메뉴 건너뛰기




Volumn 34, Issue 8, 2002, Pages 897-918

Structure-function relationships in Ca2+ cycling proteins

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL L TYPE; CALMODULIN; CALSEQUESTRIN; CARRIER PROTEIN; PHOSPHOLAMBAN; POTASSIUM CHANNEL; SARCOLIPIN; SODIUM CALCIUM EXCHANGE PROTEIN; TROPONIN C; UNCLASSIFIED DRUG;

EID: 0036702524     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmcc.2002.2031     Document Type: Review
Times cited : (64)

References (144)
  • 2
    • 0029689693 scopus 로고    scopus 로고
    • Structural and functional diversity of voltage-activated calcium channels
    • De Waard M, Gurnett CA, Campbell KP. Structural and functional diversity of voltage-activated calcium channels. Ion Channels 1996; 4: 41-87.
    • (1996) Ion Channels , vol.4 , pp. 41-87
    • De Waard, M.1    Gurnett, C.A.2    Campbell, K.P.3
  • 4
    • 0030827670 scopus 로고    scopus 로고
    • Phosphorylation of the synaptic protein interaction site on N-type calcium channels inhibits interactions with SNARE proteins
    • Yokoyama CT, Sheng ZH, Catterall WA. Phosphorylation of the synaptic protein interaction site on N-type calcium channels inhibits interactions with SNARE proteins. J Neurosci 1997; 17: 6929-6938.
    • (1997) J Neurosci , vol.17 , pp. 6929-6938
    • Yokoyama, C.T.1    Sheng, Z.H.2    Catterall, W.A.3
  • 7
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou M, Morais-Cabral JH, Mann S, MacKinnon R. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature 2001; 411: 657-661.
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 10
    • 0035498849 scopus 로고    scopus 로고
    • See potassium run
    • Miller C. See potassium run. Nature 2001; 414: 23-24.
    • (2001) Nature , vol.414 , pp. 23-24
    • Miller, C.1
  • 13
    • 0015856482 scopus 로고
    • Voltage dependent charge movement of skeletal muscle: A possible step in excitation-contraction coupling
    • Schneider MF, Chandler WK. Voltage dependent charge movement of skeletal muscle: A possible step in excitation-contraction coupling. Nature 1973; 242: 244-246.
    • (1973) Nature , vol.242 , pp. 244-246
    • Schneider, M.F.1    Chandler, W.K.2
  • 14
    • 0028063942 scopus 로고
    • Critical roles of the S3 segment and S3-S4 linker of repeat I in activation of L-type calcium channels
    • Nakai J, Adams BA, Imoto K, Beam KG. Critical roles of the S3 segment and S3-S4 linker of repeat I in activation of L-type calcium channels. Proc Natl Acad Sci USA 1994; 91: 1014-1018.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1014-1018
    • Nakai, J.1    Adams, B.A.2    Imoto, K.3    Beam, K.G.4
  • 15
    • 0028080195 scopus 로고
    • Molecular determinants of voltage-dependent inactivation in calcium channels
    • Zhang JF, Ellinor PT, Aldrich RW, Tsien RW. Molecular determinants of voltage-dependent inactivation in calcium channels. Nature 1994; 372: 97-100.
    • (1994) Nature , vol.372 , pp. 97-100
    • Zhang, J.F.1    Ellinor, P.T.2    Aldrich, R.W.3    Tsien, R.W.4
  • 17
    • 0027197578 scopus 로고
    • 2+ channels due to phosphorylation by cAMP-dependent protein kinase
    • 2+ channels due to phosphorylation by cAMP-dependent protein kinase. Nature 1993; 364: 240-243.
    • (1993) Nature , vol.364 , pp. 240-243
    • Sculptoreanu, A.1    Scheuer, T.2    Catterall, W.A.3
  • 19
    • 0025356933 scopus 로고
    • Cardiac-type excitation-contraction coupling in dysgenic skeletal muscle injected with cardiac dihydropyridine receptor cDNA
    • Tanabe T, Mikami A, Numa S, Beam KG. Cardiac-type excitation-contraction coupling in dysgenic skeletal muscle injected with cardiac dihydropyridine receptor cDNA. Nature 1990; 344: 451-453.
    • (1990) Nature , vol.344 , pp. 451-453
    • Tanabe, T.1    Mikami, A.2    Numa, S.3    Beam, K.G.4
  • 20
    • 0025288735 scopus 로고
    • Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling
    • Tanabe T, Beam KG, Adams BA, Niidome T, Numa S. Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 1990; 346: 567-569.
    • (1990) Nature , vol.346 , pp. 567-569
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 21
    • 0028595727 scopus 로고
    • Identification of a syntaxin-binding site on N-type calcium channels
    • Sheng ZH, Rettig J, Takahashi M, Catterall WA. Identification of a syntaxin-binding site on N-type calcium channels. Neuron 1994; 13: 1303-1313.
    • (1994) Neuron , vol.13 , pp. 1303-1313
    • Sheng, Z.H.1    Rettig, J.2    Takahashi, M.3    Catterall, W.A.4
  • 22
    • 0030922550 scopus 로고    scopus 로고
    • Malignant-hyperthermia susceptibility is associated with a mutation of the alpha 1-subunit of the human dihydropyridine-sensitive L-type voltage-dependent calcium-channel receptor in skeletal muscle
    • Monnier N, Procaccio V, Stieglitz P, Lunardi J. Malignant-hyperthermia susceptibility is associated with a mutation of the alpha 1-subunit of the human dihydropyridine-sensitive L-type voltage-dependent calcium-channel receptor in skeletal muscle. Am J Hum Genet 1997; 60: 1316-1325.
    • (1997) Am J Hum Genet , vol.60 , pp. 1316-1325
    • Monnier, N.1    Procaccio, V.2    Stieglitz, P.3    Lunardi, J.4
  • 23
    • 0028168917 scopus 로고
    • 2+ channel regulation by a conserved beta subunit domain
    • 2+ channel regulation by a conserved beta subunit domain. Neuron 1994; 13: 495-503.
    • (1994) Neuron , vol.13 , pp. 495-503
    • De Waard, M.1    Pragnell, M.2    Campbell, K.P.3
  • 24
    • 0028233952 scopus 로고
    • Structural basis of ion channel permeation and selectivity
    • Sather WA, Yang J, Tsien RW. Structural basis of ion channel permeation and selectivity. Curr Opin Neurobiol 1994; 4: 313-323.
    • (1994) Curr Opin Neurobiol , vol.4 , pp. 313-323
    • Sather, W.A.1    Yang, J.2    Tsien, R.W.3
  • 27
    • 0031830729 scopus 로고    scopus 로고
    • Contributions of electron microscopy and single-particle techniques to the determination of the ryanodine receptor three-dimensional structure
    • Samso M, Wagenknecht T. Contributions of electron microscopy and single-particle techniques to the determination of the ryanodine receptor three-dimensional structure. J Struct Biol 1998; 121: 172-180.
    • (1998) J Struct Biol , vol.121 , pp. 172-180
    • Samso, M.1    Wagenknecht, T.2
  • 30
    • 0028937373 scopus 로고
    • Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel
    • Serysheva, II, Orlova EV, Chiu W, Sherman MB, Hamilton SL, van Heel M. Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel. Nat Struct Biol 1995; 2: 18-24.
    • (1995) Nat Struct Biol , vol.2 , pp. 18-24
    • Serysheva II1    Orlova, E.V.2    Chiu, W.3    Sherman, M.B.4    Hamilton, S.L.5    Van Heel, M.6
  • 31
    • 0029153507 scopus 로고
    • Three-dimensional architecture of the skeletal muscle ryanodine receptor
    • Wagenknecht T, Radermacher M. Three-dimensional architecture of the skeletal muscle ryanodine receptor. FEBS Lett 1995; 369: 43-46.
    • (1995) FEBS Lett , vol.369 , pp. 43-46
    • Wagenknecht, T.1    Radermacher, M.2
  • 32
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • Radermacher M, Rao V, Grassucci R, Frank J, Timerman AP, Fleischer S, Wagenknecht T. Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J Cell Biol 1994; 127: 411-423.
    • (1994) J Cell Biol , vol.127 , pp. 411-423
    • Radermacher, M.1    Rao, V.2    Grassucci, R.3    Frank, J.4    Timerman, A.P.5    Fleischer, S.6    Wagenknecht, T.7
  • 33
    • 0031464972 scopus 로고    scopus 로고
    • Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor
    • Wagenknecht T, Radermacher M, Grassucci R, Berkowitz J, Xin HB, Fleischer S. Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor. J Biol Chem 1997; 272: 32463-32471.
    • (1997) J Biol Chem , vol.272 , pp. 32463-32471
    • Wagenknecht, T.1    Radermacher, M.2    Grassucci, R.3    Berkowitz, J.4    Xin, H.B.5    Fleischer, S.6
  • 36
    • 0034049351 scopus 로고    scopus 로고
    • Amino acid residues 4425-4621 localized on the three-dimensional structure of the skeletal muscle ryanodine receptor
    • Benacquista BL, Sharma MR, Samso M, Zorzato F, Treves S, Wagenknecht T. Amino acid residues 4425-4621 localized on the three-dimensional structure of the skeletal muscle ryanodine receptor. Biophys J 2000; 78: 1349-1358.
    • (2000) Biophys J , vol.78 , pp. 1349-1358
    • Benacquista, B.L.1    Sharma, M.R.2    Samso, M.3    Zorzato, F.4    Treves, S.5    Wagenknecht, T.6
  • 37
    • 0035932955 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus
    • Liu Z, Zhang J, Sharma MR, Li P, Chen SR, Wagenknecht T. Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus. Proc Natl Acad Sci USA 2001; 98: 6104-6109.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6104-6109
    • Liu, Z.1    Zhang, J.2    Sharma, M.R.3    Li, P.4    Chen, S.R.5    Wagenknecht, T.6
  • 39
  • 40
    • 0033543667 scopus 로고    scopus 로고
    • Molecular identification of the ryanodine receptor pore-forming segment
    • Zhao M, Li P, Li X, Zhang L, Winkfein RJ, Chen SR. Molecular identification of the ryanodine receptor pore-forming segment. J Biol Chem 1999; 274: 25971-25974.
    • (1999) J Biol Chem , vol.274 , pp. 25971-25974
    • Zhao, M.1    Li, P.2    Li, X.3    Zhang, L.4    Winkfein, R.J.5    Chen, S.R.6
  • 43
    • 0026562518 scopus 로고
    • Mapping of the calpain proteolysis products of the junctional foot protein of the skeletal muscle triad junction
    • Brandt NR, Caswell AH, Brandt T, Brew K, Mellgren RL. Mapping of the calpain proteolysis products of the junctional foot protein of the skeletal muscle triad junction. J Membr Biol 1992; 127: 35-47.
    • (1992) J Membr Biol , vol.127 , pp. 35-47
    • Brandt, N.R.1    Caswell, A.H.2    Brandt, T.3    Brew, K.4    Mellgren, R.L.5
  • 45
    • 0020580035 scopus 로고
    • 2+-ATPase vesicles treated with vanadate
    • 2+-ATPase vesicles treated with vanadate. J Biol Chem 1983; 258: 2599-2603.
    • (1983) J Biol Chem , vol.258 , pp. 2599-2603
    • Dux, L.1    Martonosi, A.2
  • 47
    • 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 1985; 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
  • 48
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution
    • Zhang P, Toyoshima C, Yonekura K, Green NM, Stokes DL. Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution. Nature 1998; 392: 835-839.
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.M.4    Stokes, D.L.5
  • 49
    • 0034033869 scopus 로고    scopus 로고
    • 2--ATPase defines a new domain structure
    • 2--ATPase defines a new domain structure. Biophys J 2000; 78: 1765-1776.
    • (2000) Biophys J , vol.78 , pp. 1765-1776
    • Stokes, D.L.1    Green, N.M.2
  • 52
    • 0029565489 scopus 로고
    • 2+-ATPase by site-directed mutagenesis
    • 2+-ATPase by site-directed mutagenesis. Biosci Rep 1995; 15: 243-261.
    • (1995) Biosci Rep , vol.15 , pp. 243-261
    • Andersen, J.P.1
  • 54
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A 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
  • 58
    • 0031595675 scopus 로고    scopus 로고
    • 2+ pump of sarcoplasmic reticulum: A view along the lipid bilayer at 9-A resolution
    • 2+ pump of sarcoplasmic reticulum: A view along the lipid bilayer at 9-A resolution. Biophys J 1998; 75: 41-52.
    • (1998) Biophys J , vol.75 , pp. 41-52
    • Ogawa, H.1    Stokes, D.L.2    Sasabe, H.3    Toyoshima, C.4
  • 59
    • 0023874795 scopus 로고
    • +- and other cation transport ATPases
    • +- and other cation transport ATPases. J Biol Chem 1988; 263: 8646-8657.
    • (1988) J Biol Chem , vol.263 , pp. 8646-8657
    • Shull, G.E.1    Greeb, J.2
  • 61
    • 0020000695 scopus 로고
    • 2+-H + exchange in reconstituted liposomal systems
    • 2+-H + exchange in reconstituted liposomal systems. J Biol Chem 1982; 257: 2350-2356.
    • (1982) J Biol Chem , vol.257 , pp. 2350-2356
    • Niggli, V.1    Sigel, E.2    Carafoli, E.3
  • 63
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler EE, Zacharias DA. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol Rev 2001; 81: 21-50.
    • (2001) Physiol Rev , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 66
    • 0027069575 scopus 로고
    • 2+ pump interacts with the transduction domain of the enzyme
    • 2+ pump interacts with the transduction domain of the enzyme. Protein Sci 1992; 1: 1613-1621.
    • (1992) Protein Sci , vol.1 , pp. 1613-1621
    • Falchetto, R.1    Vorherr, T.2    Carafoli, E.3
  • 69
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman HK, Jones LR. Phospholamban: Protein structure, mechanism of action, and role in cardiac function. Physiol Rev 1998; 78: 921-947.
    • (1998) Physiol Rev , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 70
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • Luo W, Grupp IL, Harrer J, Ponniah S, Grupp G, Duffy JJ, Doetschman T, Kranias EG. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res 1994; 75: 401-409.
    • (1994) Circ Res , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 72
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams PD, Arkin IT, Engelman DM, Brunger AT. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nat Struct Biol 1995; 2: 154-162.
    • (1995) Nat Struct Biol , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 74
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • Simmerman HK, Kobayashi YM, Autry JM, Jones LR. A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. J Biol Chem 1996; 271: 5941-5946.
    • (1996) J Biol Chem , vol.271 , pp. 5941-5946
    • Simmerman, H.K.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 75
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura Y, Kurzydlowski K, Tada M, MacLennan DH. Phospholamban inhibitory function is activated by depolymerization. J Biol Chem 1997; 272: 15061-15064.
    • (1997) J Biol Chem , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 76
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers
    • Cornea RL, Jones LR, Autry JM, Thomas DD. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry 1997; 36: 2960-2967.
    • (1997) Biochemistry , vol.36 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4
  • 77
    • 0033616627 scopus 로고    scopus 로고
    • Depolymerization of phospholamban in the presence of calcium pump: A fluorescence energy transfer study
    • Reddy LG, Jones LR, Thomas DD. Depolymerization of phospholamban in the presence of calcium pump: A fluorescence energy transfer study. Biochemistry 1999; 38: 3954-3962.
    • (1999) Biochemistry , vol.38 , pp. 3954-3962
    • Reddy, L.G.1    Jones, L.R.2    Thomas, D.D.3
  • 78
    • 0030905733 scopus 로고    scopus 로고
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation. J Biol Chem 1997; 272: 15872-15880.
    • (1997) J Biol Chem , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 80
    • 0033040491 scopus 로고    scopus 로고
    • Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer
    • Pollesello P, Annila A, Ovaska M. Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer. Biophys J 1999; 76: 1784-1795.
    • (1999) Biophys J , vol.76 , pp. 1784-1795
    • Pollesello, P.1    Annila, A.2    Ovaska, M.3
  • 82
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton DR, Zheng JH, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991; 253: 414-420.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 85
    • 0028168416 scopus 로고
    • 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban
    • 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J Biol Chem 1994; 269: 22929-22932.
    • (1994) J Biol Chem , vol.269 , pp. 22929-22932
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 86
    • 0032755399 scopus 로고    scopus 로고
    • 2+-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites
    • 2+-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites. J Biol Chem 1999; 274: 32855-32862.
    • (1999) J Biol Chem , vol.274 , pp. 32855-32862
    • Asahi, M.1    Kimura, Y.2    Kurzydlowski, K.3    Tada, M.4    MacLennan, D.H.5
  • 88
    • 0034901813 scopus 로고    scopus 로고
    • Locating phospholamban in co-crystals with Ca(2 +)-ATPase by cryoelectron microscopy
    • Young HS, Jones LR, Stokes DL. Locating phospholamban in co-crystals with Ca(2 +)-ATPase by cryoelectron microscopy. Biophys J 2001; 81: 884-894.
    • (2001) Biophys J , vol.81 , pp. 884-894
    • Young, H.S.1    Jones, L.R.2    Stokes, D.L.3
  • 89
    • 0000787574 scopus 로고
    • Isolation of sarcoplasmic reticulum proteins
    • eds. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • MacLennan DH, Yip CC, Iles GH, Seeman P. Isolation of sarcoplasmic reticulum proteins. In: (eds). The Mechanism of Muscle Contraction. Cold Spring Harbor: Cold Spring Harbor Laboratory Press. 1972: 469-478.
    • (1972) The Mechanism of Muscle Contraction , pp. 469-478
    • MacLennan, D.H.1    Yip, C.C.2    Iles, G.H.3    Seeman, P.4
  • 90
    • 0026450976 scopus 로고
    • Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide
    • Wawrzynow A, Theibert JL, Murphy C, Jona I, Martonosi A, Collins JH. Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide. Arch Biochem Biophys 1992; 298: 620-623.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 620-623
    • Wawrzynow, A.1    Theibert, J.L.2    Murphy, C.3    Jona, I.4    Martonosi, A.5    Collins, J.H.6
  • 93
    • 0034656175 scopus 로고    scopus 로고
    • Corticosteroids decrease mRNA levels of SERCA pumps, whereas they increase sarcolipin mRNA in the rat diaphragm
    • Gayan-Ramirez G, Vanzeir L, Wuytack F, Decramer M. Corticosteroids decrease mRNA levels of SERCA pumps, whereas they increase sarcolipin mRNA in the rat diaphragm. J Physiol 2000; 524(Pt 2): 387-397.
    • (2000) J Physiol , vol.524 , Issue.PART 2 , pp. 387-397
    • Gayan-Ramirez, G.1    Vanzeir, L.2    Wuytack, F.3    Decramer, M.4
  • 96
    • 0035903095 scopus 로고    scopus 로고
    • Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes
    • Hellstern S, Pegoraro S, Karim CB, Lustig A, Thomas DD, Moroder L, Engel J. Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes. J Biol Chem 2001; 276: 30845-30852.
    • (2001) J Biol Chem , vol.276 , pp. 30845-30852
    • Hellstern, S.1    Pegoraro, S.2    Karim, C.B.3    Lustig, A.4    Thomas, D.D.5    Moroder, L.6    Engel, J.7
  • 100
    • 0033852625 scopus 로고    scopus 로고
    • Sodium-calcium exchange: A molecular perspective
    • Philipson KD, Nicoll DA. Sodium-calcium exchange: A molecular perspective. Annu Rev Physiol 2000; 62: 111-133.
    • (2000) Annu Rev Physiol , vol.62 , pp. 111-133
    • Philipson, K.D.1    Nicoll, D.A.2
  • 102
    • 0027952387 scopus 로고
    • Interaction of cardiac Na-Ca exchanger and exchange inhibitory peptide with membrane phospholipids
    • Shannon TR, Hale CC, Milanick MA. Interaction of cardiac Na-Ca exchanger and exchange inhibitory peptide with membrane phospholipids. Am J Physiol 1994; 266: C1350-C1356.
    • (1994) Am J Physiol , vol.266
    • Shannon, T.R.1    Hale, C.C.2    Milanick, M.A.3
  • 104
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman LS. Thin filament-mediated regulation of cardiac contraction. Annu Rev Physiol 1996; 58: 447-481.
    • (1996) Annu Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 105
    • 0034625062 scopus 로고    scopus 로고
    • Bepridil opens the regulatory N-terminal lobe of cardiac troponin C
    • Li Y, Love ML, Putkey JA, Cohen C. Bepridil opens the regulatory N-terminal lobe of cardiac troponin C. Proc Natl Acad Sci USA 2000; 97: 5140-5145.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5140-5145
    • Li, Y.1    Love, M.L.2    Putkey, J.A.3    Cohen, C.4
  • 106
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips GN Jr, Fillers JP, Cohen C. Tropomyosin crystal structure and muscle regulation. J Mol Biol 1986; 192: 111-131.
    • (1986) J Mol Biol , vol.192 , pp. 111-131
    • Phillips G.N., Jr.1    Fillers, J.P.2    Cohen, C.3
  • 107
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire JM, Morris EP. A new look at thin filament regulation in vertebrate skeletal muscle. Faseb J 1998; 12: 761-771.
    • (1998) Faseb J , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 109
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg O, James MN. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature 1985; 313: 653-659.
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.2
  • 110
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution
    • Herzberg O, James MN. Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution. J Mol Biol 1988; 203: 761-779.
    • (1988) J Mol Biol , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.2
  • 111
    • 0023947009 scopus 로고
    • Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution
    • Satyshur KA, Rao ST, Pyzalska D, Drendel W, Greaser M, Sundaralingam M. Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution. J Biol Chem 1988; 263: 1628-1647.
    • (1988) J Biol Chem , vol.263 , pp. 1628-1647
    • Satyshur, K.A.1    Rao, S.T.2    Pyzalska, D.3    Drendel, W.4    Greaser, M.5    Sundaralingam, M.6
  • 113
    • 0028181768 scopus 로고
    • Solution structure of the TR1C fragment of skeletal muscle troponin-C
    • Findlay WA, Sonnichsen FD, Sykes BD. Solution structure of the TR1C fragment of skeletal muscle troponin-C. J Biol Chem 1994; 269: 6773-6778.
    • (1994) J Biol Chem , vol.269 , pp. 6773-6778
    • Findlay, W.A.1    Sonnichsen, F.D.2    Sykes, B.D.3
  • 114
    • 0020000247 scopus 로고
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J Biol Chem 1982; 257: 7678-7683.
    • (1982) J Biol Chem , vol.257 , pp. 7678-7683
    • Zot, H.G.1    Potter, J.D.2
  • 116
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky CM, Sykes BD. NMR solution structure of calcium-saturated skeletal muscle troponin C, Biochemistry 1995; 34: 15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 118
    • 0030936958 scopus 로고    scopus 로고
    • Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins
    • Gagne SM, Li MX, Sykes BD. Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins. Biochemistry 1997; 36: 4386-4392.
    • (1997) Biochemistry , vol.36 , pp. 4386-4392
    • Gagne, S.M.1    Li, M.X.2    Sykes, B.D.3
  • 122
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu YS, Bugg CE, Cook WJ. Structure of calmodulin refined at 2.2 Å resolution. J Mol Biol 1988; 204: 191-204.
    • (1988) J Mol Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 124
    • 0027331307 scopus 로고
    • The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain
    • Finn BE, Drakenberg T, Forsen S. The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain. FEBS Lett 1993; 336: 368-374.
    • (1993) FEBS Lett , vol.336 , pp. 368-374
    • Finn, B.E.1    Drakenberg, T.2    Forsen, S.3
  • 125
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang M, Tanaka T, Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol 1995; 2: 758-767.
    • (1995) Nat Struct Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 126
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 1992; 256: 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 127
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
    • Meador WE, Means AR, Quiocho FA. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 1992; 257: 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 128
    • 0015071225 scopus 로고
    • Isolation of a calcium-sequestering protein from sarcoplasmic reticulum
    • MacLennan DH, Wong PT. Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. Proc Natl Acad Sci USA 1971; 68: 1231-1235.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 1231-1235
    • MacLennan, D.H.1    Wong, P.T.2
  • 129
    • 0028906807 scopus 로고
    • Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum
    • Guo W, Campbell KP. Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum. J Biol Chem 1995; 270: 9027-9030.
    • (1995) J Biol Chem , vol.270 , pp. 9027-9030
    • Guo, W.1    Campbell, K.P.2
  • 130
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • Zhang L, Kelley J, Schmeisser G, Kobayashi YM, Jones LR. Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem 1997; 272: 23389-23397.
    • (1997) J Biol Chem , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5
  • 131
    • 0030371176 scopus 로고    scopus 로고
    • Role of parvalbumin in skeletal muscle relaxation
    • Rall J. Role of parvalbumin in skeletal muscle relaxation. News in Physiological Sciences 1996; 11: 249-255.
    • (1996) News in Physiological Sciences , vol.11 , pp. 249-255
    • Rall, J.1
  • 133
    • 0023876640 scopus 로고
    • Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning
    • Scott BT, Simmerman HK, Collins JH, Nadal-Ginard B, Jones LR. Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. J Biol Chem 1988; 263: 8958-8964.
    • (1988) J Biol Chem , vol.263 , pp. 8958-8964
    • Scott, B.T.1    Simmerman, H.K.2    Collins, J.H.3    Nadal-Ginard, B.4    Jones, L.R.5
  • 134
    • 0000962563 scopus 로고
    • Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
    • Holmgren A, Soderberg BO, Eklund H, Branden CI. Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. Proc Natl Acad Sci USA 1975; 72: 2305-2309.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2305-2309
    • Holmgren, A.1    Soderberg, B.O.2    Eklund, H.3    Branden, C.I.4
  • 137
    • 0019810179 scopus 로고
    • Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: An electron-probe study
    • Somlyo AV, Gonzalez-Serratos HG, Shuman H, McClellan G, Somlyo AP. Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: An electron-probe study. J Cell Biol 1981; 90: 577-594.
    • (1981) J Cell Biol , vol.90 , pp. 577-594
    • Somlyo, A.V.1    Gonzalez-Serratos, H.G.2    Shuman, H.3    McClellan, G.4    Somlyo, A.P.5
  • 138
    • 0023372321 scopus 로고
    • The structure of calsequestrin in triads of vertebrate skeletal muscle: A deep-etch study
    • Franzini-Armstrong C, Kenney LJ, Varriano-Marston E. The structure of calsequestrin in triads of vertebrate skeletal muscle: A deep-etch study. J Cell Biol 1987; 105: 49-56.
    • (1987) J Cell Biol , vol.105 , pp. 49-56
    • Franzini-Armstrong, C.1    Kenney, L.J.2    Varriano-Marston, E.3
  • 139
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
    • Saito A, Seiler S, Chu A, Fleischer S. Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J Cell Biol 1984; 99: 875-885.
    • (1984) J Cell Biol , vol.99 , pp. 875-885
    • Saito, A.1    Seiler, S.2    Chu, A.3    Fleischer, S.4
  • 140
    • 0021794373 scopus 로고
    • Purification and crystallization of the calcium binding protein of sarcoplasmic reticulum from skeletal muscle
    • Maurer A, Tanaka M, Ozawa T, Fleischer S. Purification and crystallization of the calcium binding protein of sarcoplasmic reticulum from skeletal muscle. Proc Natl Acad Sci USA 1985; 82: 4036-4040.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4036-4040
    • Maurer, A.1    Tanaka, M.2    Ozawa, T.3    Fleischer, S.4
  • 141
  • 142
    • 0018142678 scopus 로고
    • The multifarious couplings of energy transduction
    • Williams RJP. The multifarious couplings of energy transduction. Biochim Biophys Acta 1978; 505: 1-44.
    • (1978) Biochim Biophys Acta , vol.505 , pp. 1-44
    • Williams, R.J.P.1
  • 143
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. Journal of Applied Crystallography 1991; 24: 946-956.
    • (1991) Journal of Applied Crystallography , vol.24 , pp. 946-956
    • Kraulis, P.J.1
  • 144
    • 0031576345 scopus 로고    scopus 로고
    • Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution
    • Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN. Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution. J Mol Biol 1997; 273: 238-255.
    • (1997) J Mol Biol , vol.273 , pp. 238-255
    • Strynadka, N.C.1    Cherney, M.2    Sielecki, A.R.3    Li, M.X.4    Smillie, L.B.5    James, M.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.