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Volumn 50, Issue 2, 2003, Pages 337-365

The structure of the Ca2+-ATPase of sarcoplasmic reticulum

Author keywords

Calcium homeostasis; Calcium pump; Calcium transport; Excitation contraction coupling; Sarcoplasmic reticulum; Skeletal and cardiac muscles

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; CALCIUM; LANTHANIDE; PHOSPHATE; VANADIC ACID;

EID: 0042381683     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2003_3690     Document Type: Review
Times cited : (28)

References (179)
  • 3
    • 0029565489 scopus 로고
    • 2+ ATPase by site directed mutagenesis
    • 2+ ATPase by site directed mutagenesis. Biosci Rep.; 15: 243-61.
    • (1995) Biosci Rep , vol.15 , pp. 243-261
    • Andersen, J.P.1
  • 5
    • 0035282170 scopus 로고    scopus 로고
    • Functional properties of Na-K ATPase and their structural implications as detected by biophysical techniques
    • Apell H-J, Karlish SJ. (2001) Functional properties of Na-K ATPase and their structural implications as detected by biophysical techniques. J Membr Biol.; 180: 1-9.
    • (2001) J Membr Biol , vol.180 , pp. 1-9
    • Apell, H.-J.1    Karlish, S.J.2
  • 6
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • Aravind L, Galperin MY, Koonin EV. (1998) The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem Sci.; 23: 127-9.
    • (1998) Trends Biochem Sci , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 8
    • 0024652740 scopus 로고
    • 2+ uptake kinetics and structure of the sarcoplasmic reticulum membrane
    • 2+ uptake kinetics and structure of the sarcoplasmic reticulum membrane. Biophys J.; 55: 739-53.
    • (1989) Biophys J , vol.55 , pp. 739-753
    • Asturias, F.J.1    Blasie, J.K.2
  • 9
    • 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: 488-502.
    • (1991) Biophys J , vol.59 , pp. 488-502
    • Asturias, F.J.1    Blasie, J.K.2
  • 10
    • 0028219938 scopus 로고
    • 2+-ATPase enzyme in the presence of terbium: A time-resolved X-ray diffraction study
    • 2+-ATPase enzyme in the presence of terbium: a time-resolved X-ray diffraction study. Biophys J.; 66: 1665-77.
    • (1994) Biophys J , vol.66 , pp. 1665-1677
    • Asturias, F.J.1    Fischetti, R.J.2    Blasie, J.K.3
  • 11
    • 0028354441 scopus 로고
    • 2+-ATPase enzyme in the presence of terbium: A time-resolved X-ray diffraction study
    • 2+-ATPase enzyme in the presence of terbium: a time-resolved X-ray diffraction study. Biophys J.; 66: 1653-64.
    • (1994) Biophys J , vol.66 , pp. 1653-1664
    • Asturias, F.J.1    Fischetti, R.F.2    Blasie, J.K.3
  • 13
    • 0014623470 scopus 로고
    • Comparative ultrastructure and calcium transport in heart and skeletal muscle microsomes
    • Baskin RJ, Deamer DW. (1969) Comparative ultrastructure and calcium transport in heart and skeletal muscle microsomes. J Cell Biol.; 43: 610-5.
    • (1969) J Cell Biol , vol.43 , pp. 610-615
    • Baskin, R.J.1    Deamer, D.W.2
  • 14
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle D, Weeks D, Sachs G. (1995) The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J Biol Chem.; 270: 25678-84.
    • (1995) J Biol Chem , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 15
    • 0021289168 scopus 로고
    • 4 and membrane potential on the structure of sarcoplasmic reticulum membrane
    • 4 and membrane potential on the structure of sarcoplasmic reticulum membrane. J Membr Biol.; 78: 73-9.
    • (1984) J Membr Biol , vol.78 , pp. 73-79
    • Beeler, T.J.1    Dux, L.2    Martonosi, A.N.3
  • 16
    • 0026489495 scopus 로고
    • 2+ transport ATPase of sarcoplasmic reticulum
    • 2+ transport ATPase of sarcoplasmic reticulum. Biochim Biophys Acta.; 1113: 323-38.
    • (1992) Biochim Biophys Acta , vol.1113 , pp. 323-338
    • Bigelow, D.J.1    Inesi, G.2
  • 18
    • 0021794209 scopus 로고
    • Biological membrane structure as seen by X-ray and neutron diffraction techniques
    • Blasie JK, Herbette L, Pachence J. (1985a) Biological membrane structure as seen by X-ray and neutron diffraction techniques. J Membr Biol.; 86: 1-7.
    • (1985) J Membr Biol , vol.86 , pp. 1-7
    • Blasie, J.K.1    Herbette, L.2    Pachence, J.3
  • 19
    • 0021867661 scopus 로고
    • Time resolved X-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport
    • Blasie JK, Herbette LG, Pascolini D, Skita V, Pierce DH, Scarpa A. (1985b) Time resolved X-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport. Biophys J.; 48: 9-18.
    • (1985) Biophys J , vol.48 , pp. 9-18
    • Blasie, J.K.1    Herbette, L.G.2    Pascolini, D.3    Skita, V.4    Pierce, D.H.5    Scarpa, A.6
  • 20
    • 0025184481 scopus 로고
    • Large-scale structural changes in the sarcoplasmic reticulum appear essential for calcium transport
    • Blasie JK, Pascolini D, Asturias F, Herbette LG, Pierce D, Scarpa A. (1990) Large-scale structural changes in the sarcoplasmic reticulum appear essential for calcium transport. Biophys J.; 58: 687-93.
    • (1990) Biophys J , vol.58 , pp. 687-693
    • Blasie, J.K.1    Pascolini, D.2    Asturias, F.3    Herbette, L.G.4    Pierce, D.5    Scarpa, A.6
  • 21
    • 0015953495 scopus 로고
    • Developmental changes in the composition and function of sarcoplasmic reticulum
    • Boland R, Martonosi A, Tillack TW. (1974) Developmental changes in the composition and function of sarcoplasmic reticulum. J Biol Chem.; 249: 612-23.
    • (1974) J Biol Chem , vol.249 , pp. 612-623
    • Boland, R.1    Martonosi, A.2    Tillack, T.W.3
  • 22
    • 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: 597-607.
    • (1986) Cell , vol.44 , pp. 597-607
    • Brandl, C.J.1    Green, N.M.2    Korczak, B.3    MacLennan, D.H.4
  • 23
  • 25
    • 0029664953 scopus 로고    scopus 로고
    • 2+ translocation across sarcoplasmic reticulum ATPase randomizes the two transported ions
    • 2+ translocation across sarcoplasmic reticulum ATPase randomizes the two transported ions. J Biol Chem.; 271: 20566-72.
    • (1996) J Biol Chem , vol.271 , pp. 20566-20572
    • Canet, D.1    Forge, V.2    Guillain, F.3    Mintz, E.4
  • 26
    • 0021930155 scopus 로고
    • Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum
    • Castellani L, Hardwicke PMD, Vibert P. (1985) Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum. J Mol Biol.; 185: 579-94.
    • (1985) J Mol Biol , vol.185 , pp. 579-594
    • Castellani, L.1    Hardwicke, P.M.D.2    Vibert, P.3
  • 27
    • 0024207276 scopus 로고
    • Isolation of transverse tubule membranes from skeletal muscle: Ion transport activity, reformation of triad junctions and isolation of junctional spanning protein of triads
    • Caswell AH, Brandt NR, Brunschwig J-P, Purkerson S. (1988) Isolation of transverse tubule membranes from skeletal muscle: Ion transport activity, reformation of triad junctions and isolation of junctional spanning protein of triads. Methods Enzymol.; 157: 68-84.
    • (1988) Methods Enzymol , vol.157 , pp. 68-84
    • Caswell, A.H.1    Brandt, N.R.2    Brunschwig, J.-P.3    Purkerson, S.4
  • 29
    • 0024271082 scopus 로고
    • Isolation of sarcoplasmic reticulum fractions referable to longitudinal tubules and junctional terminal cisternae from rabbit skeletal muscle
    • Chu A, Dixon MC, Saito A, Seiler S, Fleischer S. (1988) Isolation of sarcoplasmic reticulum fractions referable to longitudinal tubules and junctional terminal cisternae from rabbit skeletal muscle. Methods Enzymol.; 157: 36-46.
    • (1988) Methods Enzymol , vol.157 , pp. 36-46
    • Chu, A.1    Dixon, M.C.2    Saito, A.3    Seiler, S.4    Fleischer, S.5
  • 30
    • 0022830347 scopus 로고
    • Oligovanadate binding to sarcoplasmic reticulum. Evidence for substrate analogue behaviour
    • Coan C, Scales DJ, Murphy AJ. (1986) Oligovanadate binding to sarcoplasmic reticulum. Evidence for substrate analogue behaviour. J Biol Chem. ; 261: 10394-403.
    • (1986) J Biol Chem , vol.261 , pp. 10394-10403
    • Coan, C.1    Scales, D.J.2    Murphy, A.J.3
  • 31
    • 0028178370 scopus 로고
    • 2+ binding to occluded sites in the CrATP-ATPase complex of sarcoplasmic reticulum: Evidence for two independent high affinity sites
    • 2+ binding to occluded sites in the CrATP-ATPase complex of sarcoplasmic reticulum: evidence for two independent high affinity sites. Biochemistry.; 33: 3722-31.
    • (1994) Biochemistry , vol.33 , pp. 3722-3731
    • Coan, C.1    Ji, J.Y.2    Amaral, J.A.3
  • 32
    • 0024212108 scopus 로고
    • Isolation of the junctional face membrane of sarcoplasmic reticulum
    • Costello B, Chadwick C, Fleischer S. (1988) Isolation of the junctional face membrane of sarcoplasmic reticulum. Methods Enzymol.; 157: 46-50.
    • (1988) Methods Enzymol , vol.157 , pp. 46-50
    • Costello, B.1    Chadwick, C.2    Fleischer, S.3
  • 33
    • 0023159879 scopus 로고
    • 2+-ATPase in sarcoplasmic reticulum occurs without major changes in secondary structure
    • 2+-ATPase in sarcoplasmic reticulum occurs without major changes in secondary structure. Biochem J.; 241: 663-9.
    • (1987) Biochem J , vol.241 , pp. 663-669
    • Csermely, P.1    Katopis, C.2    Wallace, B.A.3
  • 34
    • 0022270516 scopus 로고
    • 51V-nmr analysis of the binding of vanadium (V) oligoanions to sarcoplasmic reticulum
    • 51V-nmr analysis of the binding of vanadium (V) oligoanions to sarcoplasmic reticulum. Biochem J.; 230: 807-15.
    • (1985) Biochem J , vol.230 , pp. 807-815
    • Csermely, P.1    Martonosi, A.2    Levy, G.C.3    Ejchart, A.J.4
  • 38
    • 0027336605 scopus 로고
    • 2+ binding on the profile structure of the sarcoplasmic reticulum membrane using time resolved X-ray diffraction
    • 2+ binding on the profile structure of the sarcoplasmic reticulum membrane using time resolved X-ray diffraction. Biophys J.; 64: 1750-9.
    • (1993) Biophys J , vol.64 , pp. 1750-1759
    • DeLong, L.J.1    Blasie, J.K.2
  • 40
    • 0020580035 scopus 로고
    • 2+-ATPase vesicles treated with vanadate
    • 2+-ATPase vesicles treated with vanadate. J Biol Chem.; 258: 2599-603.
    • (1983) J Biol Chem , vol.258 , pp. 2599-2603
    • Dux, L.1    Martonosi, A.2
  • 41
    • 0021112409 scopus 로고
    • 2+-ATPase membrane crystals in sarcoplasmic reticulum. The effect of trypsin digestion
    • 2+-ATPase membrane crystals in sarcoplasmic reticulum. The effect of trypsin digestion. J Biol Chem.; 258: 10111-5.
    • (1983) J Biol Chem , vol.258 , pp. 10111-10115
    • Dux, L.1    Martonosi, A.2
  • 42
    • 0021100167 scopus 로고
    • 2+, ATP and inorganic phosphate
    • 2+, ATP and inorganic phosphate. J Biol Chem.; 258: 11896-902.
    • (1983) J Biol Chem , vol.258 , pp. 11896-11902
    • Dux, L.1    Martonosi, A.2
  • 43
    • 0021100155 scopus 로고
    • The regulation of ATPase-ATPase interactions in sarcoplasmic reticulum membranes II. The influence of membrane potential
    • Dux L, Martonosi A. (1983d) The regulation of ATPase-ATPase interactions in sarcoplasmic reticulum membranes II. The influence of membrane potential. J Biol Chem.; 258: 11903-7.
    • (1983) J Biol Chem , vol.258 , pp. 11903-11907
    • Dux, L.1    Martonosi, A.2
  • 44
    • 0021288256 scopus 로고
    • 2+-ATPase in sarcoplasmic reticulum of fast and slow skeletal and cardiac muscles
    • 2+-ATPase in sarcoplasmic reticulum of fast and slow skeletal and cardiac muscles. Eur J Biochem.; 141: 43-9.
    • (1984) Eur J Biochem , vol.141 , pp. 43-49
    • Dux, L.1    Martonosi, A.2
  • 48
    • 73049137785 scopus 로고
    • Calcium binding activity of vesicular relaxing factor
    • Ebashi S. (1961) Calcium binding activity of vesicular relaxing factor. J Biochem.; 50: 236-44.
    • (1961) J Biochem , vol.50 , pp. 236-244
    • Ebashi, S.1
  • 49
    • 84968965880 scopus 로고
    • Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle
    • Ebashi S, Lipmann F. (1962) Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J Cell Biol.; 14: 389-400.
    • (1962) J Cell Biol , vol.14 , pp. 389-400
    • Ebashi, S.1    Lipmann, F.2
  • 52
    • 0029075071 scopus 로고
    • Subcellular targeting of the endoplasmic reticulum and plasma membrane calcium pumps: A study using recombinant chimeras
    • Foletti D, Guerini D, Carafoli E. (1995) Subcellular targeting of the endoplasmic reticulum and plasma membrane calcium pumps: a study using recombinant chimeras. FASEB J.; 9: 670-80.
    • (1995) FASEB J , vol.9 , pp. 670-680
    • Foletti, D.1    Guerini, D.2    Carafoli, E.3
  • 54
    • 0022271368 scopus 로고
    • 2+ ATPase in sarcoplasmic reticulum membrane as determined by shadowing techniques
    • 2+ ATPase in sarcoplasmic reticulum membrane as determined by shadowing techniques. Biophys J.; 48: 607-15.
    • (1985) Biophys J , vol.48 , pp. 607-615
    • Franzini-Armstrong, C.1    Ferguson, D.G.2
  • 55
    • 0024457801 scopus 로고
    • 2+-ATPase using terbium formycin triphosphate as an analogue of Mg-ATP
    • 2+-ATPase using terbium formycin triphosphate as an analogue of Mg-ATP. Eur J Biochem.; 184: 131-40.
    • (1989) Eur J Biochem , vol.184 , pp. 131-140
    • Girardet, J.-L.1    Dupont, Y.2    Lacapere, J.J.3
  • 56
    • 0036196950 scopus 로고    scopus 로고
    • A hundred years of sodium pumping
    • Glynn IM. (2002) A hundred years of sodium pumping. Annu Rev Physiol.; 64: 1-18.
    • (2002) Annu Rev Physiol , vol.64 , pp. 1-18
    • Glynn, I.M.1
  • 57
    • 0037043686 scopus 로고    scopus 로고
    • Calcium callisthenics
    • Green NM, MacLennan DH. (2002) Calcium callisthenics. Nature.; 418: 598-99.
    • (2002) Nature , vol.418 , pp. 598-599
    • Green, N.M.1    MacLennan, D.H.2
  • 58
    • 0026707393 scopus 로고
    • Structural modelling of P-type ion pumps
    • Green NM, Stokes DL. (1992) Structural modelling of P-type ion pumps. Acta Physiol Scand (Suppl.).; 146 (607): 59-68.
    • (1992) Acta Physiol Scand (Suppl.) , vol.146 , Issue.607 , pp. 59-68
    • Green, N.M.1    Stokes, D.L.2
  • 59
    • 0023819315 scopus 로고
    • 2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site
    • 2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site. J Biol Chem.; 263: 15032-40.
    • (1988) J Biol Chem , vol.263 , pp. 15032-15040
    • Gunteski-Humblin, A.-M.1    Greeb, J.2    Shull, G.E.3
  • 61
    • 72949126637 scopus 로고
    • Die calciumpumpe der "Erschlaffungsgrana" des muskels und ihre abhängigkeit von der ATP-spaltung
    • Hasselbach W, Makinose M. (1961) Die calciumpumpe der "Erschlaffungsgrana" des muskels und ihre abhängigkeit von der ATP-spaltung. Biochem Z.; 333: 518-28.
    • (1961) Biochem Z , vol.333 , pp. 518-528
    • Hasselbach, W.1    Makinose, M.2
  • 62
    • 78651121430 scopus 로고
    • Über den mechanismus des calciumtransportes durch die membranen des sarkoplasmatischen reticulums
    • Hasselbach W, Makinose M. (1963) Über den mechanismus des calciumtransportes durch die membranen des sarkoplasmatischen reticulums. Biochem Z.; 339: 94-111.
    • (1963) Biochem Z , vol.339 , pp. 94-111
    • Hasselbach, W.1    Makinose, M.2
  • 63
    • 0035976792 scopus 로고    scopus 로고
    • Three-dimensional structure of renal Na-K-ATPase from cryo-electron microscopy of two-dimensional crystals
    • Hebert H, Purhonen P, Vorum H, Thomsen K, Maunsbach AB. (2001) Three-dimensional structure of renal Na-K-ATPase from cryo-electron microscopy of two-dimensional crystals. J Mol Biol.; 314: 479-94.
    • (2001) J Mol Biol , vol.314 , pp. 479-494
    • Hebert, H.1    Purhonen, P.2    Vorum, H.3    Thomsen, K.4    Maunsbach, A.B.5
  • 64
  • 65
    • 0022254305 scopus 로고
    • The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffraction
    • Herbette L, DeFoor P, Fleischer S, Pascolini D, Scarpa A, Blasie JK. (1985) The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffraction. Biochim Biophys Acta.; 817: 103-22.
    • (1985) Biochim Biophys Acta , vol.817 , pp. 103-122
    • Herbette, L.1    DeFoor, P.2    Fleischer, S.3    Pascolini, D.4    Scarpa, A.5    Blasie, J.K.6
  • 66
    • 0021099585 scopus 로고
    • 2+ binding sites on sarcoplasmic reticulum ATPase
    • 2+ binding sites on sarcoplasmic reticulum ATPase. J Biol Chem.; 258: 6858-62.
    • (1983) J Biol Chem , vol.258 , pp. 6858-6862
    • Highsmith, S.R.1    Head, M.R.2
  • 67
    • 0034730656 scopus 로고    scopus 로고
    • Distinct topologies of mono- and decavanadate binding and photooxidative cleavage in the sarcoplasmic reticulum ATPase
    • Hua S, Inesi G, Toyoshima C. (2000) Distinct topologies of mono- and decavanadate binding and photooxidative cleavage in the sarcoplasmic reticulum ATPase. J Biol Chem.; 275: 30546-50.
    • (2000) J Biol Chem , vol.275 , pp. 30546-30550
    • Hua, S.1    Inesi, G.2    Toyoshima, C.3
  • 68
    • 0012050077 scopus 로고
    • Tryptic digestion and localization of calcium uptake and ATPase activity in fragments of sarcoplasmic reticulum
    • Ikemoto N, Sreter FA, Nakamura A, Gergely J (1968) Tryptic digestion and localization of calcium uptake and ATPase activity in fragments of sarcoplasmic reticulum. J Ultrastructure Res.; 23: 216-32.
    • (1968) J Ultrastructure Res , vol.23 , pp. 216-232
    • Ikemoto, N.1    Sreter, F.A.2    Nakamura, A.3    Gergely, J.4
  • 69
    • 0021421122 scopus 로고
    • 2+ and adenyl-5′-yl-imidodiphosphate as detected by trypsin sensitivity analysis
    • 2+ and adenyl-5′ -yl-imidodiphosphate as detected by trypsin sensitivity analysis. J Biochem.; 95: 1305-13.
    • (1984) J Biochem , vol.95 , pp. 1305-1313
    • Imamura, Y.1    Saito, K.2    Kawakita, M.3
  • 70
    • 0027198546 scopus 로고
    • Calcium ATPase of sarcoplasmic reticulum has four binding sites for calcium
    • Jencks WP, Yang T, Peisach D, Myung J. (1993) Calcium ATPase of sarcoplasmic reticulum has four binding sites for calcium. Biochemistry.; 32: 7030-4.
    • (1993) Biochemistry , vol.32 , pp. 7030-7034
    • Jencks, W.P.1    Yang, T.2    Peisach, D.3    Myung, J.4
  • 72
    • 0022465303 scopus 로고
    • 2+ transport ATPase in sarcoplasmic reticulum
    • 2+ transport ATPase in sarcoplasmic reticulum. Biochem J.; 234: 363-71.
    • (1986) Biochem J , vol.234 , pp. 363-371
    • Jona, I.1    Martonosi, A.2
  • 75
    • 0026775405 scopus 로고
    • 2+-ATPase SERCA1a contains endoplasmic reticulum targeting information
    • 2+-ATPase SERCA1a contains endoplasmic reticulum targeting information. Biochem Biophys Res Commun.; 186: 219-27.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 219-227
    • Karin, N.J.1    Settle, V.J.2
  • 80
    • 0036727524 scopus 로고    scopus 로고
    • A P-type ion pump at work
    • Lancaster CRD. (2002) A P-type ion pump at work. Nat Struct Biol.; 9: 643-5.
    • (2002) Nat Struct Biol , vol.9 , pp. 643-645
    • Lancaster, C.R.D.1
  • 81
    • 0035875164 scopus 로고    scopus 로고
    • What the structure of a calcium pump tells us about its mechanism?
    • Lee AG, East M. (2001) What the structure of a calcium pump tells us about its mechanism? Biochem J.; 356: 665-83.
    • (2001) Biochem J , vol.356 , pp. 665-683
    • Lee, A.G.1    East, M.2
  • 82
    • 0037063730 scopus 로고    scopus 로고
    • 2+-ATPase structure in the E1 and E2 conformations: Mechanism, helix-helix and helix-lipid interactions
    • 2+-ATPase structure in the E1 and E2 conformations: mechanism, helix-helix and helix-lipid interactions. Biochim Biophys Acta.; 1565: 246-66.
    • (2002) Biochim Biophys Acta , vol.1565 , pp. 246-266
    • Lee, A.G.1
  • 84
    • 0026691835 scopus 로고
    • Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps
    • Lytton J, Westlin M, Burk SE, Shull GE, MacLennan DH. (1992) Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps. J Biol Chem.; 267: 14483-9.
    • (1992) J Biol Chem , vol.267 , pp. 14483-14489
    • Lytton, J.1    Westlin, M.2    Burk, S.E.3    Shull, G.E.4    MacLennan, D.H.5
  • 86
    • 0033624484 scopus 로고    scopus 로고
    • 2+ signalling and muscle disease
    • 2+ signalling and muscle disease. Eur J Biochem.; 267: 5291-7.
    • (2000) Eur J Biochem , vol.267 , pp. 5291-5297
    • MacLennan, D.H.1
  • 88
    • 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: 696-700.
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Korczak, B.3    Green, N.M.4
  • 92
    • 0014410980 scopus 로고
    • Sarcoplasmic reticulum V. The structure of sarcoplasmic reticulum membrane
    • Martonosi A. (1968) Sarcoplasmic reticulum V. The structure of sarcoplasmic reticulum membrane. Biochim Biophys Acta.; 150: 694-704.
    • (1968) Biochim Biophys Acta , vol.150 , pp. 694-704
    • Martonosi, A.1
  • 93
    • 77956813361 scopus 로고
    • 2+ transport ATPases of sarco(endo)plasmic reticulum and plasma membrane
    • de Pont JJHHM. ed. Amsterdam, Elsevier
    • 2+ transport ATPases of sarco(endo)plasmic reticulum and plasma membrane. In Molecular aspects of transport proteins. de Pont JJHHM. ed., pp 57-116. Amsterdam, Elsevier.
    • (1992) Molecular Aspects of Transport Proteins , pp. 57-116
    • Martonosi, A.1
  • 96
    • 0042008053 scopus 로고    scopus 로고
    • The network of calcium regulation in muscle
    • Martonosi A, Pikula S. (2003) The network of calcium regulation in muscle. Acta Biochim Polon.; 50: 1-29.
    • (2003) Acta Biochim Polon , vol.50 , pp. 1-29
    • Martonosi, A.1    Pikula, S.2
  • 98
    • 77956737449 scopus 로고    scopus 로고
    • The ATP binding sites of P-type ion transport ATPases: Properties, structure, conformations, and mechanism of coupling
    • McIntosh DB. (1998) The ATP binding sites of P-type ion transport ATPases: properties, structure, conformations, and mechanism of coupling. Adv Mol Cell Biol.; 23A: 33-99.
    • (1998) Adv Mol Cell Biol , vol.23 A , pp. 33-99
    • McIntosh, D.B.1
  • 100
    • 0033932608 scopus 로고    scopus 로고
    • Portrait of a P-type pump
    • McIntosh DB. (2000) Portrait of a P-type pump. Nat Struct Biol.; 7: 532-5.
    • (2000) Nat Struct Biol , vol.7 , pp. 532-535
    • McIntosh, D.B.1
  • 104
    • 0026584967 scopus 로고
    • Simultaneous internalization and binding of calcium during the initial phase of calcium uptake by the sarcoplasmic reticulum Ca pump
    • Meszaros LG, Bak JZ. (1992) Simultaneous internalization and binding of calcium during the initial phase of calcium uptake by the sarcoplasmic reticulum Ca pump. Biochemistry.; 31: 1195-200.
    • (1992) Biochemistry , vol.31 , pp. 1195-1200
    • Meszaros, L.G.1    Bak, J.Z.2
  • 105
    • 0027371188 scopus 로고
    • +-binding sites of the sarcoplasmic reticulum calcium pump
    • +-binding sites of the sarcoplasmic reticulum calcium pump. Biochemistry.; 32: 10085-8.
    • (1993) Biochemistry , vol.32 , pp. 10085-10088
    • Meszaros, L.G.1    Bak, J.Z.2
  • 106
    • 85143328503 scopus 로고
    • General and practical aspects of membrane protein crystallization
    • Michel H. ed. Boca Raton, CRC Press
    • Michel H. (1990) General and practical aspects of membrane protein crystallization. In Crystallization of membrane proteins. Michel H. ed., pp 73-88. Boca Raton, CRC Press.
    • (1990) Crystallization of Membrane Proteins , pp. 73-88
    • Michel, H.1
  • 107
    • 0031574613 scopus 로고    scopus 로고
    • 2+ transport by the sarcoplasmic reticulum ATPase
    • 2+ transport by the sarcoplasmic reticulum ATPase. Biochim Biophys Acta.; 1318: 52-70.
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 52-70
    • Mintz, E.1    Guillain, F.2
  • 110
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport and energy transduction of P type ATPases
    • Moller JV, Juul B, leMaire M. (1996) Structural organization, ion transport and energy transduction of P type ATPases. Biochim Biophys Acta.; 1286: 1-51.
    • (1996) Biochim Biophys Acta , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    LeMaire, M.3
  • 111
    • 0025734090 scopus 로고
    • Differences in the susceptibility of various cation transport ATPases to vanadate catalysed photocleavage
    • Molnar E, Varga S, Martonosi A. (1991) Differences in the susceptibility of various cation transport ATPases to vanadate catalysed photocleavage. Biochim Biophys Acta.; 1068: 17-26.
    • (1991) Biochim Biophys Acta , vol.1068 , pp. 17-26
    • Molnar, E.1    Varga, S.2    Martonosi, A.3
  • 114
    • 0025148986 scopus 로고
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum. J Cell Sci.; 97: 487-95.
    • (1990) J Cell Sci , vol.97 , pp. 487-495
    • Murakami, K.1    Tanabe, K.2    Takada, S.3
  • 115
    • 0028145053 scopus 로고
    • Lumenal and cytoplasmic binding sites for calcium on the calcium ATPase of sarcoplasmic reticulum are different and independent
    • Myung J, Jencks WP. (1994) Lumenal and cytoplasmic binding sites for calcium on the calcium ATPase of sarcoplasmic reticulum are different and independent. Biochemistry.; 33: 8775-85.
    • (1994) Biochemistry , vol.33 , pp. 8775-8785
    • Myung, J.1    Jencks, W.P.2
  • 116
    • 0028929927 scopus 로고
    • There is only one phosphoenzyme intermediate with bound calcium on the reaction pathway of the sarcoplasmic reticulum calcium ATPase
    • Myung J, Jencks WP. (1995) There is only one phosphoenzyme intermediate with bound calcium on the reaction pathway of the sarcoplasmic reticulum calcium ATPase. Biochemistry.; 34: 3077-83.
    • (1995) Biochemistry , vol.34 , pp. 3077-3083
    • Myung, J.1    Jencks, W.P.2
  • 117
    • 0037908635 scopus 로고    scopus 로고
    • Sarco/endoplasmic-reticulum calcium ATPase SERCA1 is maintained in the endoplasmic reticulum by a retrieval signal located between residues 1 and 211
    • Newton T, Black JP, Butler J, Lee AG, Chad J, East JM. (2003) Sarco/endoplasmic-reticulum calcium ATPase SERCA1 is maintained in the endoplasmic reticulum by a retrieval signal located between residues 1 and 211. Biochem J.; 371: 775-82.
    • (2003) Biochem J , vol.371 , pp. 775-782
    • Newton, T.1    Black, J.P.2    Butler, J.3    Lee, A.G.4    Chad, J.5    East, J.M.6
  • 118
    • 0031595675 scopus 로고    scopus 로고
    • 2+-pump of sarcoplasmic reticulum: A view along the lipid bilayer at 9 Å resolution
    • 2+-pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9 Å resolution. Biophys J.; 75: 41-52.
    • (1998) Biophys J , vol.75 , pp. 41-52
    • Ogawa, H.1    Stokes, D.L.2    Sasabe, H.3    Toyoshima, C.4
  • 120
  • 121
    • 0042494333 scopus 로고
    • 2+ transport ATPases isolated from sarcoplasmic reticulum of rabbit, chicken and lobster muscle
    • 2+ transport ATPases isolated from sarcoplasmic reticulum of rabbit, chicken and lobster muscle. Comp Biochem Physiol B.; 65: 181-9.
    • (1980) Comp Biochem Physiol B , vol.65 , pp. 181-189
    • Ohnoki, S.1    Martonosi, A.2
  • 122
    • 0024819294 scopus 로고
    • Complementary DNA cloning of a protein highly homologous to mammalian sarcoplasmic reticulum Ca-ATPase from the crustacean Artemia
    • Palmero I, Sastre L. (1989) Complementary DNA cloning of a protein highly homologous to mammalian sarcoplasmic reticulum Ca-ATPase from the crustacean Artemia. J Mol Biol.; 210: 737-48.
    • (1989) J Mol Biol , vol.210 , pp. 737-748
    • Palmero, I.1    Sastre, L.2
  • 123
    • 0023153758 scopus 로고
    • 2+-ATPase interactions in sarcoplasmic reticulum
    • 2+-ATPase interactions in sarcoplasmic reticulum. Biophys J.; 51: 205-20.
    • (1987) Biophys J , vol.51 , pp. 205-220
    • Papp, S.1    Pikula, S.2    Martonosi, A.3
  • 126
    • 0002251849 scopus 로고
    • Structure and function of membrane systems of skeletal muscle cells
    • Peachey LD, Adrian RH, eds. Bethesda, American Physiological Society
    • Peachey LD, Franzini-Armstrong C. (1983) Structure and function of membrane systems of skeletal muscle cells. In Handbook of physiology, Section 10, Skeletal Muscle. Peachey LD, Adrian RH, eds, pp 23-71. Bethesda, American Physiological Society.
    • (1983) Handbook of Physiology, Section 10, Skeletal Muscle , pp. 23-71
    • Peachey, L.D.1    Franzini-Armstrong, C.2
  • 127
    • 0021616826 scopus 로고
    • Crystallization of intramembrane particles in rabbit sarcoplasmic reticulum vesicles by vanadate
    • Peracchia C, Dux L, Martonosi A. (1984) Crystallization of intramembrane particles in rabbit sarcoplasmic reticulum vesicles by vanadate. J Muscle Res Cell Motil.; 5: 431-42.
    • (1984) J Muscle Res Cell Motil , vol.5 , pp. 431-442
    • Peracchia, C.1    Dux, L.2    Martonosi, A.3
  • 128
    • 0019731183 scopus 로고
    • 2+ ATPase from sarcoplasmic reticulum
    • 2+ ATPase from sarcoplasmic reticulum. Eur J Biochem.; 121: 187-195.
    • (1981) Eur J Biochem , vol.121 , pp. 187-195
    • Pick, U.1
  • 135
    • 0032545098 scopus 로고    scopus 로고
    • 2+ ATPase from sarcoplasmic reticulum: Merging electron diffraction tilt series and imaging the (h, k, o) projection
    • 2+ ATPase from sarcoplasmic reticulum: merging electron diffraction tilt series and imaging the (h, k, o) projection. J Mol Biol.; 284: 1547-64.
    • (1998) J Mol Biol , vol.284 , pp. 1547-1564
    • Shi, D.1    Lewis, M.R.2    Young, H.S.3    Stokes, D.L.4
  • 138
    • 0025344903 scopus 로고
    • Structure of CaATPase: Electron microscopy of frozen-hydrated crystals at 6 Å resolution in projection
    • Stokes DL, Green NM. (1990a) Structure of CaATPase: electron microscopy of frozen-hydrated crystals at 6 Å resolution in projection. J Mol Biol.; 213: 529-38.
    • (1990) J Mol Biol , vol.213 , pp. 529-538
    • Stokes, D.L.1    Green, N.M.2
  • 139
    • 0025019294 scopus 로고
    • Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing
    • Stokes DL, Green NM. (1990b) Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing. Biophys J.; 57: 1-14.
    • (1990) Biophys J , vol.57 , pp. 1-14
    • Stokes, D.L.1    Green, N.M.2
  • 140
    • 0034033869 scopus 로고    scopus 로고
    • 2+-ATPase defines a new domain structure
    • 2+-ATPase defines a new domain structure. Biophys J.; 78: 1765-76.
    • (2000) Biophys J , vol.78 , pp. 1765-1776
    • Stokes, D.L.1    Green, N.M.2
  • 141
    • 0028179410 scopus 로고
    • 2+, thapsigargin, adenosine-5′(β,γ methylene) triphosphate and chromium (III)-ATP on crystallization
    • 2+, thapsigargin, adenosine-5′(β,γ methylene) triphosphate and chromium (III) -ATP on crystallization. J Biol Chem.; 269: 11606-13.
    • (1994) J Biol Chem , vol.269 , pp. 11606-11613
    • Stokes, D.L.1    Lacapere, J.-J.2
  • 142
    • 0035875154 scopus 로고    scopus 로고
    • 2+-ATPase of the sarcoplasmic reticulum
    • 2+-ATPase of the sarcoplasmic reticulum. Biochem J.; 356: 685-704.
    • (2001) Biochem J , vol.356 , pp. 685-704
    • Sweadner, K.J.1    Donnet, C.2
  • 148
    • 0028360739 scopus 로고
    • 2+-ATPase from skeletal muscle sarcoplasmic reticulum
    • 2+-ATPase from skeletal muscle sarcoplasmic reticulum. J Biol Chem.; 269: 10107-11.
    • (1994) J Biol Chem , vol.269 , pp. 10107-10111
    • Taylor, K.A.1    Varga, S.2
  • 149
    • 0015973647 scopus 로고
    • The ultrastructure of developing sarcoplasmic reticulum
    • Tillack TW, Boland R, Martonosi A. (1974) The ultrastructure of developing sarcoplasmic reticulum. J Biol Chem.; 249: 624-33.
    • (1974) J Biol Chem , vol.249 , pp. 624-633
    • Tillack, T.W.1    Boland, R.2    Martonosi, A.3
  • 151
    • 0017367579 scopus 로고
    • 2 terminal acetylated methionyl sequence
    • 2 terminal acetylated methionyl sequence. Biochem Biophys Res Commun.; 74: 1242-8.
    • (1977) Biochem Biophys Res Commun , vol.74 , pp. 1242-1248
    • Tong, S.W.1
  • 152
    • 0019062272 scopus 로고
    • Studies on the structure of the calcium-dependent adenosine triphosphatase from rabbit skeletal muscle sarcoplasmic reticulum
    • Tong SW. (1980) Studies on the structure of the calcium-dependent adenosine triphosphatase from rabbit skeletal muscle sarcoplasmic reticulum. Arch Biochem Biophys.; 203: 780-91.
    • (1980) Arch Biochem Biophys , vol.203 , pp. 780-791
    • Tong, S.W.1
  • 154
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Ĺ resolution
    • Toyoshima C, Nakasake M, Nomura H, Ogawa H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Ĺ resolution. Nature.; 405: 647-55.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasake, M.2    Nomura, H.3    Ogawa, H.4
  • 155
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C, Nomura H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium. Nature.; 418: 605-11.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 156
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • Toyoshima C, Sasabe H, Stokes DL. (1993) Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature.; 362: 469-71.
    • (1993) Nature , vol.362 , pp. 469-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 158
    • 0027793739 scopus 로고
    • +)-ATPase enzyme from pig kidney
    • +)-ATPase enzyme from pig kidney. Acta Physiol Hung., 81: 409-24.
    • (1993) Acta Physiol Hung , vol.81 , pp. 409-424
    • Varga, S.1
  • 159
    • 0028700954 scopus 로고
    • +)-ATPase enzyme from hog and rabbit stomachs
    • +)-ATPase enzyme from hog and rabbit stomachs. Acta Physiol Hung.; 82: 365-76.
    • (1994) Acta Physiol Hung , vol.82 , pp. 365-376
    • Varga, S.1
  • 160
    • 0021869073 scopus 로고
    • The binding of vanadium (V) oligoanions to sarcoplasmic reticulum
    • Varga S, Csermely P, Martonosi A. (1985) The binding of vanadium (V) oligoanions to sarcoplasmic reticulum. Eur J Biochem.; 148: 119-26.
    • (1985) Eur J Biochem , vol.148 , pp. 119-126
    • Varga, S.1    Csermely, P.2    Martonosi, A.3
  • 161
    • 0026641594 scopus 로고
    • Giant sarcoplasmic reticulum vesicles: A study of membrane morphogenesis
    • Varga S, Martonosi A. (1992) Giant sarcoplasmic reticulum vesicles: a study of membrane morphogenesis. J Muscle Res Cell Motil.; 13: 497-510.
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 497-510
    • Varga, S.1    Martonosi, A.2
  • 165
    • 0029591698 scopus 로고
    • Modulation of SERCA2 activity: Regulated splicing and interaction with phospholamban
    • Verboomen H, Mertens L, Eggermont J, Wuytack F, Van Den Bosch L. (1995) Modulation of SERCA2 activity: regulated splicing and interaction with phospholamban. Biosci Rep.; 15: 307-15.
    • (1995) Biosci Rep , vol.15 , pp. 307-315
    • Verboomen, H.1    Mertens, L.2    Eggermont, J.3    Wuytack, F.4    Van Den Bosch, L.5
  • 166
    • 0028814227 scopus 로고
    • +-ATPase
    • +-ATPase. Acta Physiol Scand.; 154:Suppl 624, 1-146.
    • (1995) Acta Physiol Scand , vol.154 , Issue.624 SUPPL. , pp. 1-146
    • Vilsen, B.1
  • 168
    • 0001533582 scopus 로고
    • On the role of calcium in the activity of adenosine-5′ -triphosphate hydrolysis by actomyosin
    • Weber A. (1959) On the role of calcium in the activity of adenosine-5′-triphosphate hydrolysis by actomyosin. J Biol Chem.; 234: 2764-9.
    • (1959) J Biol Chem , vol.234 , pp. 2764-2769
    • Weber, A.1
  • 169
    • 0009845746 scopus 로고
    • The regulation of myofibrillar activity by calcium
    • Weber A, Herz R, Reiss I. (1964) The regulation of myofibrillar activity by calcium. Proc Roy Soc London Series B.; 160: 489-501.
    • (1964) Proc Roy Soc London Series B , vol.160 , pp. 489-501
    • Weber, A.1    Herz, R.2    Reiss, I.3
  • 173
    • 0024823960 scopus 로고
    • 2+ transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosinne triphosphopyridoxal
    • 2+ transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosinne triphosphopyridoxal. J Biochem.; 106: 1121-5.
    • (1989) J Biochem , vol.106 , pp. 1121-1125
    • Yamamoto, H.1    Imamura, Y.2    Tagaya, M.3    Fukui, T.4    Kawakita, M.5
  • 179
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8 resolution
    • Zhang P, Toyoshima C, Yonekura K, Green NM, Stokes DL. (1998) Structure of the calcium pump from sarcoplasmic reticulum at 8 resolution. Nature.; 392: 835-9.
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.M.4    Stokes, D.L.5


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