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Volumn 49, Issue 4, 1999, Pages 325-333

Molecular aspects of the excitation-contraction coupling in skeletal muscle

Author keywords

Calcium; Dihydropyridine receptor; Muscle; Ryanodine receptor; Sarcoplasmic reticulum

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CALMODULIN; FK 506 BINDING PROTEIN; RECEPTOR; RECEPTOR SUBTYPE; RYANODINE RECEPTOR;

EID: 0032737648     PISSN: 0021521X     EISSN: None     Source Type: Journal    
DOI: 10.2170/jjphysiol.49.325     Document Type: Review
Times cited : (18)

References (81)
  • 1
    • 0015856482 scopus 로고
    • Voltage dependent charge movement in skeletal muscle: A possible step in excitation-contraction coupling
    • Schneider M and Chandler W: Voltage dependent charge movement in skeletal muscle: a possible step in excitation-contraction coupling. Nature 242: 244-246, 1973
    • (1973) Nature , vol.242 , pp. 244-246
    • Schneider, M.1    Chandler, W.2
  • 2
    • 0016652070 scopus 로고
    • Membrane particles and transmission at the triad
    • Franzini-Armstrong C: Membrane particles and transmission at the triad. Fed Proc 34: 1382-1389, 1975
    • (1975) Fed Proc , vol.34 , pp. 1382-1389
    • Franzini-Armstrong, C.1
  • 3
    • 0014931506 scopus 로고
    • Calcium induced release of calcium from the sarcoplasmic reticulum of skinned skeletal muscle fibres
    • Endo M, Tanaka M, and Ogawa Y: Calcium induced release of calcium from the sarcoplasmic reticulum of skinned skeletal muscle fibres. Nature 228: 34-36, 1970
    • (1970) Nature , vol.228 , pp. 34-36
    • Endo, M.1    Tanaka, M.2    Ogawa, Y.3
  • 4
    • 0014929598 scopus 로고
    • Regenerative calcium release within muscle cells
    • Ford LE and Podolsky RJ: Regenerative calcium release within muscle cells. Science 167: 58-59, 1970
    • (1970) Science , vol.167 , pp. 58-59
    • Ford, L.E.1    Podolsky, R.J.2
  • 5
    • 0021280174 scopus 로고
    • Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules
    • Curtis BM and Catterall WA: Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules. Biochemistry 23: 2113-2118, 1984
    • (1984) Biochemistry , vol.23 , pp. 2113-2118
    • Curtis, B.M.1    Catterall, W.A.2
  • 6
    • 0022151294 scopus 로고
    • 2+ release channels with ryanodine in junctional terminal cisternae of sarcoplasmic reticulum of fast skeletal muscle
    • 2+ release channels with ryanodine in junctional terminal cisternae of sarcoplasmic reticulum of fast skeletal muscle. Proc Natl Acad Sci USA 82: 7256-7259, 1985
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7256-7259
    • Fleischer, S.1    Ogunbunmi, E.2    Dixon, M.3    Fleer, E.4
  • 7
    • 0022413366 scopus 로고
    • Sarcoplasmic reticulum contains adenine nucleotide-activated calcium channels
    • Smith JS, Coronado R, and Meissner G: Sarcoplasmic reticulum contains adenine nucleotide-activated calcium channels. Nature 316: 446-449, 1985
    • (1985) Nature , vol.316 , pp. 446-449
    • Smith, J.S.1    Coronado, R.2    Meissner, G.3
  • 11
    • 0016882456 scopus 로고
    • Effects of glycerol treatment and maintained depolarization on charge movement in skeletal muscle
    • Chandler WK, Rakowski RF, and Schneider MF: Effects of glycerol treatment and maintained depolarization on charge movement in skeletal muscle. J Physiol (Lond) 254: 285-316, 1976
    • (1976) J Physiol (Lond) , vol.254 , pp. 285-316
    • Chandler, W.K.1    Rakowski, R.F.2    Schneider, M.F.3
  • 12
    • 0023716276 scopus 로고
    • Intramembrane charge movements in skeletal muscle
    • Huang CL: Intramembrane charge movements in skeletal muscle. Physiol Rev 68: 1197-1147, 1988
    • (1988) Physiol Rev , vol.68 , pp. 1197-11147
    • Huang, C.L.1
  • 13
    • 0025850997 scopus 로고
    • Interfering with calcium release suppresses I gamma, the "hump" component of intramembranous charge movement in skeletal muscle
    • Csernoch L, Pizarro G, Uribe I, Rodriguez M, and Rios E: Interfering with calcium release suppresses I gamma, the "hump" component of intramembranous charge movement in skeletal muscle. J Gen Physiol 97: 845-884, 1991
    • (1991) J Gen Physiol , vol.97 , pp. 845-884
    • Csernoch, L.1    Pizarro, G.2    Uribe, I.3    Rodriguez, M.4    Rios, E.5
  • 14
    • 0021843849 scopus 로고
    • Dihydropyridine receptors in muscle are voltage-dependent but most are not functional calcium channels
    • Schwartz LM, McCleskey EW, and Almers W: Dihydropyridine receptors in muscle are voltage-dependent but most are not functional calcium channels. Nature 314: 747-751, 1985
    • (1985) Nature , vol.314 , pp. 747-751
    • Schwartz, L.M.1    McCleskey, E.W.2    Almers, W.3
  • 15
    • 0023113884 scopus 로고
    • Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle
    • Rios E and Brum G: Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle. Nature 325: 717-720, 1987
    • (1987) Nature , vol.325 , pp. 717-720
    • Rios, E.1    Brum, G.2
  • 16
    • 0027064887 scopus 로고
    • A single nucleotide deletion in the skeletal muscle-specific calcium channel transcript of muscular dysgenesis (mdg) mice
    • Chaudhari N: A single nucleotide deletion in the skeletal muscle-specific calcium channel transcript of muscular dysgenesis (mdg) mice. J Biol Chem 267: 25636-25639, 1992
    • (1992) J Biol Chem , vol.267 , pp. 25636-25639
    • Chaudhari, N.1
  • 17
    • 0015861656 scopus 로고
    • Electrical properties of normal and dysgenic mouse skeletal muscle in culture
    • Powell JA and Fambrough DM: Electrical properties of normal and dysgenic mouse skeletal muscle in culture. J Cell Physiol 82: 21-38, 1973
    • (1973) J Cell Physiol , vol.82 , pp. 21-38
    • Powell, J.A.1    Fambrough, D.M.2
  • 18
    • 0025336609 scopus 로고
    • Intramembrane charge movement restored in dysgenic skeletal muscle by injection of dihydropyridine receptor cDNAs
    • Adams BA, Tanabe T, Mikami A, Numa S, and Beam KG: Intramembrane charge movement restored in dysgenic skeletal muscle by injection of dihydropyridine receptor cDNAs. Nature 346: 569-572, 1990
    • (1990) Nature , vol.346 , pp. 569-572
    • Adams, B.A.1    Tanabe, T.2    Mikami, A.3    Numa, S.4    Beam, K.G.5
  • 19
    • 0023723765 scopus 로고
    • Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA
    • Tanabe T, Beam K, Powell J, and Numa S: Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA. Nature 336: 134-139, 1988
    • (1988) Nature , vol.336 , pp. 134-139
    • Tanabe, T.1    Beam, K.2    Powell, J.3    Numa, S.4
  • 21
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • Block B, Imagawa T, Campbell K, and Franzini-Armstrong C: Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J Cell Biol 107: 2587-2600, 1988
    • (1988) J Cell Biol , vol.107 , pp. 2587-2600
    • Block, B.1    Imagawa, T.2    Campbell, K.3    Franzini-Armstrong, C.4
  • 22
    • 0028065352 scopus 로고
    • Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA
    • Takekura H, Bennett L, Tanabe T, Beam KG, and Franzini-Armstrong C: Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA. Biophys J 67: 793-803, 1994
    • (1994) Biophys J , vol.67 , pp. 793-803
    • Takekura, H.1    Bennett, L.2    Tanabe, T.3    Beam, K.G.4    Franzini-Armstrong, C.5
  • 23
    • 0017364364 scopus 로고
    • Calcium release from the sarcoplasmic reticulum
    • Endo M: Calcium release from the sarcoplasmic reticulum. Physiol Rev 57: 71-108, 1977
    • (1977) Physiol Rev , vol.57 , pp. 71-108
    • Endo, M.1
  • 24
    • 0344487761 scopus 로고
    • Calcium release from sarcoplasmic reticulum
    • Endo M: Calcium release from sarcoplasmic reticulum. Curr Top Membr Transp 25: 181-230, 1985
    • (1985) Curr Top Membr Transp , vol.25 , pp. 181-230
    • Endo, M.1
  • 25
    • 0345694638 scopus 로고
    • Twitches in the presence of ethylene glycolbis-(β-aminoethylether)-N,N′-tetraacetic acid
    • Armstrong C, Bezanilla F, and Horowicz P: Twitches in the presence of ethylene glycolbis-(β-aminoethylether)-N,N′-tetraacetic acid. Biochim Biophys Acta 468: 31-50, 1972
    • (1972) Biochim Biophys Acta , vol.468 , pp. 31-50
    • Armstrong, C.1    Bezanilla, F.2    Horowicz, P.3
  • 26
    • 0023931017 scopus 로고
    • Effects of extracellular calcium on calcium movements of excitation-contraction coupling in frog skeletal muscle fibres
    • Brum G, Ríos E, and Stefani E: Effects of extracellular calcium on calcium movements of excitation-contraction coupling in frog skeletal muscle fibres. J Physiol (Lond) 398: 441-473, 1988
    • (1988) J Physiol (Lond) , vol.398 , pp. 441-473
    • Brum, G.1    Ríos, E.2    Stefani, E.3
  • 27
    • 0021287212 scopus 로고
    • Extracellular ions and excitation-contraction coupling in frog twitch muscle fibres
    • Miledi R, Parker I, and Zhu PH: Extracellular ions and excitation-contraction coupling in frog twitch muscle fibres. J Physiol (Lond) 351: 687-710, 1984
    • (1984) J Physiol (Lond) , vol.351 , pp. 687-710
    • Miledi, R.1    Parker, I.2    Zhu, P.H.3
  • 28
    • 0001641097 scopus 로고
    • Calcium-induced calcium release and "depolarization"-induced calcium release: Their physiological significance
    • Thorens S and Endo M: Calcium-induced calcium release and "depolarization"-induced calcium release: their physiological significance. Proc Jpn Acad 51: 473-478, 1975
    • (1975) Proc Jpn Acad , vol.51 , pp. 473-478
    • Thorens, S.1    Endo, M.2
  • 30
    • 0030893595 scopus 로고    scopus 로고
    • The pharmacology of ryanodine and related compounds
    • Sutko JL, Airey JA, Welch W, and Ruest L: The pharmacology of ryanodine and related compounds. Pharmacol Rev 49: 53-98, 1997
    • (1997) Pharmacol Rev , vol.49 , pp. 53-98
    • Sutko, J.L.1    Airey, J.A.2    Welch, W.3    Ruest, L.4
  • 31
    • 0023008143 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. J Biol Chem 261: 6300-6306, 1986
    • (1986) J Biol Chem , vol.261 , pp. 6300-6306
    • Meissner, G.1
  • 32
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai FA, Erickson HP, Rousseau E, Liu QY, and Meissner G: Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 331: 315-319, 1988
    • (1988) Nature , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.Y.4    Meissner, G.5
  • 34
    • 0023809190 scopus 로고
    • Purified ryanodine receptor from rabbit skeletal muscle is the calcium-release channel of sarcoplasmic reticulum
    • Smith JS, Imagawa T, Ma J, Fill M, Campbell KP, and Coronado R: Purified ryanodine receptor from rabbit skeletal muscle is the calcium-release channel of sarcoplasmic reticulum. J Gen Physiol 92: 1-26, 1988
    • (1988) J Gen Physiol , vol.92 , pp. 1-26
    • Smith, J.S.1    Imagawa, T.2    Ma, J.3    Fill, M.4    Campbell, K.P.5    Coronado, R.6
  • 35
    • 0023241909 scopus 로고
    • Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures
    • Inui M, Saito A, and Fleischer S: Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures. J Biol Chem 262: 15637-15642, 1987
    • (1987) J Biol Chem , vol.262 , pp. 15637-15642
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 36
    • 0028332473 scopus 로고
    • Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene
    • Takeshima H, Iino M, Takekura H, Nishi M, Kuno J, Minowa O, Takano H, and Noda T: Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature 369: 556-559, 1994
    • (1994) Nature , vol.369 , pp. 556-559
    • Takeshima, H.1    Iino, M.2    Takekura, H.3    Nishi, M.4    Kuno, J.5    Minowa, O.6    Takano, H.7    Noda, T.8
  • 38
    • 0028919291 scopus 로고
    • Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor
    • Takekura H, Nishi M, Noda T, Takeshima H, and Franzini-Armstrong C: Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor. Proc Natl Acad Sci USA 92: 3381-3385, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3381-3385
    • Takekura, H.1    Nishi, M.2    Noda, T.3    Takeshima, H.4    Franzini-Armstrong, C.5
  • 39
    • 0029971070 scopus 로고    scopus 로고
    • Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles
    • Conti A, Gorza L, and Sorreritino V: Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles. Biochem J 316: 19-23, 1996
    • (1996) Biochem J , vol.316 , pp. 19-23
    • Conti, A.1    Gorza, L.2    Sorreritino, V.3
  • 41
    • 0030888590 scopus 로고    scopus 로고
    • A region of the ryanodine receptor critical for excitation-contraction coupling in skeletal muscle
    • Yamazawa T, Takeshima H, Shimuta M, and Iino M: A region of the ryanodine receptor critical for excitation-contraction coupling in skeletal muscle. J Biol Chem 272: 8161-8164, 1997
    • (1997) J Biol Chem , vol.272 , pp. 8161-8164
    • Yamazawa, T.1    Takeshima, H.2    Shimuta, M.3    Iino, M.4
  • 42
    • 0030981209 scopus 로고    scopus 로고
    • Functional and morphological features of skeletal muscle from mutant mice lacking both type 1 and type 3 ryanodine receptors
    • Ikemoto T, Komazaki S, Takeshima H, Nishi M, Noda T, Iino M, and Endo M: Functional and morphological features of skeletal muscle from mutant mice lacking both type 1 and type 3 ryanodine receptors. J Physiol (Lond) 501: 305-312, 1997
    • (1997) J Physiol (Lond) , vol.501 , pp. 305-312
    • Ikemoto, T.1    Komazaki, S.2    Takeshima, H.3    Nishi, M.4    Noda, T.5    Iino, M.6    Endo, M.7
  • 44
    • 0027426069 scopus 로고
    • Calcium sparks: Elementary events underlying excitation-contraction coupling in heart muscle
    • Cheng H, Lederer WJ, and Cannell MB: Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle. Science 262: 740-744, 1993
    • (1993) Science , vol.262 , pp. 740-744
    • Cheng, H.1    Lederer, W.J.2    Cannell, M.B.3
  • 45
    • 0029005888 scopus 로고
    • The control of calcium release in heart muscle
    • Cannell MB, Cheng H, and Lederer WJ: The control of calcium release in heart muscle. Science 268: 1045-1049, 1995
    • (1995) Science , vol.268 , pp. 1045-1049
    • Cannell, M.B.1    Cheng, H.2    Lederer, W.J.3
  • 47
    • 0032532529 scopus 로고    scopus 로고
    • Local calcium release in mammalian skeletal muscle
    • Shirokova N, Garcia J, and Rios E: Local calcium release in mammalian skeletal muscle. J Physiol (Lond) 512: 377-384, 1998
    • (1998) J Physiol (Lond) , vol.512 , pp. 377-384
    • Shirokova, N.1    Garcia, J.2    Rios, E.3
  • 49
    • 0025327389 scopus 로고
    • Surface topography analysis of the ryanodine receptor/junctional channel complex based on proteolysis sensitivity mapping
    • Marks AR, Fleischer S, and Tempst P: Surface topography analysis of the ryanodine receptor/junctional channel complex based on proteolysis sensitivity mapping. J Biol Chem 265: 13143-13149, 1990
    • (1990) J Biol Chem , vol.265 , pp. 13143-13149
    • Marks, A.R.1    Fleischer, S.2    Tempst, P.3
  • 50
    • 0027461582 scopus 로고
    • Ryanodine receptors: How many, where and why?
    • Sorrentino V and Volpe P: Ryanodine receptors: how many, where and why? TIPS 14: 98-103, 1993
    • (1993) TIPS , vol.14 , pp. 98-103
    • Sorrentino, V.1    Volpe, P.2
  • 53
    • 0030798639 scopus 로고    scopus 로고
    • Characterization of type 3 ryanodine receptor (RyR3) of sarcoplasmic reticulum from rabbit skeletal muscles
    • Murayama T and Ogawa Y: Characterization of type 3 ryanodine receptor (RyR3) of sarcoplasmic reticulum from rabbit skeletal muscles. J Biol Chem 272: 24030-24037, 1997
    • (1997) J Biol Chem , vol.272 , pp. 24030-24037
    • Murayama, T.1    Ogawa, Y.2
  • 54
    • 0030783094 scopus 로고    scopus 로고
    • 2+ release channel (ryanodine receptor) expressed in HEK293 cells
    • 2+ release channel (ryanodine receptor) expressed in HEK293 cells. J Biol Chem 272: 24234-24246, 1997
    • (1997) J Biol Chem , vol.272 , pp. 24234-24246
    • Chen, S.R.W.1    Li, X.2    Ebisawa, K.3    Zhang, L.4
  • 56
    • 0029085592 scopus 로고
    • 2+ release in the sarcoplasmic reticulum of rabbit skeletal muscle fibres
    • 2+ release in the sarcoplasmic reticulum of rabbit skeletal muscle fibres. J Physiol (Lond) 487: 573-582, 1995
    • (1995) J Physiol (Lond) , vol.487 , pp. 573-582
    • Ikemoto, T.1    Iino, M.2    Endo, M.3
  • 58
    • 0032418614 scopus 로고    scopus 로고
    • 2+ release of skeletal muscle from mutant mice expressing either ryanodine receptor type 1 or type 3
    • 2+ release of skeletal muscle from mutant mice expressing either ryanodine receptor type 1 or type 3. Pflügers Arch 437: 43-48, 1998
    • (1998) Pflügers Arch , vol.437 , pp. 43-48
    • Ikemoto, T.1    Takeshima, H.2    Iino, M.3    Endo, M.4
  • 60
  • 61
    • 0024566091 scopus 로고
    • Three-dimensional architecture of the calcium channel/foot structure of sarcoplasmic reticulum
    • Wagenknecht T, Grassucci R, Frank J, Saito A, Inui M, and Fleischer S: Three-dimensional architecture of the calcium channel/foot structure of sarcoplasmic reticulum. Nature 338: 167-170, 1989
    • (1989) Nature , vol.338 , pp. 167-170
    • Wagenknecht, T.1    Grassucci, R.2    Frank, J.3    Saito, A.4    Inui, M.5    Fleischer, S.6
  • 63
    • 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, and Fleischer S: Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor. J Biol Chem 272: 32463-32471, 1997
    • (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
  • 65
    • 0025356933 scopus 로고
    • Cardiac-type excitation-contraction coupling in dysgenic skeletal muscle injected with cardiac dihydropyridine receptor cDNA
    • Tanabe T, Mikami A, Numa S, and Beam KG: Cardiac-type excitation-contraction coupling in dysgenic skeletal muscle injected with cardiac dihydropyridine receptor cDNA. Nature 344: 451-453, 1990
    • (1990) Nature , vol.344 , pp. 451-453
    • Tanabe, T.1    Mikami, A.2    Numa, S.3    Beam, K.G.4
  • 66
    • 0025288735 scopus 로고
    • Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling
    • Tanabe T, Beam KG, Adams BA, Niidome T, and Numa S: Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 346: 567-569, 1990
    • (1990) Nature , vol.346 , pp. 567-569
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 67
    • 0032566748 scopus 로고    scopus 로고
    • Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling
    • Nakai J, Tanabe T, Konno T, Adams B, and Beam KG: Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling. J Biol Chem 273: 24983-24986, 1998
    • (1998) J Biol Chem , vol.273 , pp. 24983-24986
    • Nakai, J.1    Tanabe, T.2    Konno, T.3    Adams, B.4    Beam, K.G.5
  • 73
    • 0029983398 scopus 로고    scopus 로고
    • Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor
    • Nakai J, Dirksen RT, Nguyen HT, Pessah IN, Beam KG, and Allen PD: Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature 380: 72-75, 1996
    • (1996) Nature , vol.380 , pp. 72-75
    • Nakai, J.1    Dirksen, R.T.2    Nguyen, H.T.3    Pessah, I.N.4    Beam, K.G.5    Allen, P.D.6
  • 74
    • 0029662341 scopus 로고    scopus 로고
    • 2+ release channels: Does diversity in form equal diversity in function?
    • 2+ release channels: does diversity in form equal diversity in function? Physiol Rev 76: 1027-1071, 1996
    • (1996) Physiol Rev , vol.76 , pp. 1027-1071
    • Sutko, J.L.1    Airey, J.A.2
  • 75
    • 0028332825 scopus 로고
    • Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle
    • Oyamada H, Murayama T, Takagi T, Iino M, Iwabe N, Miyata T Ogawa Y, and Endo M: Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle. J Biol Chem 269: 17206-17214, 1994
    • (1994) J Biol Chem , vol.269 , pp. 17206-17214
    • Oyamada, H.1    Murayama, T.2    Takagi, T.3    Iino, M.4    Iwabe, N.5    Miyata, T.6    Ogawa, Y.7    Endo, M.8
  • 76
    • 0029923335 scopus 로고    scopus 로고
    • a and b isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3
    • Ottini L, Marziali G, Conti A, Charlesworth A, and Sorrentino V: a and b isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3. Biochem J 315: 207-216, 1996
    • (1996) Biochem J , vol.315 , pp. 207-216
    • Ottini, L.1    Marziali, G.2    Conti, A.3    Charlesworth, A.4    Sorrentino, V.5
  • 77
    • 0028926924 scopus 로고
    • Embryonic chicken skeletal muscle cells fail to develop normal excitation-contraction coupling in the absence of the alpha ryanodine receptor. Implications for a two-ryanodine receptor system
    • Ivanenko A, McKemy DD, Kenyon JL, Airey JA, and Sutko JL: Embryonic chicken skeletal muscle cells fail to develop normal excitation-contraction coupling in the absence of the alpha ryanodine receptor. Implications for a two-ryanodine receptor system. J Biol Chem 270: 4220-4223, 1995
    • (1995) J Biol Chem , vol.270 , pp. 4220-4223
    • Ivanenko, A.1    McKemy, D.D.2    Kenyon, J.L.3    Airey, J.A.4    Sutko, J.L.5
  • 78
    • 0022555602 scopus 로고
    • The removal of myoplasmic free calcium following calcium release in frog skeletal muscle
    • Melzer W, Rios E, and Schneider MF: The removal of myoplasmic free calcium following calcium release in frog skeletal muscle. J Physiol (Lond) 372: 261-292, 1986
    • (1986) J Physiol (Lond) , vol.372 , pp. 261-292
    • Melzer, W.1    Rios, E.2    Schneider, M.F.3
  • 79
    • 0027467564 scopus 로고
    • Calcium transients and calcium release in rat fast-twitch skeletal muscle fibres
    • Garcia J and Schneider MF: Calcium transients and calcium release in rat fast-twitch skeletal muscle fibres. J Physiol (Lond) 463: 709-728, 1993
    • (1993) J Physiol (Lond) , vol.463 , pp. 709-728
    • Garcia, J.1    Schneider, M.F.2
  • 80
    • 0031437520 scopus 로고    scopus 로고
    • Intramembrane charge movement and sarcoplasmic calcium release in enzymatically isolated mammalian skeletal muscle fibres
    • Szentesi P, Jacquemond V, Kovacs L, and Csernoch L: Intramembrane charge movement and sarcoplasmic calcium release in enzymatically isolated mammalian skeletal muscle fibres J Physiol (Lond) 505: 371-384, 1997
    • (1997) J Physiol (Lond) , vol.505 , pp. 371-384
    • Szentesi, P.1    Jacquemond, V.2    Kovacs, L.3    Csernoch, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.