36, 727-756
    • (1967) Annu. Rev. Biochem. , vol.36 , pp. 727-756
    • Albers, R.W.1
  • 9
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 Å resolution
    • Shinoda, T., Ogawa, H., Cornelius, F., and Toyoshima, C. (2009) Crystal structure of the sodium-potassium pump at 2.4 Å resolution Nature 459, 446-450
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 20
    • 55549091439 scopus 로고    scopus 로고
    • An ion gating mechanism of gastric H,K-ATPase based on molecular dynamics simulations
    • Law, R. J., Munson, K., Sachs, G., and Lightstone, F. C. (2008) An ion gating mechanism of gastric H,K-ATPase based on molecular dynamics simulations Biophys. J. 95, 2739-2749
    • (2008) Biophys. J. , vol.95 , pp. 2739-2749
    • Law, R.J.1    Munson, K.2    Sachs, G.3    Lightstone, F.C.4
  • 23
  • 24
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., Van Der Spoel, D., and Lindahl, E. (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 27
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell, A. D., Jr., Feig, M., and Brooks, C. L., 3rd (2004) Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations J. Comput. Chem. 25, 1400-1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 29
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models
    • Bjelkmar, P. r., Larsson, P., Cuendet, M. A., Hess, B., and Lindahl, E. (2010) Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models J. Chem. Theory Comput. 6, 459-466
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 459-466
    • Bjelkmar, P.R.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 31
    • 84869067020 scopus 로고    scopus 로고
    • Molecular dynamics simulations of phosphatidylcholine membranes: A comparative force field study
    • Piggot, T. J., Piñeiro, á., and Khalid, S. (2012) Molecular dynamics simulations of phosphatidylcholine membranes: A comparative force field study J. Chem. Theory Comput. 8, 4593-4609
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 4593-4609
    • Piggot, T.J.1    Piñeiro, Á.2    Khalid, S.3
  • 33
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 36
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • Nose, S. (1984) A unified formulation of the constant temperature molecular dynamics methods J. Chem. Phys. 81, 511-519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nose, S.1
  • 37
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. (1985) Canonical dynamics: Equilibrium phase-space distributions Phys. Rev. A 31, 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 38
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: a new molecular dynamics method
    • DOI 10.1063/1.328693
    • Parrinello, M. and Rahman, A. (1981) Polymorphic transitions in single crystals: A new molecular dynamics method J. Appl. Phys. 52, 7182-7190 (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 39
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nosé, S. and Klein, M. L. (1983) Constant pressure molecular dynamics for molecular systems Mol. Phys. 50, 1055-1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nosé, S.1    Klein, M.L.2
  • 40
    • 68149155963 scopus 로고    scopus 로고
    • Self-guided Langevin dynamics study of regulatory interactions in NtrC
    • Damjanovic, A., Garcia-Moreno, E. B., and Brooks, B. R. (2009) Self-guided Langevin dynamics study of regulatory interactions in NtrC Proteins 76, 1007-1019
    • (2009) Proteins , vol.76 , pp. 1007-1019
    • Damjanovic, A.1    Garcia-Moreno, E.B.2    Brooks, B.R.3
  • 41
    • 77954256616 scopus 로고    scopus 로고
    • G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • Wolf, M. G., Hoefling, M., Aponte-Santamaria, C., Grubmuller, H., and Groenhof, G. (2010) g-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation J. Comput. Chem. 31, 2169-2174
    • (2010) J. Comput. Chem. , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaria, C.3    Grubmuller, H.4    Groenhof, G.5
  • 45
    • 84944648082 scopus 로고
    • Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides
    • Shannon, R. (1976) Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides Acta Crystallogr., Sect. A 32, 751-767
    • (1976) Acta Crystallogr., Sect. A , vol.32 , pp. 751-767
    • Shannon, R.1
  • 46
    • 78649876136 scopus 로고    scopus 로고
    • Selectivity of externally facing ion-binding sites in the Na/K pump to alkali metals and organic cations
    • Ratheal, I. M., Virgin, G. K., Yu, H., Roux, B., Gatto, C., and Artigas, P. (2010) Selectivity of externally facing ion-binding sites in the Na/K pump to alkali metals and organic cations Proc. Natl. Acad. Sci. U.S.A. 107, 18718-18723
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 18718-18723
    • Ratheal, I.M.1    Virgin, G.K.2    Yu, H.3    Roux, B.4    Gatto, C.5    Artigas, P.6


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