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Volumn 22, Issue 4, 2012, Pages 491-499

Flexible P-type ATPases interacting with the membrane

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); HEAVY METAL; P TYPE ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84865291615     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2012.05.009     Document Type: Review
Times cited : (21)

References (74)
  • 2
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 angstrom resolution
    • Toyoshima C., Nakasako M., Nomura H., Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 angstrom resolution. Nature 2000, 405:647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 4
    • 79951681214 scopus 로고    scopus 로고
    • The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump
    • Møller J.V., Olesen C., Winther A.M.L., Nissen P. The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump. Q Rev Biophys 2010, 43:1-66.
    • (2010) Q Rev Biophys , vol.43 , pp. 1-66
    • Møller, J.V.1    Olesen, C.2    Winther, A.M.L.3    Nissen, P.4
  • 8
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4Å resolution
    • Shinoda T., Ogawa H., Cornelius F., Toyoshima C. Crystal structure of the sodium-potassium pump at 2.4Å resolution. Nature 2009, 459:446-450.
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 9
    • 0024381425 scopus 로고
    • Purification of limited tryptic fragments of Ca2+ Mg2+-adenosine triphosphatase of the sarcoplasmic reticulum and identification of conformation-sensitive cleavage sites
    • Imamura Y., Kawakita M. Purification of limited tryptic fragments of Ca2+ Mg2+-adenosine triphosphatase of the sarcoplasmic reticulum and identification of conformation-sensitive cleavage sites. J Biochem 1989, 105:775-781.
    • (1989) J Biochem , vol.105 , pp. 775-781
    • Imamura, Y.1    Kawakita, M.2
  • 10
    • 0025192950 scopus 로고
    • Ca2+-induced conformational changes and location of Ca2+ transport sites in sarcoplasmic reticulum Ca2+-ATPase as detected by the use of proteolytic enzyme (V8)
    • le Maire M., Lund S., Viel A., Champeil P., Møller J.V. Ca2+-induced conformational changes and location of Ca2+ transport sites in sarcoplasmic reticulum Ca2+-ATPase as detected by the use of proteolytic enzyme (V8). J Biol Chem 1990, 265:1111-1123.
    • (1990) J Biol Chem , vol.265 , pp. 1111-1123
    • le Maire, M.1    Lund, S.2    Viel, A.3    Champeil, P.4    Møller, J.V.5
  • 11
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: a structural perspective
    • Lee A.G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta 2003, 1612:1-40.
    • (2003) Biochim Biophys Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 12
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9Å resolution
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., Pebay-Peyroula E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9Å resolution. Structure 1999, 7:909-917.
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 14
    • 70349863382 scopus 로고    scopus 로고
    • Lipid-protein interactions probed by electron crystallography
    • Reichow S.L., Gonen T. Lipid-protein interactions probed by electron crystallography. Curr Opin Struct Biol 2009, 19:560-565.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 560-565
    • Reichow, S.L.1    Gonen, T.2
  • 15
    • 26844439857 scopus 로고    scopus 로고
    • Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+)
    • Obara K., Miyashita N., Xu C., Toyoshima I., Sugita Y., Inesi G., Toyoshima C. Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+). Proc Natl Acad Sci USA 2005, 102:14489-14496.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14489-14496
    • Obara, K.1    Miyashita, N.2    Xu, C.3    Toyoshima, I.4    Sugita, Y.5    Inesi, G.6    Toyoshima, C.7
  • 18
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima C., Nomura H., Tsuda T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 2004, 432:361-368.
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 19
    • 69549106325 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump (Na+ K+-ATPase) with bound potassium and ouabain
    • Ogawa H., Shinoda T., Cornelius F., Toyoshima C. Crystal structure of the sodium-potassium pump (Na+ K+-ATPase) with bound potassium and ouabain. Proc Natl Acad Sci USA 2009, 106:13742-13747.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13742-13747
    • Ogawa, H.1    Shinoda, T.2    Cornelius, F.3    Toyoshima, C.4
  • 22
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: the case of the calcium pump
    • Lee A.G. How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim Biophys Acta 1998, 1376:381-390.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 381-390
    • Lee, A.G.1
  • 23
    • 0020485872 scopus 로고
    • Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase studied with fluorescence quenching by a brominated phospholipid
    • East J.M., Lee A.G. Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase studied with fluorescence quenching by a brominated phospholipid. Biochemistry 1982, 21:4144-4151.
    • (1982) Biochemistry , vol.21 , pp. 4144-4151
    • East, J.M.1    Lee, A.G.2
  • 24
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function - the hydrophobic matching hypothesis revisited
    • Jensen MØ, Mouritsen O.G. Lipids do influence protein function - the hydrophobic matching hypothesis revisited. Biochim Biophys Acta 2004, 1666:205-226.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 205-226
    • Jensen MØ1    Mouritsen, O.G.2
  • 25
    • 84861557025 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the Ca2+-pump: a structural analysis
    • Lervik A., Bresme F., Kjelstrup S. Molecular dynamics simulations of the Ca2+-pump: a structural analysis. Phys Chem Chem Phys 2012, 14:3543-3553.
    • (2012) Phys Chem Chem Phys , vol.14 , pp. 3543-3553
    • Lervik, A.1    Bresme, F.2    Kjelstrup, S.3
  • 28
    • 34347247711 scopus 로고    scopus 로고
    • Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors
    • Takahashi M., Kondou Y., Toyoshima C. Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors. Proc Natl Acad Sci USA 2007, 104:5800-5805.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5800-5805
    • Takahashi, M.1    Kondou, Y.2    Toyoshima, C.3
  • 29
    • 0038031808 scopus 로고    scopus 로고
    • Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban
    • Asahi M., Sugita Y., Kurzydlowski K., De Leon S., Tada M., Toyoshima C., MacLennan D.H. Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban. Proc Natl Acad Sci USA 2003, 100:5040-5045.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5040-5045
    • Asahi, M.1    Sugita, Y.2    Kurzydlowski, K.3    De Leon, S.4    Tada, M.5    Toyoshima, C.6    MacLennan, D.H.7
  • 31
    • 0037160127 scopus 로고    scopus 로고
    • Sarcolipin overexpression in rat slow twitch muscle inhibits sarcoplasmic reticulum Ca2+ uptake and impairs contractile function
    • Tupling A.R., Asahi M., MacLennan D.H. Sarcolipin overexpression in rat slow twitch muscle inhibits sarcoplasmic reticulum Ca2+ uptake and impairs contractile function. J Biol Chem 2002, 277:44740-44746.
    • (2002) J Biol Chem , vol.277 , pp. 44740-44746
    • Tupling, A.R.1    Asahi, M.2    MacLennan, D.H.3
  • 32
    • 0026567125 scopus 로고
    • Molecular mechanism of regulation of Ca2+ pump ATPase by phospholamban in cardiac sarcoplasmic reticulum. Effects of synthetic phospholamban peptides on Ca2+ pump ATPase
    • Sasaki T., Inui M., Kimura Y., Kuzuya T., Tada M. Molecular mechanism of regulation of Ca2+ pump ATPase by phospholamban in cardiac sarcoplasmic reticulum. Effects of synthetic phospholamban peptides on Ca2+ pump ATPase. J Biol Chem 1992, 267:1674-1679.
    • (1992) J Biol Chem , vol.267 , pp. 1674-1679
    • Sasaki, T.1    Inui, M.2    Kimura, Y.3    Kuzuya, T.4    Tada, M.5
  • 33
    • 67649391254 scopus 로고    scopus 로고
    • Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase
    • Laursen M., Bublitz M., Moncoq K., Olesen C., Møller J.V., Young H.S., Nissen P., Morth J.P. Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase. J Biol Chem 2009, 284:13513-13518.
    • (2009) J Biol Chem , vol.284 , pp. 13513-13518
    • Laursen, M.1    Bublitz, M.2    Moncoq, K.3    Olesen, C.4    Møller, J.V.5    Young, H.S.6    Nissen, P.7    Morth, J.P.8
  • 34
    • 19244368104 scopus 로고
    • Structure and biological activity of sesquiterpene lactones from thapsia species and of analogue derivatives
    • Rasmussen U., Christensen S.B., Patkar S.A. Structure and biological activity of sesquiterpene lactones from thapsia species and of analogue derivatives. Planta Med 1982, 45:157.
    • (1982) Planta Med , vol.45 , pp. 157
    • Rasmussen, U.1    Christensen, S.B.2    Patkar, S.A.3
  • 35
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2+-ATPase
    • Thastrup O., Cullen P.J., Drobak B.K., Hanley M.R., Dawson A.P. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2+-ATPase. Proc Natl Acad Sci USA 1990, 87:2466-2470.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 37
    • 0029768099 scopus 로고    scopus 로고
    • Structural effects of neutral and anionic lipids on the nicotinic acetylcholine receptor
    • Ryan S.E., Demers C.N., Chew J.P., Baenziger J.E. Structural effects of neutral and anionic lipids on the nicotinic acetylcholine receptor. J Biol Chem 1996, 271:24590-24597.
    • (1996) J Biol Chem , vol.271 , pp. 24590-24597
    • Ryan, S.E.1    Demers, C.N.2    Chew, J.P.3    Baenziger, J.E.4
  • 38
    • 41449090448 scopus 로고    scopus 로고
    • Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening
    • Marius P., Zagnoni M., Sandison M.E., East J.M., Morgan H., Lee A.G. Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening. Biophys J 2008, 94:1689-1698.
    • (2008) Biophys J , vol.94 , pp. 1689-1698
    • Marius, P.1    Zagnoni, M.2    Sandison, M.E.3    East, J.M.4    Morgan, H.5    Lee, A.G.6
  • 42
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of beta subunits in oligomeric P-type ATPases
    • Geering K. The functional role of beta subunits in oligomeric P-type ATPases. J Bioenerg Biomembr 2001, 33:425-438.
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 425-438
    • Geering, K.1
  • 45
    • 33645984859 scopus 로고    scopus 로고
    • Role of FXYD proteins in ion transport
    • Garty H., Karlish S.J. Role of FXYD proteins in ion transport. Annu Rev Physiol 2006, 68:431-459.
    • (2006) Annu Rev Physiol , vol.68 , pp. 431-459
    • Garty, H.1    Karlish, S.J.2
  • 46
    • 79954415607 scopus 로고    scopus 로고
    • Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase
    • Yatime L., Laursen M., Morth J.P., Esmann M., Nissen P., Fedosova N.U. Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase. J Struct Biol 2011, 174:296-306.
    • (2011) J Struct Biol , vol.174 , pp. 296-306
    • Yatime, L.1    Laursen, M.2    Morth, J.P.3    Esmann, M.4    Nissen, P.5    Fedosova, N.U.6
  • 50
    • 37349040730 scopus 로고    scopus 로고
    • Purification of the human alpha2 isoform of Na K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1
    • Lifshitz Y., Petrovich E., Haviv H., Goldshleger R., Tal D.M., Garty H., Karlish S.J.D. Purification of the human alpha2 isoform of Na K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1. Biochemistry 2007, 46:14937-14950.
    • (2007) Biochemistry , vol.46 , pp. 14937-14950
    • Lifshitz, Y.1    Petrovich, E.2    Haviv, H.3    Goldshleger, R.4    Tal, D.M.5    Garty, H.6    Karlish, S.J.D.7
  • 51
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • Marsh D., Horváth L.I. Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim Biophys Acta 1998, 1376:267-296.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horváth, L.I.2
  • 52
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 1998, 7:1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 53
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok V.A., Voelker D.R., Campbell P.A., Cohen J.J., Bratton D.L., Henson P.M. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol 1992, 148:2207-2216.
    • (1992) J Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 55
    • 78649790906 scopus 로고    scopus 로고
    • Curcumin is a lipid dependent inhibitor of the Na K-ATPase that likely interacts at the protein-lipid interface
    • Mahmmoud Y.A. Curcumin is a lipid dependent inhibitor of the Na K-ATPase that likely interacts at the protein-lipid interface. Biochim Biophys Acta 2011, 1808:466-473.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 466-473
    • Mahmmoud, Y.A.1
  • 56
    • 35148853739 scopus 로고    scopus 로고
    • Curcumin is a modulator of bilayer material properties
    • Ingolfsson H.I., Koeppe R.E., Andersen O.S. Curcumin is a modulator of bilayer material properties. Biochemistry 2007, 46:10384-10391.
    • (2007) Biochemistry , vol.46 , pp. 10384-10391
    • Ingolfsson, H.I.1    Koeppe, R.E.2    Andersen, O.S.3
  • 57
    • 0031872002 scopus 로고    scopus 로고
    • Effect of cholesterol on molecular order and dynamics in highly polyunsaturated phospholipid bilayers
    • Mitchell D.C., Litman B.J. Effect of cholesterol on molecular order and dynamics in highly polyunsaturated phospholipid bilayers. Biophys J 1998, 75:896-908.
    • (1998) Biophys J , vol.75 , pp. 896-908
    • Mitchell, D.C.1    Litman, B.J.2
  • 58
    • 78650889008 scopus 로고    scopus 로고
    • Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump
    • Glaves J.P., Trieber C.A., Ceholski D.K., Stokes D.L., Young H.S. Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump. J Mol Biol 2011, 405:707-723.
    • (2011) J Mol Biol , vol.405 , pp. 707-723
    • Glaves, J.P.1    Trieber, C.A.2    Ceholski, D.K.3    Stokes, D.L.4    Young, H.S.5
  • 59
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982, 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 60
    • 0019934717 scopus 로고
    • The helical hydrophobic moment - a measure of the amphiphilicity of a helix
    • Eisenberg D., Weiss R.M., Terwilliger T.C. The helical hydrophobic moment - a measure of the amphiphilicity of a helix. Nature 1982, 299:371-374.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 61
    • 84859832471 scopus 로고    scopus 로고
    • Structural models of the human copper P-type ATPases ATP7A and ATP7B
    • Gourdon P., Sitsel O., Karlsen J.L., Møller L.B., Nissen P. Structural models of the human copper P-type ATPases ATP7A and ATP7B. Biol Chem 2012, 393:205-216.
    • (2012) Biol Chem , vol.393 , pp. 205-216
    • Gourdon, P.1    Sitsel, O.2    Karlsen, J.L.3    Møller, L.B.4    Nissen, P.5
  • 62
    • 84857129152 scopus 로고    scopus 로고
    • Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases
    • Baldridge R.D., Graham T.R. Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases. Proc Natl Acad Sci USA 2012, 109:E290-E298.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Baldridge, R.D.1    Graham, T.R.2
  • 63
    • 84857136080 scopus 로고    scopus 로고
    • Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2
    • Coleman J.A., Vestergaard A.L., Molday R.S., Vilsen B., Andersen J.P. Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2. Proc Natl Acad Sci USA 2012, 109:1449-1454.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 1449-1454
    • Coleman, J.A.1    Vestergaard, A.L.2    Molday, R.S.3    Vilsen, B.4    Andersen, J.P.5
  • 64
    • 70349731740 scopus 로고    scopus 로고
    • Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast
    • Zhou X., Graham T.R. Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast. Proc Natl Acad Sci USA 2009, 106:16586-16591.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16586-16591
    • Zhou, X.1    Graham, T.R.2
  • 67
    • 3042728119 scopus 로고    scopus 로고
    • Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae
    • Saito K., Fujimura-Kamada K., Furuta N., Kato U., Umeda M., Tanaka K. Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae. Mol Biol Cell 2004, 15:3418-3432.
    • (2004) Mol Biol Cell , vol.15 , pp. 3418-3432
    • Saito, K.1    Fujimura-Kamada, K.2    Furuta, N.3    Kato, U.4    Umeda, M.5    Tanaka, K.6
  • 68
    • 33749531732 scopus 로고    scopus 로고
    • Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane
    • Chen S., Wang J., Muthusamy B.P., Biu K., Zare S., Andersen R.J., Graham T.R. Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane. Traffic 2006, 7:1503-1517.
    • (2006) Traffic , vol.7 , pp. 1503-1517
    • Chen, S.1    Wang, J.2    Muthusamy, B.P.3    Biu, K.4    Zare, S.5    Andersen, R.J.6    Graham, T.R.7
  • 69
    • 67650516832 scopus 로고    scopus 로고
    • Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p
    • Lenoir G., Williamson P., Puts C.F., Holthuis J.C. Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p. J Biol Chem 2009, 284:17956-17967.
    • (2009) J Biol Chem , vol.284 , pp. 17956-17967
    • Lenoir, G.1    Williamson, P.2    Puts, C.F.3    Holthuis, J.C.4
  • 71
    • 79955763752 scopus 로고    scopus 로고
    • Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization and lipid transport activity of the P4-ATPase ATP8A2
    • Coleman J.A., Molday R.S. Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization and lipid transport activity of the P4-ATPase ATP8A2. J Biol Chem 2011, 286:17205-17216.
    • (2011) J Biol Chem , vol.286 , pp. 17205-17216
    • Coleman, J.A.1    Molday, R.S.2
  • 72
    • 0038143257 scopus 로고    scopus 로고
    • Electrogenicity of Na,K- and H K-ATPase activity and presence of a positively charged amino acid in the fifth trasmembrane segment
    • Burnay M., Crambert G., Kharoubi-Hess S., Geering K., Horisberger J.D. Electrogenicity of Na,K- and H K-ATPase activity and presence of a positively charged amino acid in the fifth trasmembrane segment. J Biol Chem 2003, 278:19237-19244.
    • (2003) J Biol Chem , vol.278 , pp. 19237-19244
    • Burnay, M.1    Crambert, G.2    Kharoubi-Hess, S.3    Geering, K.4    Horisberger, J.D.5
  • 73
    • 0032540752 scopus 로고    scopus 로고
    • Ca2+ transport by reconstituted synaptosomal ATPase is associated with H+ countertransport and net charge displacement
    • Salvador J.M., Inesi G., Rigaud J.L., Mata A.M. Ca2+ transport by reconstituted synaptosomal ATPase is associated with H+ countertransport and net charge displacement. J Biol Chem 1998, 273:18230-18234.
    • (1998) J Biol Chem , vol.273 , pp. 18230-18234
    • Salvador, J.M.1    Inesi, G.2    Rigaud, J.L.3    Mata, A.M.4
  • 74
    • 78651394444 scopus 로고    scopus 로고
    • Characterization of a Listeria monocytogenes Ca2+ pump - a SERCA-type ATPase with only one Ca2+-binding site
    • Faxén K., Andersen J.L., Gourdon P., Fedosova N., Morth J.P., Nissen P., Møller J.V. Characterization of a Listeria monocytogenes Ca2+ pump - a SERCA-type ATPase with only one Ca2+-binding site. J Biol Chem 2011, 286:1609-1617.
    • (2011) J Biol Chem , vol.286 , pp. 1609-1617
    • Faxén, K.1    Andersen, J.L.2    Gourdon, P.3    Fedosova, N.4    Morth, J.P.5    Nissen, P.6    Møller, J.V.7


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