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Volumn 140, Issue 2, 2012, Pages 93-108

Luminal Ca 2+ controls activation of the cardiac yanodine receptor by ATP

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; CALCIUM CHANNEL STIMULATING AGENT; RYANODINE RECEPTOR;

EID: 84866174265     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201110708     Document Type: Article
Times cited : (32)

References (90)
  • 3
    • 0025291967 scopus 로고
    • Divalent cation activation and inhibition of single calcium release channels from sheep cardiac sarcoplasmic reticulum
    • Ashley, R.H., and A.J. Williams. 1990. Divalent cation activation and inhibition of single calcium release channels from sheep cardiac sarcoplasmic reticulum. J. Gen. Physiol. 95:981-1005. http://dx.doi.org/10.1085/jgp.95.5.981
    • (1990) J. Gen. Physiol. , vol.95 , pp. 981-1005
    • Ashley, R.H.1    Williams, A.J.2
  • 4
    • 0029029280 scopus 로고
    • Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes
    • Bassani, J.W.M., W.L. Yuan, and D.M. Bers. 1995. Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am. J. Physiol. 268:C1313-C1319.
    • (1995) Am. J. Physiol. , vol.268
    • Bassani, J.W.M.1    Yuan, W.L.2    Bers, D.M.3
  • 5
    • 0036219539 scopus 로고    scopus 로고
    • Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels
    • Beard, N.A., M.M. Sakowska, A.F. Dulhunty, and D.R. Laver. 2002. Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels. Biophys. J. 82:310-320. http://dx.doi.org/10.1016/S0006-3495(02)75396-4
    • (2002) Biophys. J. , vol.82 , pp. 310-320
    • Beard, N.A.1    Sakowska, M.M.2    Dulhunty, A.F.3    Laver, D.R.4
  • 6
    • 36849013016 scopus 로고    scopus 로고
    • Enhanced ryanodine receptor-mediated calcium leak determines reduced sarcoplasmic reticulum calcium content in chronic canine heart failure
    • Belevych, A., Z. Kubalova, D. Terentyev, R.L. Hamlin, C.A. Carnes, and S. Györke. 2007. Enhanced ryanodine receptor-mediated calcium leak determines reduced sarcoplasmic reticulum calcium content in chronic canine heart failure. Biophys. J. 93:4083-4092. http://dx.doi.org/10.1529/biophysj.107.114546
    • (2007) Biophys. J. , vol.93 , pp. 4083-4092
    • Belevych, A.1    Kubalova, Z.2    Terentyev, D.3    Hamlin, R.L.4    Carnes, C.A.5    Györke, S.6
  • 7
    • 0023550239 scopus 로고
    • Regulation of twitch tension in sheep cardiac Purkinje fibers during calcium overload
    • Berlin, J.R., M.B. Cannell, and W.J. Lederer. 1987. Regulation of twitch tension in sheep cardiac Purkinje fibers during calcium overload. Am. J. Physiol. 253:H1540-H1547.
    • (1987) Am. J. Physiol. , vol.253
    • Berlin, J.R.1    Cannell, M.B.2    Lederer, W.J.3
  • 10
    • 0037223062 scopus 로고    scopus 로고
    • Structural characteristics that govern binding to, and modulation through, the cardiac ryanodine receptor nucleotide binding site
    • Chan, W.M., W. Welch, and R. Sitsapesan. 2003. Structural characteristics that govern binding to, and modulation through, the cardiac ryanodine receptor nucleotide binding site. Mol. Pharmacol. 63:174-182. http://dx.doi.org/10.1124/mol.63.1.174
    • (2003) Mol. Pharmacol. , vol.63 , pp. 174-182
    • Chan, W.M.1    Welch, W.2    Sitsapesan, R.3
  • 12
    • 0032927515 scopus 로고    scopus 로고
    • AMP is a partial agonist at the sheep cardiac ryanodine receptor
    • Ching, L.L., A.J. Williams, and R. Sitsapesan. 1999. AMP is a partial agonist at the sheep cardiac ryanodine receptor. Br. J. Pharmacol. 127:161-171. http://dx.doi.org/10.1038/sj.bjp.0702491
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 161-171
    • Ching, L.L.1    Williams, A.J.2    Sitsapesan, R.3
  • 15
    • 80054835534 scopus 로고    scopus 로고
    • Modulation of cardiac ryanodine receptor channels by alkaline earth cations
    • Diaz-Sylvester, P.L., M. Porta, and J.A. Copello. 2011. Modulation of cardiac ryanodine receptor channels by alkaline earth cations. PLoS ONE. 6:e26693. http://dx.doi.org/10.1371/journal.pone.0026693
    • (2011) PLoS ONE , vol.6
    • Diaz-Sylvester, P.L.1    Porta, M.2    Copello, J.A.3
  • 16
    • 0021914538 scopus 로고
    • Time and calcium dependence of activation and inactivation of calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned canine cardiac Purkinje cell
    • Fabiato, A. 1985. Time and calcium dependence of activation and inactivation of calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned canine cardiac Purkinje cell. J. Gen. Physiol. 85:247-289. http://dx.doi.org/10.1085/jgp.85.2.247
    • (1985) J. Gen. Physiol. , vol.85 , pp. 247-289
    • Fabiato, A.1
  • 17
    • 0016768145 scopus 로고
    • Contractions induced by a calcium-triggered release of calcium from the sarcoplasmic reticulum of single skinned cardiac cells
    • Fabiato, A., and F. Fabiato. 1975. Contractions induced by a calcium-triggered release of calcium from the sarcoplasmic reticulum of single skinned cardiac cells. J. Physiol. 249:469-495.
    • (1975) J. Physiol. , vol.249 , pp. 469-495
    • Fabiato, A.1    Fabiato, F.2
  • 18
    • 0017885455 scopus 로고
    • Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiace and skeletal muscles
    • Fabiato, A., and F. Fabiato. 1978. Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiace and skeletal muscles. J. Physiol. 276:233-255.
    • (1978) J. Physiol. , vol.276 , pp. 233-255
    • Fabiato, A.1    Fabiato, F.2
  • 21
    • 0141571322 scopus 로고    scopus 로고
    • Ryanodine receptor mutations associated with stress-induced ventricular tachycardia mediate increased calcium release in stimulated cardiomyocytes
    • George, C.H., G.V. Higgs, and F.A. Lai. 2003. Ryanodine receptor mutations associated with stress-induced ventricular tachycardia mediate increased calcium release in stimulated cardiomyocytes. Circ. Res. 93:531-540. http://dx.doi.org/10.1161/01.RES.0000091335.07574.86
    • (2003) Circ. Res. , vol.93 , pp. 531-540
    • George, C.H.1    Higgs, G.V.2    Lai, F.A.3
  • 23
    • 0034084757 scopus 로고    scopus 로고
    • Calcium handling and cell contraction in rat cardiomyocytes depleted of intracellular magnesium
    • Griffiths, E.J. 2000. Calcium handling and cell contraction in rat cardiomyocytes depleted of intracellular magnesium. Cardiovasc. Res. 47:116-123. http://dx.doi.org/10.1016/S0008-6363(00)00061-4
    • (2000) Cardiovasc. Res. , vol.47 , pp. 116-123
    • Griffiths, E.J.1
  • 24
    • 59649126967 scopus 로고    scopus 로고
    • 2+ in cardiac myocytes
    • 2+ in cardiac myocytes. J. Gen. Physiol. 132:721-730. http://dx.doi.org/10.1085/jgp.200810119
    • (2008) J. Gen. Physiol. , vol.132 , pp. 721-730
    • Gusev, K.1    Niggli, E.2
  • 25
    • 0141448292 scopus 로고    scopus 로고
    • 2+ sensing sites
    • 2+ sensing sites. Biophys. J. 75:2801-2810. http://dx.doi.org/10.1016/S0006-3495(98)77723-9
    • (1998) Biophys. J. , vol.75 , pp. 2801-2810
    • Györke, I.1    Györke, S.2
  • 26
    • 38849091360 scopus 로고    scopus 로고
    • Modulation of ryanodine receptor by luminal calcium and accessory proteins in health and cardiac disease
    • Györke, S., and D. Terentyev. 2008. Modulation of ryanodine receptor by luminal calcium and accessory proteins in health and cardiac disease. Cardiovasc. Res. 77:245-255. http://dx.doi.org/10.1093/cvr/cvm038
    • (2008) Cardiovasc. Res. , vol.77 , pp. 245-255
    • Györke, S.1    Terentyev, D.2
  • 27
    • 0142260723 scopus 로고    scopus 로고
    • Dual effects of tetracaine on spontaneous calcium release in rat ventricular myocytes
    • Györke, S., V. Lukyanenko, and I. Györke. 1997. Dual effects of tetracaine on spontaneous calcium release in rat ventricular myocytes. J. Physiol. 500:297-309.
    • (1997) J. Physiol. , vol.500 , pp. 297-309
    • Györke, S.1    Lukyanenko, V.2    Györke, I.3
  • 29
    • 1942423621 scopus 로고    scopus 로고
    • The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium
    • Györke, I., N. Hester, L.R. Jones, and S. Györke. 2004. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys. J. 86:2121-2128. http://dx.doi.org/10.1016/S0006-3495(04)74271-X
    • (2004) Biophys. J. , vol.86 , pp. 2121-2128
    • Györke, I.1    Hester, N.2    Jones, L.R.3    Györke, S.4
  • 32
    • 0035916903 scopus 로고    scopus 로고
    • Decreased sarcoplasmic reticulum calcium content is responsible for defective excitation-contraction coupling in canine heart failure
    • Hobai, I.A., and B. O'Rourke. 2001. Decreased sarcoplasmic reticulum calcium content is responsible for defective excitation-contraction coupling in canine heart failure. Circulation. 103:1577-1584. http://dx.doi.org/10.1161/01.CIR.103.11.1577
    • (2001) Circulation , vol.103 , pp. 1577-1584
    • Hobai, I.A.1    O'Rourke, B.2
  • 33
    • 3342967512 scopus 로고    scopus 로고
    • Is the failing heart energy starved? On using chemical energy to support cardiac function
    • Ingwall, J.S., and R.G. Weiss. 2004. Is the failing heart energy starved? On using chemical energy to support cardiac function. Circ. Res. 95:135-145. http://dx.doi.org/10.1161/01.RES.0000137170.41939.d9
    • (2004) Circ. Res. , vol.95 , pp. 135-145
    • Ingwall, J.S.1    Weiss, R.G.2
  • 34
    • 0037047646 scopus 로고    scopus 로고
    • 2+ release channel (ryanodine receptor) mutant associated with ventricular tachycardia and sudden death
    • 2+ release channel (ryanodine receptor) mutant associated with ventricular tachycardia and sudden death. Circ. Res. 91:218-225. http://dx.doi.org/10.1161/01.RES.0000028455.36940.5E
    • (2002) Circ. Res. , vol.91 , pp. 218-225
    • Jiang, D.1    Xiao, B.2    Zhang, L.3    Chen, S.R.4
  • 36
    • 33644673205 scopus 로고    scopus 로고
    • 2+ activation are common defects of RyR2 mutations linked to ventricular tachycardia and sudden death
    • 2+ activation are common defects of RyR2 mutations linked to ventricular tachycardia and sudden death. Circ. Res. 97:1173-1181. http://dx.doi.org/10.1161/01.RES.0000192146.85173.4b
    • (2005) Circ. Res. , vol.97 , pp. 1173-1181
    • Jiang, D.1    Wang, R.2    Xiao, B.3    Kong, H.4    Hunt, D.J.5    Choi, P.6    Zhang, L.7    Chen, S.R.8
  • 37
    • 36749047449 scopus 로고    scopus 로고
    • 2+ activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death
    • 2+ activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death. Proc. Natl. Acad. Sci. USA. 104:18309-18314. http://dx.doi.org/10.1073/pnas.0706573104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18309-18314
    • Jiang, D.1    Chen, W.2    Wang, R.3    Zhang, L.4    Chen, S.R.5
  • 39
    • 0018198761 scopus 로고
    • Role of calcium ions in transient inward currents and aftercontractions induced by strophanthidin in cardiac Purkinje fibres
    • Kass, R.S., W.J. Lederer, R.W. Tsien, and R. Weingart. 1978. Role of calcium ions in transient inward currents and aftercontractions induced by strophanthidin in cardiac Purkinje fibres. J. Physiol. 281:187-208.
    • (1978) J. Physiol. , vol.281 , pp. 187-208
    • Kass, R.S.1    Lederer, W.J.2    Tsien, R.W.3    Weingart, R.4
  • 40
    • 67650391702 scopus 로고    scopus 로고
    • New roles of calsequestrin and triadin in cardiac muscle
    • Knollmann, B.C. 2009. New roles of calsequestrin and triadin in cardiac muscle. J. Physiol. 587:3081-3087. http://dx.doi.org/10.1113/jphysiol.2009.172098
    • (2009) J. Physiol. , vol.587 , pp. 3081-3087
    • Knollmann, B.C.1
  • 42
    • 34247882821 scopus 로고    scopus 로고
    • 2+ sites
    • 2+ sites. Biophys. J. 92:3541-3555. http://dx.doi.org/10.1529/biophysj.106.099028
    • (2007) Biophys. J. , vol.92 , pp. 3541-3555
    • Laver, D.R.1
  • 43
    • 70450255386 scopus 로고    scopus 로고
    • 2+ activation of cardiac ryanodine receptors by luminal and cytoplasmic domains
    • 2+ activation of cardiac ryanodine receptors by luminal and cytoplasmic domains. Eur. Biophys. J. 39:19-26. http://dx.doi.org/10.1007/s00249-009-0417-1
    • (2009) Eur. Biophys. J. , vol.39 , pp. 19-26
    • Laver, D.R.1
  • 44
    • 53549123851 scopus 로고    scopus 로고
    • 2+ release: cytoplasmic and luminal regulation modeled in a tetrameric channel
    • 2+ release: cytoplasmic and luminal regulation modeled in a tetrameric channel. J. Gen. Physiol. 132:429-446. http://dx.doi.org/10.1085/jgp.200810001
    • (2008) J. Gen. Physiol. , vol.132 , pp. 429-446
    • Laver, D.R.1    Honen, B.N.2
  • 45
    • 0030920356 scopus 로고    scopus 로고
    • Magnesium inhibition of ryanodine-receptor calcium channels: evidence for two independent mechanisms
    • Laver, D.R., T.M. Baynes, and A.F. Dulhunty. 1997. Magnesium inhibition of ryanodine-receptor calcium channels: evidence for two independent mechanisms. J. Membr. Biol. 156:213-229. http://dx.doi.org/10.1007/s002329900202
    • (1997) J. Membr. Biol. , vol.156 , pp. 213-229
    • Laver, D.R.1    Baynes, T.M.2    Dulhunty, A.F.3
  • 47
    • 4444298467 scopus 로고    scopus 로고
    • Sudden death in familial polymorphic ventricular tachycardia associated with calcium release channel (ryanodine receptor) leak
    • Lehnart, S.E., X.H. Wehrens, P.J. Laitinen, S.R. Reiken, S.X. Deng, Z. Cheng, D.W. Landry, K. Kontula, H. Swan, and A.R. Marks. 2004. Sudden death in familial polymorphic ventricular tachycardia associated with calcium release channel (ryanodine receptor) leak. Circulation. 109:3208-3214. http://dx.doi.org/10.1161/01.CIR.0000132472.98675.EC
    • (2004) Circulation , vol.109 , pp. 3208-3214
    • Lehnart, S.E.1    Wehrens, X.H.2    Laitinen, P.J.3    Reiken, S.R.4    Deng, S.X.5    Cheng, Z.6    Landry, D.W.7    Kontula, K.8    Swan, H.9    Marks, A.R.10
  • 48
    • 0022496352 scopus 로고
    • Adenosine-sensitive ventricular tachycardia: evidence suggesting cyclic AMP-mediated triggered activity
    • Lerman, B.B., L. Belardinelli, G.A. West, R.M. Berne, and J.P. DiMarco. 1986. Adenosine-sensitive ventricular tachycardia: evidence suggesting cyclic AMP-mediated triggered activity. Circulation. 74:270-280. http://dx.doi.org/10.1161/01.CIR.74.2.270
    • (1986) Circulation , vol.74 , pp. 270-280
    • Lerman, B.B.1    Belardinelli, L.2    West, G.A.3    Berne, R.M.4    DiMarco, J.P.5
  • 49
    • 85047676838 scopus 로고
    • One hump or two? The triggering of calcium release from the sarcoplasmic reticulum and the voltage dependence of contraction in mammalian cardiac muscle
    • Levi, A.J., P. Brooksby, and J.C. Hancox. 1993. One hump or two? The triggering of calcium release from the sarcoplasmic reticulum and the voltage dependence of contraction in mammalian cardiac muscle. Cardiovasc. Res. 27:1743-1757. http://dx.doi.org/10.1093/cvr/27.10.1743
    • (1993) Cardiovasc. Res. , vol.27 , pp. 1743-1757
    • Levi, A.J.1    Brooksby, P.2    Hancox, J.C.3
  • 50
  • 51
    • 0029824241 scopus 로고    scopus 로고
    • Regulation of calcium release by calcium inside the sarcoplasmic reticulum in ventricular myocytes
    • Lukyanenko, V., I. Györke, and S. Györke. 1996. Regulation of calcium release by calcium inside the sarcoplasmic reticulum in ventricular myocytes. Pflugers Arch. 432:1047-1054. http://dx.doi.org/10.1007/s004240050233
    • (1996) Pflugers Arch. , vol.432 , pp. 1047-1054
    • Lukyanenko, V.1    Györke, I.2    Györke, S.3
  • 55
    • 0021341974 scopus 로고
    • 2+ release in sarcoplasmic reticulum
    • 2+ release in sarcoplasmic reticulum. J. Biol. Chem. 259:2365-2374.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2365-2374
    • Meissner, G.1
  • 57
    • 0034906940 scopus 로고    scopus 로고
    • 2+, and regulation of ion pumps in ventricular myocyte
    • 2+, and regulation of ion pumps in ventricular myocyte. Biophys. J. 81:614-629. http://dx.doi.org/10.1016/S0006-3495(01)75727-X
    • (2001) Biophys. J. , vol.81 , pp. 614-629
    • Michailova, A.1    McCulloch, A.2
  • 58
    • 0023818533 scopus 로고
    • 2+ binding effects on protein conformation and protein interactions of canine cardiac calsequestrin
    • 2+ binding effects on protein conformation and protein interactions of canine cardiac calsequestrin. J. Biol. Chem. 263:1376-1381.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1376-1381
    • Mitchell, R.D.1    Simmerman, H.K.2    Jones, L.R.3
  • 59
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod, J., J. Wyman, and J.P. Changeux. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118. http://dx.doi.org/10.1016/S0022-2836(65)80285-6
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 61
    • 0025123804 scopus 로고
    • Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel
    • Nakai, J., T. Imagawa, Y. Hakamat, M. Shigekawa, H. Takeshima, and S. Numa. 1990. Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel. FEBS Lett. 271:169-177. http://dx.doi.org/10.1016/0014-5793(90)80399-4
    • (1990) FEBS Lett. , vol.271 , pp. 169-177
    • Nakai, J.1    Imagawa, T.2    Hakamat, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 63
    • 2342444645 scopus 로고    scopus 로고
    • Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization
    • Park, H., I.Y. Park, E. Kim, B. Youn, K. Fields, A.K. Dunker, and C. Kang. 2004. Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization. J. Biol. Chem. 279:18026-18033. http://dx.doi.org/10.1074/jbc.M311553200
    • (2004) J. Biol. Chem. , vol.279 , pp. 18026-18033
    • Park, H.1    Park, I.Y.2    Kim, E.3    Youn, B.4    Fields, K.5    Dunker, A.K.6    Kang, C.7
  • 65
    • 1542613385 scopus 로고    scopus 로고
    • Cellular basis of triggered arrhythmias in heart failure
    • Pogwizd, S.M., and D.M. Bers. 2004. Cellular basis of triggered arrhythmias in heart failure. Trends Cardiovasc. Med. 14:61-66. http://dx.doi.org/10.1016/j.tcm.2003.12.002
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 61-66
    • Pogwizd, S.M.1    Bers, D.M.2
  • 66
    • 0035827719 scopus 로고    scopus 로고
    • Arrhythmogenesis and contractile dysfunction in heart failure: roles of sodium-calcium exchange, inward rectifier potassium current, and residual beta-adrenergic responsiveness
    • Pogwizd, S.M., K. Schlotthauer, L. Li, W. Yuan, and D.M. Bers. 2001. Arrhythmogenesis and contractile dysfunction in heart failure: roles of sodium-calcium exchange, inward rectifier potassium current, and residual beta-adrenergic responsiveness. Circ. Res. 88:1159-1167. http://dx.doi.org/10.1161/hh1101.091193
    • (2001) Circ. Res. , vol.88 , pp. 1159-1167
    • Pogwizd, S.M.1    Schlotthauer, K.2    Li, L.3    Yuan, W.4    Bers, D.M.5
  • 69
    • 0022930996 scopus 로고
    • 2+ flux measurements of the cardiac sarcoplasmic reticulum calcium channel
    • 2+ flux measurements of the cardiac sarcoplasmic reticulum calcium channel. Biophys. J. 50:1009-1014. http://dx.doi.org/10.1016/S0006-3495(86)83543-3
    • (1986) Biophys. J. , vol.50 , pp. 1009-1014
    • Rousseau, E.1    Smith, J.S.2    Henderson, J.S.3    Meissner, G.4
  • 70
    • 0034036663 scopus 로고    scopus 로고
    • Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration
    • Shannon, T.R., K.S. Ginsburg, and D.M. Bers. 2000. Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration. Biophys. J. 78:334-343. http://dx.doi.org/10.1016/S0006-3495(00)76596-9
    • (2000) Biophys. J. , vol.78 , pp. 334-343
    • Shannon, T.R.1    Ginsburg, K.S.2    Bers, D.M.3
  • 73
    • 0026504464 scopus 로고
    • Buffering of calcium in the vicinity of a channel pore
    • Stern, M.D. 1992a. Buffering of calcium in the vicinity of a channel pore. Cell Calcium. 13:183-192. http://dx.doi.org/10.1016/0143-4160(92)90046-U
    • (1992) Cell Calcium , vol.13 , pp. 183-192
    • Stern, M.D.1
  • 74
    • 0026733599 scopus 로고
    • Theory of excitation-contraction coupling in cardiac muscle
    • Stern, M.D. 1992b. Theory of excitation-contraction coupling in cardiac muscle. Biophys. J. 63:497-517. http://dx.doi.org/10.1016/S0006-3495(92)81615-6
    • (1992) Biophys. J. , vol.63 , pp. 497-517
    • Stern, M.D.1
  • 77
    • 33745032863 scopus 로고    scopus 로고
    • Abnormal interactions of calsequestrin with the ryanodine receptor calcium release channel complex linked to exercise-induced sudden cardiac death
    • Terentyev, D., A. Nori, M. Santoro, S. Viatchenko-Karpinski, Z. Kubalova, I. Gyorke, R. Terentyeva, S. Vedamoorthyrao, N.A. Blom, G. Valle, et al. 2006. Abnormal interactions of calsequestrin with the ryanodine receptor calcium release channel complex linked to exercise-induced sudden cardiac death. Circ. Res. 98:1151-1158. http://dx.doi.org/10.1161/01.RES.0000220647.93982.08
    • (2006) Circ. Res. , vol.98 , pp. 1151-1158
    • Terentyev, D.1    Nori, A.2    Santoro, M.3    Viatchenko-Karpinski, S.4    Kubalova, Z.5    Gyorke, I.6    Terentyeva, R.7    Vedamoorthyrao, S.8    Blom, N.A.9    Valle, G.10
  • 79
    • 16244420082 scopus 로고    scopus 로고
    • Magnesium deficiency in critical illness
    • Tong, G.M., and R.K. Rude. 2005. Magnesium deficiency in critical illness. J. Intensive Care Med. 20:3-17. http://dx.doi.org/10.1177/0885066604271539
    • (2005) J. Intensive Care Med. , vol.20 , pp. 3-17
    • Tong, G.M.1    Rude, R.K.2
  • 82
    • 77952491660 scopus 로고    scopus 로고
    • Catecholaminergic polymorphic ventricular tachycardia is caused by mutation-linked defective conformational regulation of the ryanodine receptor
    • Uchinoumi, H., M. Yano, T. Suetomi, M. Ono, X. Xu, H. Tateishi, T. Oda, S. Okuda, M. Doi, S. Kobayashi, et al. 2010. Catecholaminergic polymorphic ventricular tachycardia is caused by mutation-linked defective conformational regulation of the ryanodine receptor. Circ. Res. 106:1413-1424. http://dx.doi.org/10.1161/CIRCRESAHA.109.209312
    • (2010) Circ. Res. , vol.106 , pp. 1413-1424
    • Uchinoumi, H.1    Yano, M.2    Suetomi, T.3    Ono, M.4    Xu, X.5    Tateishi, H.6    Oda, T.7    Okuda, S.8    Doi, M.9    Kobayashi, S.10
  • 84
    • 67349175061 scopus 로고    scopus 로고
    • Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle
    • Wei, L., A.D. Hanna, N.A. Beard, and A.F. Dulhunty. 2009. Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle. Cell Calcium. 45:474-484. http://dx.doi.org/10.1016/j.ceca.2009.03.006
    • (2009) Cell Calcium , vol.45 , pp. 474-484
    • Wei, L.1    Hanna, A.D.2    Beard, N.A.3    Dulhunty, A.F.4
  • 85
    • 0031751235 scopus 로고    scopus 로고
    • 2+
    • 2+. Biophys. J. 75:2302-2312. http://dx.doi.org/10.1016/S0006-3495(98)77674-X
    • (1998) Biophys. J. , vol.75 , pp. 2302-2312
    • Xu, L.1    Meissner, G.2
  • 86
    • 77950517152 scopus 로고    scopus 로고
    • Defective calmodulin binding to the cardiac ryanodine receptor plays a key role in CPVT-associated channel dysfunction
    • Xu, X., M. Yano, H. Uchinoumi, A. Hino, T. Suetomi, M. Ono, H. Tateishi, T. Oda, S. Okuda, M. Doi, et al. 2010. Defective calmodulin binding to the cardiac ryanodine receptor plays a key role in CPVT-associated channel dysfunction. Biochem. Biophys. Res. Commun. 394:660-666. http://dx.doi.org/10.1016/j.bbrc.2010.03.046
    • (2010) Biochem. Biophys. Res. Commun. , vol.394 , pp. 660-666
    • Xu, X.1    Yano, M.2    Uchinoumi, H.3    Hino, A.4    Suetomi, T.5    Ono, M.6    Tateishi, H.7    Oda, T.8    Okuda, S.9    Doi, M.10
  • 87
    • 27644494432 scopus 로고    scopus 로고
    • Calcium activation of ryanodine receptor channels-reconciling RyR gating models with tetrameric channel structure
    • Zahradník, I., S. Györke, and A. Zahradníková. 2005. Calcium activation of ryanodine receptor channels-reconciling RyR gating models with tetrameric channel structure. J. Gen. Physiol. 126:515-527. http://dx.doi.org/10.1085/jgp.200509328
    • (2005) J. Gen. Physiol. , vol.126 , pp. 515-527
    • Zahradník, I.1    Györke, S.2    Zahradníková, A.3
  • 89
    • 77954326098 scopus 로고    scopus 로고
    • Frequency and release flux of calcium sparks in rat cardiac myocytes: a relation to RYR gating
    • Zahradníková, A., I. Valent, and I. Zahradník. 2010. Frequency and release flux of calcium sparks in rat cardiac myocytes: a relation to RYR gating. J. Gen. Physiol. 136:101-116. http://dx.doi.org/10.1085/jgp.200910380
    • (2010) J. Gen. Physiol. , vol.136 , pp. 101-116
    • Zahradníková, A.1    Valent, I.2    Zahradník, I.3
  • 90
    • 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., J. Kelley, G. Schmeisser, Y.M. Kobayashi, and L.R. Jones. 1997. Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J. Biol. Chem. 272:23389-23397. http://dx.doi.org/10.1074/jbc.272.37.23389
    • (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


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