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Volumn 9, Issue 4, 2014, Pages

Microsecond molecular dynamics simulations of Mg2+- And K +- Bound E1 intermediate states of the calcium pump

Author keywords

[No Author keywords available]

Indexed keywords

MAGNESIUM ION; POTASSIUM ION; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; CALCIUM; MAGNESIUM; POTASSIUM;

EID: 84899715406     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0095979     Document Type: Article
Times cited : (33)

References (61)
  • 2
    • 84881112022 scopus 로고    scopus 로고
    • New crystal structures of PII-type ATPases: Excitement continues
    • Toyoshima C, Cornelius F (2013) New crystal structures of PII-type ATPases: excitement continues. Curr Opin Struct Biol 23: 507-514.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 507-514
    • Toyoshima, C.1    Cornelius, F.2
  • 3
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini M, Carafoli E (2009) Calcium pumps in health and disease. Physiol Rev 89: 1341-1378.
    • (2009) Physiol Rev , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 4
    • 79951681214 scopus 로고    scopus 로고
    • The sarcoplasmic Ca2+-ATPase: Design of a perfect chemi-osmotic pump
    • Moller JV, Olesen C, Winther AM, Nissen P (2010) The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump. Q Rev Biophys 43: 501-566.
    • (2010) Q Rev Biophys , vol.43 , pp. 501-566
    • Moller, J.V.1    Olesen, C.2    Winther, A.M.3    Nissen, P.4
  • 5
    • 0027266757 scopus 로고
    • 2+ pump in reconstituted proteoliposomes
    • Yu X, Carroll S, Rigaud JL, Inesi G (1993) H+ countertransport and electrogenicity of the sarcoplasmic reticulum Ca2+ pump in reconstituted proteoliposomes. Biophys J 64: 1232-1242. (Pubitemid 23143287)
    • (1993) Biophysical Journal , vol.64 , Issue.4 , pp. 1232-1242
    • Yu, X.1    Carroll, S.2    Rigaud, J.-L.3    Inesi, G.4
  • 6
    • 47249128944 scopus 로고    scopus 로고
    • Specificity of ligand binding to transport sites: Ca2+ binding to the Ca2+ transport ATPase and its dependence on H+ and Mg2 +
    • Zafar S, Hussain A, Liu Y, Lewis D, Inesi G (2008) Specificity of ligand binding to transport sites: Ca2+ binding to the Ca2+ transport ATPase and its dependence on H+ and Mg2 +. Arch Biochem Biophys 476: 87-94.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 87-94
    • Zafar, S.1    Hussain, A.2    Liu, Y.3    Lewis, D.4    Inesi, G.5
  • 7
    • 0026095279 scopus 로고
    • Interaction of potassium and magnesium with the high affinity calcium-binding sites of the sarcoplasmic reticulum calcium-ATPase
    • Moutin MJ, Dupont Y (1991) Interaction of potassium and magnesium with the high affinity calcium-binding sites of the sarcoplasmic reticulum calcium-ATPase. J Biol Chem 266: 5580-5586.
    • (1991) J Biol Chem , vol.266 , pp. 5580-5586
    • Moutin, M.J.1    Dupont, Y.2
  • 9
    • 38149066061 scopus 로고    scopus 로고
    • Conformational fluctuations of the Ca2+-ATPase in the native membrane environment. Effects of pH, temperature, catalytic substrates, and thapsigargin
    • Inesi G, Lewis D, Toyoshima C, Hirata A, de Meis L (2008) Conformational fluctuations of the Ca2+-ATPase in the native membrane environment. Effects of pH, temperature, catalytic substrates, and thapsigargin. J Biol Chem 283: 1189-1196.
    • (2008) J Biol Chem , vol.283 , pp. 1189-1196
    • Inesi, G.1    Lewis, D.2    Toyoshima, C.3    Hirata, A.4    De Meis, L.5
  • 10
    • 0020479307 scopus 로고
    • Direct fluorescence measurements of Mg2+ binding to sarcoplasmic reticulum ATPase
    • Guillain F, Gingold MP, Champeil P (1982) Direct fluorescence measurements of Mg2+ binding to sarcoplasmic reticulum ATPase. J Biol Chem 257: 7366-7371.
    • (1982) J Biol Chem , vol.257 , pp. 7366-7371
    • Guillain, F.1    Gingold, M.P.2    Champeil, P.3
  • 11
    • 0025891483 scopus 로고
    • Interaction of alkaline metal ions with Ca(2+)-binding sites of Ca(2+)-ATPase of sarcoplasmic reticulum: 23Na-NMR studies
    • Timonin IM, Dvoryantsev SN, Petrov VV, Ruuge EK, Levitsky DO (1991) Interaction of alkaline metal ions with Ca(2+)-binding sites of Ca(2+)-ATPase of sarcoplasmic reticulum: 23Na-NMR studies. Biochim Biophys Acta 1066: 43-53.
    • (1991) Biochim Biophys Acta , vol.1066 , pp. 43-53
    • Timonin, I.M.1    Dvoryantsev, S.N.2    Petrov, V.V.3    Ruuge, E.K.4    Levitsky, D.O.5
  • 12
    • 84866595055 scopus 로고    scopus 로고
    • Calcium binding and allosteric signaling mechanisms for the sarcoplasmic reticulum Ca(2)+ ATPase
    • Kekenes-Huskey PM, Metzger VT, Grant BJ, Andrew McCammon J (2012) Calcium binding and allosteric signaling mechanisms for the sarcoplasmic reticulum Ca(2)+ ATPase. Protein Sci 21: 1429-1443.
    • (2012) Protein Sci , vol.21 , pp. 1429-1443
    • Kekenes-Huskey, P.M.1    Metzger, V.T.2    Grant, B.J.3    Andrew McCammon, J.4
  • 13
    • 80055040431 scopus 로고    scopus 로고
    • Atomic-level characterization of the activation mechanism of SERCA by calcium
    • Espinoza-Fonseca LM, Thomas DD (2011) Atomic-level characterization of the activation mechanism of SERCA by calcium. PLoS One 6: e26936.
    • (2011) PLoS One , vol.6
    • Espinoza-Fonseca, L.M.1    Thomas, D.D.2
  • 14
    • 84865530106 scopus 로고    scopus 로고
    • Coarse-grained simulations of transitions in the E2-to-E1 conformations for Ca ATPase (SERCA) show entropy-enthalpy compensation
    • Nagarajan A, Andersen JP, Woolf TB (2012) Coarse-grained simulations of transitions in the E2-to-E1 conformations for Ca ATPase (SERCA) show entropy-enthalpy compensation. J Mol Biol 422: 575-593.
    • (2012) J Mol Biol , vol.422 , pp. 575-593
    • Nagarajan, A.1    Andersen, J.P.2    Woolf, T.B.3
  • 15
    • 84874957001 scopus 로고    scopus 로고
    • Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state
    • Toyoshima C, Iwasawa S, Ogawa H, Hirata A, Tsueda J, et al. (2013) Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state. Nature 495: 260-264.
    • (2013) Nature , vol.495 , pp. 260-264
    • Toyoshima, C.1    Iwasawa, S.2    Ogawa, H.3    Hirata, A.4    Tsueda, J.5
  • 16
    • 84874994481 scopus 로고    scopus 로고
    • The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm
    • Winther AM, Bublitz M, Karlsen JL, Moller JV, Hansen JB, et al. (2013) The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm. Nature 495: 265-269.
    • (2013) Nature , vol.495 , pp. 265-269
    • Winther, A.M.1    Bublitz, M.2    Karlsen, J.L.3    Moller, J.V.4    Hansen, J.B.5
  • 17
    • 0025983357 scopus 로고
    • Intracellular free Mg2+ concentration in skeletal muscle fibres of frog and crayfish
    • Gunzel D, Galler S (1991) Intracellular free Mg2+ concentration in skeletal muscle fibres of frog and crayfish. Pflugers Arch 417: 446-453.
    • (1991) Pflugers Arch , vol.417 , pp. 446-453
    • Gunzel, D.1    Galler, S.2
  • 18
    • 0025341473 scopus 로고
    • Intracellular free magnesium in frog skeletal muscle studied with a new type of magnesium-selective microelectrode: Interactions between magnesium and sodium in the regulation of [Mg]i
    • Blatter LA (1990) Intracellular free magnesium in frog skeletal muscle studied with a new type of magnesium-selective microelectrode: interactions between magnesium and sodium in the regulation of [Mg]i. Pflugers Arch 416: 238-246.
    • (1990) Pflugers Arch , vol.416 , pp. 238-246
    • Blatter, L.A.1
  • 19
    • 68349095078 scopus 로고    scopus 로고
    • High-yield heterologous expression of wild type and mutant Ca(2+) ATPase: Characterization of Ca(2+) binding sites by charge transfer
    • Liu Y, Pilankatta R, Lewis D, Inesi G, Tadini-Buoninsegni F, et al. (2009) High-yield heterologous expression of wild type and mutant Ca(2+) ATPase: Characterization of Ca(2+) binding sites by charge transfer. J Mol Biol 391: 858-871.
    • (2009) J Mol Biol , vol.391 , pp. 858-871
    • Liu, Y.1    Pilankatta, R.2    Lewis, D.3    Inesi, G.4    Tadini-Buoninsegni, F.5
  • 20
    • 0018795933 scopus 로고
    • Mg2 + and ATP effects on K+ activation of the Ca2+-transport ATPase of cardiac sarcoplasmic reticulum
    • Jones LR (1979) Mg2 + and ATP effects on K+ activation of the Ca2+-transport ATPase of cardiac sarcoplasmic reticulum. Biochimica Et Biophysica Acta 557: 230-242.
    • (1979) Biochimica et Biophysica Acta , vol.557 , pp. 230-242
    • Jones, L.R.1
  • 22
    • 0028833776 scopus 로고
    • Effects of K+ on the binding of Ca2+ to the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Lee AG, Baker K, Khan YM, East JM (1995) Effects of K+ on the binding of Ca2+ to the Ca(2+)-ATPase of sarcoplasmic reticulum. Biochem J 305 (Pt 1): 225-231.
    • (1995) Biochem J , vol.305 , Issue.PART 1 , pp. 225-231
    • Lee, A.G.1    Baker, K.2    Khan, Y.M.3    East, J.M.4
  • 25
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone phi, psi and side-chain chi(1) and chi(2) dihedral angles
    • Best RB, Zhu X, Shim J, Lopes PE, Mittal J, et al. (2012) Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone phi, psi and side-chain chi(1) and chi(2) dihedral angles. J Chem Theory Comput 8: 3257-3273.
    • (2012) J Chem Theory Comput , vol.8 , pp. 3257-3273
    • Best, R.B.1    Zhu, X.2    Shim, J.3    Lopes, P.E.4    Mittal, J.5
  • 26
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda JB, Venable RM, Freites JA, O'Connor JW, Tobias DJ, et al. (2010) Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types. J Phys Chem B 114: 7830-7843.
    • (2010) J Phys Chem B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1    Venable, R.M.2    Freites, J.A.3    O'Connor, J.W.4    Tobias, D.J.5
  • 27
    • 84859603569 scopus 로고    scopus 로고
    • Magnesium Ion-Water Coordination and Exchange in Biomolecular Simulations
    • Allnér O, Nilsson L, Villa A (2012) Magnesium Ion-Water Coordination and Exchange in Biomolecular Simulations. J Chem Theory Comput 8: 1493-1502.
    • (2012) J Chem Theory Comput , vol.8 , pp. 1493-1502
    • Allnér, O.1    Nilsson, L.2    Villa, A.3
  • 29
    • 0343005873 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of a Polyalanine Octapeptide under Ewald Boundary Conditions: Influence of Artificial Periodicity on Peptide Conformation
    • Weber W, Hünenberger PH, McCammon JA (2000) Molecular Dynamics Simulations of a Polyalanine Octapeptide under Ewald Boundary Conditions: Influence of Artificial Periodicity on Peptide Conformation. J Phys Chem B 104: 3668-3675.
    • (2000) J Phys Chem B , vol.104 , pp. 3668-3675
    • Weber, W.1    Hünenberger, P.H.2    McCammon, J.A.3
  • 30
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N•log(N) method for Ewald sums in large systems
    • Darden T, York D, 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
  • 31
  • 32
    • 33744502092 scopus 로고    scopus 로고
    • Small revisions to predicted distances around metal sites in proteins
    • Harding MM (2006) Small revisions to predicted distances around metal sites in proteins. Acta Crystallogr D Biol Crystallogr 62: 678-682.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 678-682
    • Harding, M.M.1
  • 33
    • 0035875164 scopus 로고    scopus 로고
    • What the structure of a calcium pump tells us about its mechanism
    • DOI 10.1042/0264-6021:3560665
    • Lee AG, East JM (2001) What the structure of a calcium pump tells us about its mechanism. Biochem J 356: 665-683. (Pubitemid 32588440)
    • (2001) Biochemical Journal , vol.356 , Issue.3 , pp. 665-683
    • Lee, A.G.1    East, J.M.2
  • 34
    • 69949142492 scopus 로고    scopus 로고
    • Molecular dynamics simulation exploration of cooperative migration mechanism of calcium ions in sarcoplasmic reticulum Ca2+-ATPase
    • Huang Y, Li H, Bu Y (2009) Molecular dynamics simulation exploration of cooperative migration mechanism of calcium ions in sarcoplasmic reticulum Ca2+-ATPase. J Comput Chem 30: 2136-2145.
    • (2009) J Comput Chem , vol.30 , pp. 2136-2145
    • Huang, Y.1    Li, H.2    Bu, Y.3
  • 35
    • 3843136264 scopus 로고    scopus 로고
    • 2+-ATPase phosphoenzyme intermediate
    • DOI 10.1074/jbc.M403211200
    • Inesi G, Ma H, Lewis D, Xu C (2004) Ca2+ occlusion and gating function of Glu309 in the ADP-fluoroaluminate analog of the Ca2+-ATPase phosphoenzyme intermediate. J Biol Chem 279: 31629-31637. (Pubitemid 39037833)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31629-31637
    • Inesi, G.1    Ma, H.2    Lewis, D.3    Xu, C.4
  • 36
    • 0028176742 scopus 로고
    • Amino acids Asn796 and Thr799 of the Ca(2+)-ATPase of sarcoplasmic reticulum bind Ca2+ at different sites
    • Andersen JP, Vilsen B (1994) Amino acids Asn796 and Thr799 of the Ca(2+)-ATPase of sarcoplasmic reticulum bind Ca2+ at different sites. J Biol Chem 269: 15931-15936.
    • (1994) J Biol Chem , vol.269 , pp. 15931-15936
    • Andersen, J.P.1    Vilsen, B.2
  • 37
    • 0027008485 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • Vilsen B, Andersen JP (1992) CrATP-induced Ca2+ occlusion in mutants of the Ca(2+)-ATPase of sarcoplasmic reticulum. J Biol Chem 267: 25739-25743. (Pubitemid 23013970)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.36 , pp. 25739-25743
    • Vilsen, B.1    Andersen, J.P.2
  • 38
    • 0026672665 scopus 로고
    • Functional consequences of alterations to Glu309, Glu771, and Asp800 in the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Andersen JP, Vilsen B (1992) Functional consequences of alterations to Glu309, Glu771, and Asp800 in the Ca(2+)-ATPase of sarcoplasmic reticulum. J Biol Chem 267: 19383-19387.
    • (1992) J Biol Chem , vol.267 , pp. 19383-19387
    • Andersen, J.P.1    Vilsen, B.2
  • 39
    • 0023874795 scopus 로고
    • Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases
    • Shull GE, Greeb J (1988) Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases. J Biol Chem 263: 8646-8657.
    • (1988) J Biol Chem , vol.263 , pp. 8646-8657
    • Shull, G.E.1    Greeb, J.2
  • 40
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • DOI 10.1038/35015017
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405: 647-655. (Pubitemid 30428644)
    • (2000) Nature , vol.405 , Issue.6787 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 41
    • 84944648082 scopus 로고
    • Revised Effective Ionic-Radii and Systematic Studies of Interatomic Distances in Halides and Chalcogenides
    • Shannon RD (1976) Revised Effective Ionic-Radii and Systematic Studies of Interatomic Distances in Halides and Chalcogenides. Acta Crystallographica Section A 32: 751-767.
    • (1976) Acta Crystallographica Section A , vol.32 , pp. 751-767
    • Shannon, R.D.1
  • 42
    • 21944437992 scopus 로고    scopus 로고
    • Inorganic and bioinorganic solvent exchange mechanisms
    • DOI 10.1021/cr030726o
    • Helm L, Merbach AE (2005) Inorganic and bioinorganic solvent exchange mechanisms. Chemical Reviews 105: 1923-1959. (Pubitemid 40947946)
    • (2005) Chemical Reviews , vol.105 , Issue.6 , pp. 1923-1959
    • Helm, L.1    Merbach, A.E.2
  • 43
    • 37049090798 scopus 로고
    • Comparison of the Coordinative Behavior of Calcium(Ii) and Magnesium(Ii) from Crystallographic Data
    • Carugo O, Djinovic K, Rizzi M (1993) Comparison of the Coordinative Behavior of Calcium(Ii) and Magnesium(Ii) from Crystallographic Data. Journal of the Chemical Society-Dalton Transactions: 2127-2135.
    • (1993) Journal of the Chemical Society-Dalton Transactions , pp. 2127-2135
    • Carugo, O.1    Djinovic, K.2    Rizzi, M.3
  • 44
    • 2142859139 scopus 로고    scopus 로고
    • Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc
    • DOI 10.1021/ja953943i
    • Katz AK, Glusker JP, Beebe SA, Bock CW (1996) Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc. Journal of the American Chemical Society 118: 5752-5763. (Pubitemid 26233665)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.24 , pp. 5752-5763
    • Katz, A.K.1    Glusker, J.P.2    Beebe, S.A.3    Bock, C.W.4
  • 47
    • 33748496466 scopus 로고    scopus 로고
    • Hydration energies of divalent beryllium and magnesium ions: An ab initio molecular orbital study
    • Markham GD, Glusker JP, Bock CL, Trachtman M, Bock CW (1996) Hydration energies of divalent beryllium and magnesium ions: An ab initio molecular orbital study. Journal of Physical Chemistry 100: 3488-3497. (Pubitemid 126788356)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.9 , pp. 3488-3497
    • Markham, G.D.1    Glusker, J.P.2    Bock, C.L.3    Trachtman, M.4    Bock, C.W.5
  • 48
    • 84885968069 scopus 로고    scopus 로고
    • The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum
    • Akin BL, Hurley TD, Chen Z, Jones LR (2013) The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. J Biol Chem 288: 30181-30191.
    • (2013) J Biol Chem , vol.288 , pp. 30181-30191
    • Akin, B.L.1    Hurley, T.D.2    Chen, Z.3    Jones, L.R.4
  • 49
    • 78650724760 scopus 로고    scopus 로고
    • Relationship between Ca2+-affinity and shielding of bulk water in the Ca2+-pump from molecular dynamics simulations
    • Sugita Y, Ikeguchi M, Toyoshima C (2010) Relationship between Ca2+-affinity and shielding of bulk water in the Ca2+-pump from molecular dynamics simulations. Proc Natl Acad Sci U S A 107: 21465-21469.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 21465-21469
    • Sugita, Y.1    Ikeguchi, M.2    Toyoshima, C.3
  • 50
    • 79952162827 scopus 로고    scopus 로고
    • Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+
    • Toyoshima C, Yonekura S, Tsueda J, Iwasawa S (2011) Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+. Proc Natl Acad Sci U S A 108: 1833-1838.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1833-1838
    • Toyoshima, C.1    Yonekura, S.2    Tsueda, J.3    Iwasawa, S.4
  • 51
    • 84886049897 scopus 로고    scopus 로고
    • Phosphorylated Phospholamban Stabilizes a Compact Conformation of the Cardiac Calcium-ATPase
    • Pallikkuth S, Blackwell DJ, Hu Z, Hou Z, Zieman DT, et al. (2013) Phosphorylated Phospholamban Stabilizes a Compact Conformation of the Cardiac Calcium-ATPase. Biophys J 105: 1812-1821.
    • (2013) Biophys J , vol.105 , pp. 1812-1821
    • Pallikkuth, S.1    Blackwell, D.J.2    Hu, Z.3    Hou, Z.4    Zieman, D.T.5
  • 52
    • 41949099075 scopus 로고    scopus 로고
    • Interdomain fluorescence resonance energy transfer in SERCA probed by cyan-fluorescent protein fused to the actuator domain
    • DOI 10.1021/bi702089j
    • Winters DL, Autry JM, Svensson B, Thomas DD (2008) Interdomain fluorescence resonance energy transfer in SERCA probed by cyan-fluorescent protein fused to the actuator domain. Biochemistry 47: 4246-4256. (Pubitemid 351506350)
    • (2008) Biochemistry , vol.47 , Issue.14 , pp. 4246-4256
    • Winters, D.L.1    Autry, J.M.2    Svensson, B.3    Thomas, D.D.4
  • 53
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • DOI 10.1038/nature02680
    • Toyoshima C, Mizutani T (2004) Crystal structure of the calcium pump with a bound ATP analogue. Nature 430: 529-535. (Pubitemid 38998620)
    • (2004) Nature , vol.430 , Issue.6999 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 54
    • 84885653302 scopus 로고    scopus 로고
    • Crystal structure of Na+, K(+)-ATPase in the Na(+)-bound state
    • Nyblom M, Poulsen H, Gourdon P, Reinhard L, Andersson M, et al. (2013) Crystal structure of Na+, K(+)-ATPase in the Na(+)-bound state. Science 342: 123-127.
    • (2013) Science , vol.342 , pp. 123-127
    • Nyblom, M.1    Poulsen, H.2    Gourdon, P.3    Reinhard, L.4    Andersson, M.5
  • 55
    • 84885654984 scopus 로고    scopus 로고
    • Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state
    • Kanai R, Ogawa H, Vilsen B, Cornelius F, Toyoshima C (2013) Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state. Nature 502: 201-206.
    • (2013) Nature , vol.502 , pp. 201-206
    • Kanai, R.1    Ogawa, H.2    Vilsen, B.3    Cornelius, F.4    Toyoshima, C.5
  • 56
    • 84860850396 scopus 로고    scopus 로고
    • Protein kinase A (PKA) phosphorylation of Na+/K+-ATPase opens intracellular C-terminal water pathway leading to third Na+-binding site in molecular dynamics simulations
    • Poulsen H, Nissen P, Mouritsen OG, Khandelia H (2012) Protein kinase A (PKA) phosphorylation of Na+/K+-ATPase opens intracellular C-terminal water pathway leading to third Na+-binding site in molecular dynamics simulations. J Biol Chem 287: 15959-15965.
    • (2012) J Biol Chem , vol.287 , pp. 15959-15965
    • Poulsen, H.1    Nissen, P.2    Mouritsen, O.G.3    Khandelia, H.4
  • 57
    • 80455174602 scopus 로고    scopus 로고
    • Protonation of key acidic residues is critical for the K(+)-selectivity of the Na/K pump
    • Yu H, Ratheal IM, Artigas P, Roux B (2011) Protonation of key acidic residues is critical for the K(+)-selectivity of the Na/K pump. Nat Struct Mol Biol 18: 1159-1163.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1159-1163
    • Yu, H.1    Ratheal, I.M.2    Artigas, P.3    Roux, B.4
  • 58
    • 84890548938 scopus 로고    scopus 로고
    • SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically incompetent conformation
    • Clausen JD, Bublitz M, Arnou B, Montigny C, Jaxel C, et al. (2013) SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically incompetent conformation. EMBO J 32: 3231-3243.
    • (2013) EMBO J , vol.32 , pp. 3231-3243
    • Clausen, J.D.1    Bublitz, M.2    Arnou, B.3    Montigny, C.4    Jaxel, C.5
  • 59
    • 84863423155 scopus 로고    scopus 로고
    • A microplate technique to simultaneously assay calcium accumulation in endoplasmic reticulum and SERCA release of inorganic phosphate
    • McMullen DC, Kean WS, Verma A, Cole JT, Watson WD (2012) A microplate technique to simultaneously assay calcium accumulation in endoplasmic reticulum and SERCA release of inorganic phosphate. Biol Proced Online 14: 4.
    • (2012) Biol Proced Online , vol.14 , pp. 4
    • McMullen, D.C.1    Kean, W.S.2    Verma, A.3    Cole, J.T.4    Watson, W.D.5
  • 60
    • 0021099396 scopus 로고
    • Effect of magnesium on the calcium-dependent transient kinetics of sarcoplasmic reticulum ATPase, studied by stopped flow fluorescence and phosphorylation
    • Champeil P, Gingold MP, Guillain F, Inesi G (1983) Effect of magnesium on the calcium-dependent transient kinetics of sarcoplasmic reticulum ATPase, studied by stopped flow fluorescence and phosphorylation. J Biol Chem 258: 4453-4458.
    • (1983) J Biol Chem , vol.258 , pp. 4453-4458
    • Champeil, P.1    Gingold, M.P.2    Guillain, F.3    Inesi, G.4
  • 61
    • 33646010306 scopus 로고    scopus 로고
    • Conformational changes in sarcoplasmic reticulum Ca(2+)-ATPase mutants: Effect of mutations either at Ca(2+)-binding site II or at tryptophan 552 in the cytosolic domain
    • Lenoir G, Jaxel C, Picard M, le Maire M, Champeil P, et al. (2006) Conformational changes in sarcoplasmic reticulum Ca(2+)-ATPase mutants: effect of mutations either at Ca(2+)-binding site II or at tryptophan 552 in the cytosolic domain. Biochemistry 45: 5261-5270.
    • (2006) Biochemistry , vol.45 , pp. 5261-5270
    • Lenoir, G.1    Jaxel, C.2    Picard, M.3    Le Maire, M.4    Champeil, P.5


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