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Volumn 5, Issue C, 1996, Pages 1-42

Structure of the SR/ER Ca2+-ATPase

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EID: 77957091108     PISSN: 18745342     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5342(06)80003-6     Document Type: Review
Times cited : (6)

References (123)
  • 3
    • 0026672665 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 267 (1992) 19383-19387
    • (1992) J. Biol. Chem. , vol.267 , pp. 19383-19387
    • Andersen, J.P.1    Vilsen, B.2
  • 5
    • 0028816888 scopus 로고
    • +-ATPases studied by site-directed mutagenesis
    • +-ATPases studied by site-directed mutagenesis. FEBS Lett. 359 (1995) 101-106
    • (1995) FEBS Lett. , vol.359 , pp. 101-106
    • Andersen, J.P.1    Vilsen, B.2
  • 7
    • 0027383387 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. Biochemistry 32 (1993) 10015-10020
    • (1993) Biochemistry , vol.32 , pp. 10015-10020
    • Andersen, J.P.1    Vilsen, B.2
  • 8
    • 0025911177 scopus 로고
    • Epitope mapping by amino-acid-sequence-specific antibodies reveals that both ends of the alpha subunit of Na/K-ATPase are located on the cytoplasmic side of the membrane
    • Antolovic R., Bruller H.J., Bunk S., Linder D., and Schoner W. Epitope mapping by amino-acid-sequence-specific antibodies reveals that both ends of the alpha subunit of Na/K-ATPase are located on the cytoplasmic side of the membrane. Eur. J. Biochem. 199 (1991) 195-202
    • (1991) Eur. J. Biochem. , vol.199 , pp. 195-202
    • Antolovic, R.1    Bruller, H.J.2    Bunk, S.3    Linder, D.4    Schoner, W.5
  • 10
    • 0025972010 scopus 로고
    • 2+-ATPase in the sarcoplasmic reticulum by resonance X-ray diffraction
    • 2+-ATPase in the sarcoplasmic reticulum by resonance X-ray diffraction. Biophys. J. 59 (1991) 488-502
    • (1991) Biophys. J. , vol.59 , pp. 488-502
    • Asturias, F.J.1    Blasie, J.K.2
  • 12
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle D., Weeks D., and Sachs G. The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J. Biol. Chem. 270 (1995) 25678-25684
    • (1995) J. Biol. Chem. , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 13
    • 0026018935 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. Biochemistry 30 (1991) 2113-2125
    • (1991) Biochemistry , vol.30 , pp. 2113-2125
    • Bigelow, D.J.1    Inesi, G.2
  • 14
    • 0024573346 scopus 로고
    • Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer
    • Birmachu W., Nisswandt F.L., and Thomas D.D. Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer. Biochemistry 28 (1989) 3940-3947
    • (1989) Biochemistry , vol.28 , pp. 3940-3947
    • Birmachu, W.1    Nisswandt, F.L.2    Thomas, D.D.3
  • 15
    • 0022558845 scopus 로고
    • 2+-ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences
    • 2+-ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences. Cell 44 (1986) 597-607
    • (1986) Cell , vol.44 , pp. 597-607
    • Brandl, C.J.1    Green, N.M.2    Korczak, B.3    MacLennan, D.H.4
  • 18
    • 0027732901 scopus 로고
    • Transmembrane organization of the Na,K-ATPase determined by epitope addition
    • Canfield V.A., and Levenson R. Transmembrane organization of the Na,K-ATPase determined by epitope addition. Biochemistry 32 (1993) 13782-13786
    • (1993) Biochemistry , vol.32 , pp. 13782-13786
    • Canfield, V.A.1    Levenson, R.2
  • 23
    • 0024429075 scopus 로고
    • 2+)-ATPase from rabbit skeletal muscle sarcoplasmic reticulum and their correlation with epitope location
    • 2+)-ATPase from rabbit skeletal muscle sarcoplasmic reticulum and their correlation with epitope location. Biochem. J. 262 (1989) 439-447
    • (1989) Biochem. J. , vol.262 , pp. 439-447
    • Colyer, J.1    Mata, A.M.2    Lee, A.G.3    East, J.M.4
  • 24
    • 0027439225 scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum as estimated through fluorescence energy transfer between probes
    • 2+-ATPase from sarcoplasmic reticulum as estimated through fluorescence energy transfer between probes. Eur. J. Biochem. 217 (1993) 737-744
    • (1993) Eur. J. Biochem. , vol.217 , pp. 737-744
    • Corbalan-Garcia, S.1    Teruel, J.A.2    Gomez-Fernandez, J.C.3
  • 29
    • 0023061436 scopus 로고
    • An introduction to molecular architecture and permeability of ion channels
    • Eisenman G., and Dani J.A. An introduction to molecular architecture and permeability of ion channels. Ann. Rev. Biophys. Chem. 16 (1987) 205-226
    • (1987) Ann. Rev. Biophys. Chem. , vol.16 , pp. 205-226
    • Eisenman, G.1    Dani, J.A.2
  • 30
    • 0027212191 scopus 로고
    • 2+-ATPase isoforms in the crustacean Artemia franciscana and in vertebrates
    • 2+-ATPase isoforms in the crustacean Artemia franciscana and in vertebrates. J. Biol. Chem. 268 (1993) 14090-14095
    • (1993) J. Biol. Chem. , vol.268 , pp. 14090-14095
    • Escalante, R.1    Sastro, L.2
  • 32
    • 0022558481 scopus 로고
    • 2+-activated ATPase by phosphate
    • 2+-activated ATPase by phosphate. Biochem. J. 237 (1986) 207-215
    • (1986) Biochem. J. , vol.237 , pp. 207-215
    • Froud, R.J.1    Lee, A.G.2
  • 34
    • 0025103791 scopus 로고
    • Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ion
    • Fujimori T., and Jencks W.P. Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ion. J. Biol. Chem. 265 (1990) 16262-16270
    • (1990) J. Biol. Chem. , vol.265 , pp. 16262-16270
    • Fujimori, T.1    Jencks, W.P.2
  • 35
  • 38
    • 0026707393 scopus 로고
    • Structural modelling of P-type ion pumps
    • Green N.M., and Stokes D.L. Structural modelling of P-type ion pumps. Acta Physiol. Scand. 146 (1992) 59-68
    • (1992) Acta Physiol. Scand. , vol.146 , pp. 59-68
    • Green, N.M.1    Stokes, D.L.2
  • 46
    • 0025376029 scopus 로고
    • Lysine 480 is an essential residue in the putative ATP site of lamb kidney (Na,K)-ATPase
    • Hinz H.R., and Kirley T.L. Lysine 480 is an essential residue in the putative ATP site of lamb kidney (Na,K)-ATPase. J. Biol. Chem. 265 (1990) 10260-10265
    • (1990) J. Biol. Chem. , vol.265 , pp. 10260-10265
    • Hinz, H.R.1    Kirley, T.L.2
  • 47
    • 0023814547 scopus 로고
    • Secondary structure prediction of liver microsomal cytochrome P-450; proposed model of spatial arrangement in a membrane
    • Hudecek J., and Anzenbacher P. Secondary structure prediction of liver microsomal cytochrome P-450; proposed model of spatial arrangement in a membrane. Biochim. Biophys. Acta 955 (1988) 361-370
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 361-370
    • Hudecek, J.1    Anzenbacher, P.2
  • 48
    • 0025760732 scopus 로고
    • 2+-transporting ATPase of the sarcoplasmic reticulum through its effects on fluorescence of tryptophan residues and a covalently attached fluorescent probe N-(1-anilinonaphthyl-4)maleimide
    • 2+-transporting ATPase of the sarcoplasmic reticulum through its effects on fluorescence of tryptophan residues and a covalently attached fluorescent probe N-(1-anilinonaphthyl-4)maleimide. J. Biochem. Tokyo 110 (1991) 214-219
    • (1991) J. Biochem. Tokyo , vol.110 , pp. 214-219
    • Imamura, Y.1    Kawakita, M.2
  • 51
    • 0027198546 scopus 로고
    • Calcium ATPase of sarcoplasmic reticulum has four binding sites for calcium
    • Jencks W.P., Yang T., Peisach D., and Myung J. Calcium ATPase of sarcoplasmic reticulum has four binding sites for calcium. Biochemistry 32 (1993) 7030-7034
    • (1993) Biochemistry , vol.32 , pp. 7030-7034
    • Jencks, W.P.1    Yang, T.2    Peisach, D.3    Myung, J.4
  • 52
    • 0025615830 scopus 로고
    • Antigenic determinant of a monoclonal antibody: Extracellular domain at the M3-M4 junction of the alpha-subunit of Na,K-ATPase
    • Kano I., Satoh K., Nagai F., Ushiyama K., Nakao T., Hara Y., and Kano K. Antigenic determinant of a monoclonal antibody: Extracellular domain at the M3-M4 junction of the alpha-subunit of Na,K-ATPase. Can. J. Biochem. 68 (1990) 1262-1267
    • (1990) Can. J. Biochem. , vol.68 , pp. 1262-1267
    • Kano, I.1    Satoh, K.2    Nagai, F.3    Ushiyama, K.4    Nakao, T.5    Hara, Y.6    Kano, K.7
  • 53
    • 0028970888 scopus 로고
    • 2+-ATPase: Separate binding sites for dihydroxybenzenes and sesquiterpene lactones
    • 2+-ATPase: Separate binding sites for dihydroxybenzenes and sesquiterpene lactones. Biochemistry 34 (1995) 14385-14393
    • (1995) Biochemistry , vol.34 , pp. 14385-14393
    • Khan, Y.M.1    Wictome, M.2    East, J.M.3    Lee, A.G.4
  • 55
    • 0027445899 scopus 로고
    • Coupling mechanisms in ATP-driven pumps
    • Krupka R.M. Coupling mechanisms in ATP-driven pumps. Biochim. Biophys. Acta 1183 (1993) 114-122
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 114-122
    • Krupka, R.M.1
  • 58
    • 0020079807 scopus 로고
    • Phosphorylation of calcium adenosinetriphosphatase by inorganic phosphate: Reversible inhibition at high magnesium ion concentrations
    • Loomis C.R., Martin D.W., McCaslin D.R., and Tanford C. Phosphorylation of calcium adenosinetriphosphatase by inorganic phosphate: Reversible inhibition at high magnesium ion concentrations. Biochemistry 21 (1982) 151-156
    • (1982) Biochemistry , vol.21 , pp. 151-156
    • Loomis, C.R.1    Martin, D.W.2    McCaslin, D.R.3    Tanford, C.4
  • 59
    • 0026725345 scopus 로고
    • Molecular dissection of functional domains of the E1E2-ATPase using sodium and calcium pump chimeric molecules
    • Luckie D.B., Lemas V., Boyd K.L., Fambrough D.M., and Takeyasu K. Molecular dissection of functional domains of the E1E2-ATPase using sodium and calcium pump chimeric molecules. Biophys. J. 62 (1992) 220-227
    • (1992) Biophys. J. , vol.62 , pp. 220-227
    • Luckie, D.B.1    Lemas, V.2    Boyd, K.L.3    Fambrough, D.M.4    Takeyasu, K.5
  • 61
    • 0022371456 scopus 로고
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316 (1985) 696-700
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Korczak, B.3    Green, N.M.4
  • 65
    • 0024373488 scopus 로고
    • 2+)-ATPase with anti-fluorescein antibodies
    • 2+)-ATPase with anti-fluorescein antibodies. FEBS Lett. 253 (1989) 273-275
    • (1989) FEBS Lett. , vol.253 , pp. 273-275
    • Mata, A.M.1    Lee, A.G.2    East, J.M.3
  • 69
    • 0025195683 scopus 로고
    • 2+)-ATPase from sarcoplasmic reticulum: Evidence for the luminal location of residues 877-888
    • 2+)-ATPase from sarcoplasmic reticulum: Evidence for the luminal location of residues 877-888. J. Biol. Chem. 265 (1990) 18737-18740
    • (1990) J. Biol. Chem. , vol.265 , pp. 18737-18740
    • Matthews, I.1    Sharma, R.P.2    Lee, A.G.3    East, J.M.4
  • 77
    • 0025148986 scopus 로고
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum. J. Cell Sci. 97 (1990) 487-495
    • (1990) J. Cell Sci. , vol.97 , pp. 487-495
    • Murakami, K.1    Tanabe, K.2    Takada, S.3
  • 78
    • 0028929927 scopus 로고
    • There is only one phosphoenzyme intermediate with bound calcium on the reaction pathway of the sarcoplasmic reticulum calcium ATPase
    • Myung J., and Jencks W.P. There is only one phosphoenzyme intermediate with bound calcium on the reaction pathway of the sarcoplasmic reticulum calcium ATPase. Biochemistry 34 (1995) 3077-3083
    • (1995) Biochemistry , vol.34 , pp. 3077-3083
    • Myung, J.1    Jencks, W.P.2
  • 79
    • 0022587646 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. FEBS Lett. 194 (1986) 258-262
    • (1986) FEBS Lett. , vol.194 , pp. 258-262
    • Nakamoto, R.K.1    Inesi, G.2
  • 80
    • 0025941509 scopus 로고
    • 2+-ATPase-do lanthanide ions bind to the calcium transport site?
    • 2+-ATPase-do lanthanide ions bind to the calcium transport site?. Biochemistry 30 (1991) 9966-9973
    • (1991) Biochemistry , vol.30 , pp. 9966-9973
    • Ogurusu, T.1    Wakabayashi, S.2    Shigekawa, M.3
  • 81
    • 0022486250 scopus 로고
    • +-transporting ATPase: Location of the 5′-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin
    • +-transporting ATPase: Location of the 5′-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin. Proc. Natl. Acad. Sci. USA 83 (1986) 2071-2075
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2071-2075
    • Ohta, T.1    Nagano, K.2    Yoshida, M.3
  • 82
    • 0026090409 scopus 로고
    • Kinetics of calcium dissociation from its high-affinity transport sites on sarcoplasmic reticulum ATPase
    • Orlowski S., and Champeil P. Kinetics of calcium dissociation from its high-affinity transport sites on sarcoplasmic reticulum ATPase. Biochemistry 30 (1991) 352-361
    • (1991) Biochemistry , vol.30 , pp. 352-361
    • Orlowski, S.1    Champeil, P.2
  • 83
    • 0026342277 scopus 로고
    • 2+-ATPase can no longer be kinetically distinguished when they dissociate from phosphorylated ATPase towards the lumen
    • 2+-ATPase can no longer be kinetically distinguished when they dissociate from phosphorylated ATPase towards the lumen. Biochemistry 30 (1991) 11331-11342
    • (1991) Biochemistry , vol.30 , pp. 11331-11342
    • Orlowski, S.1    Champeil, P.2
  • 84
    • 0024819294 scopus 로고
    • 2+-ATPase from the crustacean Artemia
    • 2+-ATPase from the crustacean Artemia. J. Mol. Biol. 210 (1989) 737-748
    • (1989) J. Mol. Biol. , vol.210 , pp. 737-748
    • Palmero, I.1    Sastre, L.2
  • 85
    • 0018788297 scopus 로고
    • The molecular structure of lecithin dihydrate
    • Pearson R.H., and Pascher I. The molecular structure of lecithin dihydrate. Nature 281 (1979) 499-501
    • (1979) Nature , vol.281 , pp. 499-501
    • Pearson, R.H.1    Pascher, I.2
  • 86
    • 0020479118 scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum by pH, temperature, and calcium ions
    • 2+-ATPase from sarcoplasmic reticulum by pH, temperature, and calcium ions. J. Biol. Chem. 257 (1982) 6120-6126
    • (1982) J. Biol. Chem. , vol.257 , pp. 6120-6126
    • Pick, U.1    Karlish, S.J.2
  • 87
    • 0019888172 scopus 로고
    • 2+)-adenosine triphosphatase is located on the cytoplasmic surface of the sarcoplasmic reticulum membrane
    • 2+)-adenosine triphosphatase is located on the cytoplasmic surface of the sarcoplasmic reticulum membrane. J. Biol. Chem. 256 (1981) 5957-5960
    • (1981) J. Biol. Chem. , vol.256 , pp. 5957-5960
    • Reithmeier, R.A.1    MacLennan, D.H.2
  • 88
    • 77957037606 scopus 로고
    • Functional roles of amino acids in transmembrane sequence M4 of SERCA1
    • Rice W.J., Clarke D.M., Loo T.W., and MacLennan D.H. Functional roles of amino acids in transmembrane sequence M4 of SERCA1. Biophys. J 64 (1993) A333
    • (1993) Biophys. J , vol.64
    • Rice, W.J.1    Clarke, D.M.2    Loo, T.W.3    MacLennan, D.H.4
  • 89
    • 0022348320 scopus 로고
    • 2+)-ATPase of sarcoplasmic reticulum
    • 2+)-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 260 (1985) 14421-14423
    • (1985) J. Biol. Chem. , vol.260 , pp. 14421-14423
    • Scott, T.L.1
  • 90
    • 0024505424 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum. Regulatory/superfluorescent nucleotides label the catalytic site with high efficiency
    • 2+-ATPase of sarcoplasmic reticulum. Regulatory/superfluorescent nucleotides label the catalytic site with high efficiency. J. Biol. Chem. 264 (1989) 2043-2052
    • (1989) J. Biol. Chem. , vol.264 , pp. 2043-2052
    • Seebregts, C.J.1    McIntosh, D.B.2
  • 93
    • 0027444708 scopus 로고
    • Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium
    • Smith D.L., Tao T., and Maguire M.E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 268 (1993) 22469-22479
    • (1993) J. Biol. Chem. , vol.268 , pp. 22469-22479
    • Smith, D.L.1    Tao, T.2    Maguire, M.E.3
  • 95
    • 0023463257 scopus 로고
    • 2+ that are not satisfactorily described by an E1-E2 model
    • 2+ that are not satisfactorily described by an E1-E2 model. Biochemistry 26 (1987) 7654-7667
    • (1987) Biochemistry , vol.26 , pp. 7654-7667
    • Stahl, N.1    Jencks, W.P.2
  • 98
    • 0025000180 scopus 로고
    • 2+-ATPase suggest a shape for the intramembranous domain
    • 2+-ATPase suggest a shape for the intramembranous domain. Biochem. Soc. Trans. 18 (1990) 841-843
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 841-843
    • Stokes, D.L.1    Green, N.M.2
  • 99
    • 0025019294 scopus 로고
    • Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing
    • Stokes D.L., and Green N.M. Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing. Biophys. J. 57 (1990) 1-14
    • (1990) Biophys. J. , vol.57 , pp. 1-14
    • Stokes, D.L.1    Green, N.M.2
  • 100
    • 0028236332 scopus 로고
    • Structure, transmembrane topology and helix packing of P-type ion pumps
    • Stokes D.L., Taylor W.R., and Green N.M. Structure, transmembrane topology and helix packing of P-type ion pumps. FEBS Lett. 346 (1994) 32-38
    • (1994) FEBS Lett. , vol.346 , pp. 32-38
    • Stokes, D.L.1    Taylor, W.R.2    Green, N.M.3
  • 101
    • 0019627251 scopus 로고
    • Formation of magnesium-phosphoenzyme and magnesium-calcium-phosphoenzyme in the phosphorylation of adenosine triphosphatase by orthophosphate in sarcoplasmic reticulum: Models of a reaction sequence
    • Suko J., Plank B., Preis P., Kolassa N., Hellmann G., and Conca W. Formation of magnesium-phosphoenzyme and magnesium-calcium-phosphoenzyme in the phosphorylation of adenosine triphosphatase by orthophosphate in sarcoplasmic reticulum: Models of a reaction sequence. Eur. J. Biochem. 119 (1981) 225-236
    • (1981) Eur. J. Biochem. , vol.119 , pp. 225-236
    • Suko, J.1    Plank, B.2    Preis, P.3    Kolassa, N.4    Hellmann, G.5    Conca, W.6
  • 107
    • 0027405626 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban
    • 2+-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban. J. Biol. Chem. 268 (1993) 2809-2815
    • (1993) J. Biol. Chem. , vol.268 , pp. 2809-2815
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 108
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • Toyoshima C., Sasabe H., and Stokes D.L. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 362 (1993) 469-471
    • (1993) Nature , vol.362 , pp. 469-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 113
    • 0026740539 scopus 로고
    • 2+-ATPase of frog skeletal muscle
    • 2+-ATPase of frog skeletal muscle. FEBS Lett. 306 (1992) 213-218
    • (1992) FEBS Lett. , vol.306 , pp. 213-218
    • Vilsen, B.1    Andersen, J.P.2
  • 114
    • 0027008485 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 267 (1992) 25739-25743
    • (1992) J. Biol. Chem. , vol.267 , pp. 25739-25743
    • Vilsen, B.1    Andersen, J.P.2
  • 115
    • 0025782832 scopus 로고
    • Proline kinks in transmembrane α-helices
    • von Heijne G. Proline kinks in transmembrane α-helices. J. Mol. Biol. 218 (1991) 499-503
    • (1991) J. Mol. Biol. , vol.218 , pp. 499-503
    • von Heijne, G.1
  • 116
    • 0026501841 scopus 로고
    • Regulation of the calcium ion pump of sarcoplasmic reticulum: Reversible inhibition by phospholamban and by the calmodulin binding domain of the plasma membrane calcium ion pump
    • Vorherr T., Chiesi M., Schwaller R., and Carafoli E. Regulation of the calcium ion pump of sarcoplasmic reticulum: Reversible inhibition by phospholamban and by the calmodulin binding domain of the plasma membrane calcium ion pump. Biochemistry 31 (1992) 371-376
    • (1992) Biochemistry , vol.31 , pp. 371-376
    • Vorherr, T.1    Chiesi, M.2    Schwaller, R.3    Carafoli, E.4
  • 120
    • 0024316495 scopus 로고
    • Any of several lysines can react with 5′-isothiocyanatofluorescein to inactivate sodium and potassium ion activated adenosinetriphosphatase
    • Xu K.Y. Any of several lysines can react with 5′-isothiocyanatofluorescein to inactivate sodium and potassium ion activated adenosinetriphosphatase. Biochemistry 28 (1989) 5764-5772
    • (1989) Biochemistry , vol.28 , pp. 5764-5772
    • Xu, K.Y.1
  • 122
    • 0023838740 scopus 로고
    • 2+-transporting ATPase of sarcoplasmic reticulum by adenosine triphosphopyridoxal: Identification of the reactive lysyl residue
    • 2+-transporting ATPase of sarcoplasmic reticulum by adenosine triphosphopyridoxal: Identification of the reactive lysyl residue. J. Biochem. (Tokyo) 103 (1988) 452-457
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 452-457
    • Yamamoto, H.1    Tagaya, M.2    Fukui, T.3    Kawakita, M.4
  • 123
    • 0024823960 scopus 로고
    • 2+-transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosine triphosphopyridoxal
    • 2+-transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosine triphosphopyridoxal. J. Biochem. (Tokyo) 106 (1989) 1121-1125
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 1121-1125
    • Yamamoto, H.1    Imamura, Y.2    Tagaya, M.3    Fukui, T.4    Kawakita, M.5


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