메뉴 건너뛰기




Volumn 20, Issue 2, 2014, Pages 184-192

The ryanodine receptor store-sensing gate controls Ca 2+ waves and Ca2+-triggered arrhythmias

(27)  Chen, Wenqian a   Wang, Ruiwu a   Chen, Biyi b   Zhong, Xiaowei a,f   Kong, Huihui a   Bai, Yunlong a,e   Zhou, Qiang a,e   Xie, Cuihong a,e,f   Zhang, Jingqun c   Guo, Ang b   Tian, Xixi a   Jones, Peter P a,e,g   O'Mara, Megan L a   Liu, Yingjie a   Mi, Tao a,f   Zhang, Lin a   Bolstad, Jeff a   Semeniuk, Lisa a   Cheng, Hongqiang d,e,h   Zhang, Jianlin d,e   more..


Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; ARRHYTHMIAS, CARDIAC; CAFFEINE; CALCIUM; DNA PRIMERS; ECHOCARDIOGRAPHY; GENE KNOCK-IN TECHNIQUES; HEK293 CELLS; HUMANS; IMMUNOBLOTTING; LIPID BILAYERS; MICE; MICROSCOPY, CONFOCAL; MUTAGENESIS, SITE-DIRECTED; MYOCYTES, CARDIAC; PATCH-CLAMP TECHNIQUES; POINT MUTATION; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL;

EID: 84893753403     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.3440     Document Type: Article
Times cited : (162)

References (74)
  • 1
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers, D.M. Cardiac excitation-contraction coupling. Nature 415, 198-205 (2002).
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 3
    • 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. 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 (1985).
    • (1985) J. Gen. Physiol. , vol.85 , pp. 247-289
    • Fabiato, A.1
  • 4
    • 43549098268 scopus 로고    scopus 로고
    • Calcium cycling and signaling in cardiac myocytes
    • Bers, D.M. Calcium cycling and signaling in cardiac myocytes. Annu. Rev. Physiol. 70, 23-49 (2008).
    • (2008) Annu. Rev. Physiol. , vol.70 , pp. 23-49
    • Bers, D.M.1
  • 5
    • 0025195367 scopus 로고
    • 'Quantal'Ca2+ release and the control of Ca2+ entry by inositol phosphates-a possible mechanism
    • Irvine, R.F. 'Quantal' Ca2+ release and the control of Ca2+ entry by inositol phosphates-a possible mechanism. FEBS Lett. 263, 5-9 (1990).
    • (1990) Febs Lett , vol.263 , pp. 5-9
    • Irvine, R.F.1
  • 6
    • 0025743351 scopus 로고
    • Spontaneous calcium release from inositol trisphosphate-sensitive calcium stores
    • Missiaen, L., Taylor, C.W. & Berridge, M.J. Spontaneous calcium release from inositol trisphosphate-sensitive calcium stores. Nature 352, 241-244 (1991).
    • (1991) Nature , vol.352 , pp. 241-244
    • Missiaen, L.1    Taylor, C.W.2    Berridge, M.J.3
  • 7
    • 0026615856 scopus 로고
    • Luminal Ca2+ promoting spontaneous Ca2+ release from inositol trisphosphate-sensitive stores in rat hepatocytes
    • Missiaen, L., Taylor, C.W. & Berridge, M.J. Luminal Ca2+ promoting spontaneous Ca2+ release from inositol trisphosphate-sensitive stores in rat hepatocytes. J. Physiol. (Lond.) 455, 623-640 (1992).
    • (1992) J. Physiol. (Lond.) , vol.455 , pp. 623-640
    • Missiaen, L.1    Taylor, C.W.2    Berridge, M.J.3
  • 8
    • 0026610728 scopus 로고
    • Luminal Ca2+ increases the sensitivity of Ca2+ stores to inositol 1 4,5-trisphosphate
    • Nunn, D.L. & Taylor, C.W. Luminal Ca2+ increases the sensitivity of Ca2+ stores to inositol 1,4,5-trisphosphate. Mol. Pharmacol. 41, 115-119 (1992).
    • (1992) Mol. Pharmacol. , vol.41 , pp. 115-119
    • Nunn, D.L.1    Taylor, C.W.2
  • 9
    • 0028230323 scopus 로고
    • Regulation of the gating of the sheep cardiac sarcoplasmic reticulum Ca2+-release channel by luminal Ca2+
    • Sitsapesan, R. & Williams, A. Regulation of the gating of the sheep cardiac sarcoplasmic reticulum Ca2+-release channel by luminal Ca2+. J. Membr. Biol. 137, 215-226 (1994).
    • (1994) J. Membr. Biol. , vol.137 , pp. 215-226
    • Sitsapesan, R.1    Williams, A.2
  • 10
    • 0029029280 scopus 로고
    • Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes
    • Bassani, J.W., Yuan, W., Bers, D.M. & Fractional, S.R. Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am. J. Physiol. 268, C1313-C1319 (1995).
    • (1995) Am. J. Physiol. , vol.268
    • Bassani, J.W.1    Yuan, W.2    Bers, D.M.3    Fractional, S.R.4
  • 11
    • 0141448292 scopus 로고    scopus 로고
    • Regulation of the cardiac ryanodine receptor channel by luminal Ca2+ involves luminal Ca2+ sensing sites
    • Györke, I. & Gyorke, S. Regulation of the cardiac ryanodine receptor channel by luminal Ca2+ involves luminal Ca2+ sensing sites. Biophys. J. 75, 2801-2810 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 2801-2810
    • Györke, I.1    Gyorke, S.2
  • 12
    • 0031751235 scopus 로고    scopus 로고
    • Regulation of cardiac muscle Ca2+ release channel by sarcoplasmic reticulum lumenal Ca2+
    • Xu, L. & Meissner, G. Regulation of cardiac muscle Ca2+ release channel by sarcoplasmic reticulum lumenal Ca2+. Biophys. J. 75, 2302-2312 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 2302-2312
    • Xu, L.1    Meissner, G.2
  • 13
    • 0034036663 scopus 로고    scopus 로고
    • Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration
    • Shannon, T.R., Ginsburg, K.S. & Bers, D.M. Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration. Biophys. J. 78, 334-343 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 334-343
    • Shannon, T.R.1    Ginsburg, K.S.2    Bers, D.M.3
  • 14
    • 4444357245 scopus 로고    scopus 로고
    • RyR2 mutations linked to ventricular tachycardia and sudden death reduce the threshold for store-overload-induced Ca2+ release (SOICR)
    • Jiang, D. et al. RyR2 mutations linked to ventricular tachycardia and sudden death reduce the threshold for store-overload-induced Ca2+ release (SOICR). Proc. Natl. Acad. Sci. USA 101, 13062-13067 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13062-13067
    • Jiang, D.1
  • 15
    • 33847621115 scopus 로고    scopus 로고
    • Calcium waves driven by sensitization wave-fronts
    • Keller, M., Kao, J.P., Egger, M. & Niggli, E. Calcium waves driven by "sensitization" wave-fronts. Cardiovasc. Res. 74, 39-45 (2007).
    • (2007) Cardiovasc. Res. , vol.74 , pp. 39-45
    • Keller, M.1    Kao, J.P.2    Egger, M.3    Niggli, E.4
  • 16
    • 34147113731 scopus 로고    scopus 로고
    • Skeletal and cardiac ryanodine receptors exhibit different responses to Ca2+ overload and luminal Ca2+
    • Kong, H. et al. Skeletal and cardiac ryanodine receptors exhibit different responses to Ca2+ overload and luminal Ca2+. Biophys. J. 92, 2757-2770 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 2757-2770
    • Kong, H.1
  • 17
    • 38849091360 scopus 로고    scopus 로고
    • Modulation of ryanodine receptor by luminal calcium and accessory proteins in health and cardiac disease
    • Györke, S. & Terentyev, D. Modulation of ryanodine receptor by luminal calcium and accessory proteins in health and cardiac disease. Cardiovasc. Res. 77, 245-255 (2008).
    • (2008) Cardiovasc. Res. , vol.77 , pp. 245-255
    • Györke, S.1    Terentyev, D.2
  • 18
    • 0019942895 scopus 로고
    • Fluctuations in membrane current driven by intracellular calcium in cardiac Purkinje fibers
    • Kass, R.S. & Tsien, R.W. Fluctuations in membrane current driven by intracellular calcium in cardiac Purkinje fibers. Biophys. J. 38, 259-269 (1982).
    • (1982) Biophys. J. , vol.38 , pp. 259-269
    • Kass, R.S.1    Tsien, R.W.2
  • 19
    • 0020642781 scopus 로고
    • Oscillations of intracellular Ca2+ in mammalian cardiac muscle
    • Orchard, C.H., Eisner, D. & Allen, D. Oscillations of intracellular Ca2+ in mammalian cardiac muscle. Nature 304, 735-738 (1983).
    • (1983) Nature , vol.304 , pp. 735-738
    • Orchard, C.H.1    Eisner, D.2    Allen, D.3
  • 20
    • 0020603463 scopus 로고
    • Scattered-light intensity fluctuations in diastolic rat cardiac muscle caused by spontaneous Ca2+-dependent cellular mechanical oscillations
    • Stern, M.D., Kort, A., Bhatnagar, G. & Lakatta, E. Scattered-light intensity fluctuations in diastolic rat cardiac muscle caused by spontaneous Ca2+-dependent cellular mechanical oscillations. J. Gen. Physiol. 82, 119-153 (1983).
    • (1983) J. Gen. Physiol. , vol.82 , pp. 119-153
    • Stern, M.D.1    Kort, A.2    Bhatnagar, G.3    Lakatta, E.4
  • 21
    • 0021014678 scopus 로고
    • Cellular calcium fluctuations in mammalian heart: Direct evidence from noise analysis of aequorin signals in Purkinje fibers
    • Wier, W.G., Kort, A., Stern, M., Lakatta, E. & Marban, E. Cellular calcium fluctuations in mammalian heart: direct evidence from noise analysis of aequorin signals in Purkinje fibers. Proc. Natl. Acad. Sci. USA 80, 7367-7371 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7367-7371
    • Wier, W.G.1    Kort, A.2    Stern, M.3    Lakatta, E.4    Marban, E.5
  • 22
    • 0022968995 scopus 로고
    • Mechanisms of arrhythmogenic delayed and early afterdepolarizations in ferret ventricular muscle
    • Marban, E., Robinson, S.W. & Wier, W.G. Mechanisms of arrhythmogenic delayed and early afterdepolarizations in ferret ventricular muscle. J. Clin. Invest. 78, 1185-1192 (1986).
    • (1986) J. Clin. Invest. , vol.78 , pp. 1185-1192
    • Marban, E.1    Robinson, S.W.2    Wier, W.G.3
  • 23
    • 0034721607 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum Ca2+ release causes myocyte depolarization. Underlying mechanism and threshold for triggered action potentials
    • Schlotthauer, K. & Bers, D.M. Sarcoplasmic reticulum Ca2+ release causes myocyte depolarization. Underlying mechanism and threshold for triggered action potentials. Circ. Res. 87, 774-780 (2000).
    • (2000) Circ. Res. , vol.87 , pp. 774-780
    • Schlotthauer, K.1    Bers, D.M.2
  • 24
    • 0037059457 scopus 로고    scopus 로고
    • Calcium and cardiac rhythms: Physiological and pathophysiological
    • Bers, D.M. Calcium and cardiac rhythms: physiological and pathophysiological. Circ. Res. 90, 14-17 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 14-17
    • Bers, D.M.1
  • 25
    • 1542613385 scopus 로고    scopus 로고
    • Cellular basis of triggered arrhythmias in heart failure
    • Pogwizd, S.M. & Bers, D.M. Cellular basis of triggered arrhythmias in heart failure. Trends Cardiovasc. Med. 14, 61-66 (2004).
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 61-66
    • Pogwizd, S.M.1    Bers, D.M.2
  • 26
    • 33644673205 scopus 로고    scopus 로고
    • Enhanced store overload-induced Ca2+ release and channel sensitivity to luminal Ca2+ activation are common defects of RyR2 mutations linked to ventricular tachycardia and sudden death
    • Jiang, D. et al. Enhanced store overload-induced Ca2+ release and channel sensitivity to luminal Ca2+ activation are common defects of RyR2 mutations linked to ventricular tachycardia and sudden death. Circ. Res. 97, 1173-1181 (2005).
    • (2005) Circ. Res. , vol.97 , pp. 1173-1181
    • Jiang, D.1
  • 27
    • 79954594124 scopus 로고    scopus 로고
    • Inherited dysfunction of sarcoplasmic reticulum Ca2+ handling and arrhythmogenesis
    • Priori, S.G. & Chen, S.R. Inherited dysfunction of sarcoplasmic reticulum Ca2+ handling and arrhythmogenesis. Circ. Res. 108, 871-883 (2011).
    • (2011) Circ. Res. , vol.108 , pp. 871-883
    • Priori, S.G.1    Chen, S.R.2
  • 28
    • 0028807878 scopus 로고
    • Relaxation of arterial smooth muscle by calcium sparks
    • Nelson, M.T. et al. Relaxation of arterial smooth muscle by calcium sparks. Science 270, 633-637 (1995).
    • (1995) Science , vol.270 , pp. 633-637
    • Nelson, M.T.1
  • 29
    • 77949379471 scopus 로고    scopus 로고
    • A coupled system of intracellular Ca2+ clocks and surface membrane voltage clocks controls the timekeeping mechanism of the heart's pacemaker
    • Lakatta, E.G., Maltsev, V.A. & Vinogradova, T.M. A coupled system of intracellular Ca2+ clocks and surface membrane voltage clocks controls the timekeeping mechanism of the heart's pacemaker. Circ. Res. 106, 659-673 (2010).
    • (2010) Circ. Res. , vol.106 , pp. 659-673
    • Lakatta, E.G.1    Maltsev, V.A.2    Vinogradova, T.M.3
  • 30
    • 1842373327 scopus 로고    scopus 로고
    • Measurement of sarcoplasmic reticulum Ca2+ content and sarcolemmal Ca2+ fluxes in isolated rat ventricular myocytes during spontaneous Ca2+ release
    • Díaz, M.E., Trafford, A.W., O'Neill, S.C. & Eisner, D.A. Measurement of sarcoplasmic reticulum Ca2+ content and sarcolemmal Ca2+ fluxes in isolated rat ventricular myocytes during spontaneous Ca2+ release. J. Physiol. (Lond.) 501, 3-16 (1997).
    • (1997) J. Physiol. (Lond.) , vol.501 , pp. 3-16
    • Díaz, M.E.1    Trafford, A.W.2    O'Neill, S.C.3    Eisner, D.A.4
  • 32
    • 0030068107 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum lumenal Ca2+ has access to cytosolic activation and inactivation sites of skeletal muscle Ca2+ release channel
    • Tripathy, A. & Meissner, G. Sarcoplasmic reticulum lumenal Ca2+ has access to cytosolic activation and inactivation sites of skeletal muscle Ca2+ release channel. Biophys. J. 70, 2600-2615 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 2600-2615
    • Tripathy, A.1    Meissner, G.2
  • 33
    • 36749047449 scopus 로고    scopus 로고
    • Loss of luminal Ca2+ activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death
    • Jiang, D., Chen, W., Wang, R., Zhang, L. & Chen, S.R.W. Loss of luminal Ca2+ activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death. Proc. Natl. Acad. Sci. USA 104, 18309-18314 (2007).
    • (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.W.5
  • 34
    • 34247882821 scopus 로고    scopus 로고
    • Ca2+ stores regulate ryanodine receptor Ca2+ release channels via luminal and cytosolic Ca2+ sites
    • Laver, D.R. Ca2+ stores regulate ryanodine receptor Ca2+ release channels via luminal and cytosolic Ca2+ sites. Biophys. J. 92, 3541-3555 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 3541-3555
    • Laver, D.R.1
  • 35
    • 73549088276 scopus 로고    scopus 로고
    • Flux regulation of cardiac ryanodine receptor channels
    • Liu, Y. et al. Flux regulation of cardiac ryanodine receptor channels. J. Gen. Physiol. 135, 15-27 (2010).
    • (2010) J. Gen. Physiol. , vol.135 , pp. 15-27
    • Liu, Y.1
  • 36
    • 1942423621 scopus 로고    scopus 로고
    • The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium
    • Györke, I., Hester, N., Jones, L.R. & Gyorke, S. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys. J. 86, 2121-2128 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 2121-2128
    • Györke, I.1    Hester, N.2    Jones, L.R.3    Gyorke, S.4
  • 37
    • 33748292955 scopus 로고    scopus 로고
    • Casq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardia
    • Knollmann, B.C. et al. Casq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardia. J. Clin. Invest. 116, 2510-2520 (2006).
    • (2006) J. Clin. Invest. , vol.116 , pp. 2510-2520
    • Knollmann, B.C.1
  • 38
    • 0030821712 scopus 로고    scopus 로고
    • Regulation of current flow through ryanodine receptors by luminal Ca2+
    • Sitsapesan, R. & Williams, A.J. Regulation of current flow through ryanodine receptors by luminal Ca2+. J. Membr. Biol. 159, 179-185 (1997).
    • (1997) J. Membr. Biol. , vol.159 , pp. 179-185
    • Sitsapesan, R.1    Williams, A.J.2
  • 39
    • 52449085476 scopus 로고    scopus 로고
    • Caffeine induces Ca2+ release by reducing the threshold for luminal Ca2+ activation of the ryanodine receptor
    • Kong, H. et al. Caffeine induces Ca2+ release by reducing the threshold for luminal Ca2+ activation of the ryanodine receptor. Biochem. J. 414, 441-452 (2008).
    • (2008) Biochem. J. , vol.414 , pp. 441-452
    • Kong, H.1
  • 40
    • 0033543667 scopus 로고    scopus 로고
    • Molecular identification of the ryanodine receptor pore-forming segment
    • Zhao, M. et al. Molecular identification of the ryanodine receptor pore-forming segment. J. Biol. Chem. 274, 25971-25974 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25971-25974
    • Zhao, M.1
  • 41
    • 0034981326 scopus 로고    scopus 로고
    • Light at the end of the Ca2+-release channel tunnel: Structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • Williams, A.J., West, D.J. & Sitsapesan, R. Light at the end of the Ca2+-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels. Q. Rev. Biophys. 34, 61-104 (2001).
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 42
    • 16644368098 scopus 로고    scopus 로고
    • A model of the putative pore region of the cardiac ryanodine receptor channel
    • Welch, W., Rheault, S., West, D.J. & Williams, A.J. A model of the putative pore region of the cardiac ryanodine receptor channel. Biophys. J. 87, 2335-2351 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 2335-2351
    • Welch, W.1    Rheault, S.2    West, D.J.3    Williams, A.J.4
  • 43
    • 33646171478 scopus 로고    scopus 로고
    • Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes
    • Xu, L., Wang, Y., Gillespie, D. & Meissner, G. Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes. Biophys. J. 90, 443-453 (2006).
    • (2006) Biophys. J. , vol.90 , pp. 443-453
    • Xu, L.1    Wang, Y.2    Gillespie, D.3    Meissner, G.4
  • 44
    • 67649637588 scopus 로고    scopus 로고
    • Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
    • Samsó, M., Feng, W., Pessah, I.N. & Allen, P.D. Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biol. 7, e85 (2009).
    • (2009) PLoS Biol. , vol.7
    • Samsó, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 45
    • 0032478818 scopus 로고    scopus 로고
    • The structure of the potassium channel: Molecular basis of K+ conduction and selectivity
    • Doyle, D.A. et al. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280, 69-77 (1998).
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 46
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S.B., Campbell, E.B. & Mackinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903 (2005).
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 47
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., Scheuer, T., Zheng, N. & Catterall, W.A. The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358 (2011).
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 48
    • 0034943174 scopus 로고    scopus 로고
    • Molecular basis of Ca2+ activation of the mouse cardiac Ca2+ release channel (ryanodine receptor)
    • Li, P. & Chen, S.R. Molecular basis of Ca2+ activation of the mouse cardiac Ca2+ release channel (ryanodine receptor). J. Gen. Physiol. 118, 33-44 (2001).
    • (2001) J. Gen. Physiol. , vol.118 , pp. 33-44
    • Li, P.1    Chen, S.R.2
  • 49
    • 33645318420 scopus 로고    scopus 로고
    • Atomic structure of a Na+-and K+-conducting channel
    • Shi, N., Ye, S., Alam, A., Chen, L. & Jiang, Y. Atomic structure of a Na+-and K+-conducting channel. Nature 440, 570-574 (2006).
    • (2006) Nature , vol.440 , pp. 570-574
    • Shi, N.1    Ye, S.2    Alam, A.3    Chen, L.4    Jiang, Y.5
  • 50
    • 79961153702 scopus 로고    scopus 로고
    • Carvedilol and its new analogs suppress arrhythmogenic store overload-induced Ca2+ release
    • Zhou, Q. et al. Carvedilol and its new analogs suppress arrhythmogenic store overload-induced Ca2+ release. Nat. Med. 17, 1003-1009 (2011).
    • (2011) Nat. Med. , vol.17 , pp. 1003-1009
    • Zhou, Q.1
  • 51
    • 33746788063 scopus 로고    scopus 로고
    • Arrhythmogenesis in catecholaminergic polymorphic ventricular tachycardia: Insights from a RyR2 R4496C knock-in mouse model
    • Liu, N. et al. Arrhythmogenesis in catecholaminergic polymorphic ventricular tachycardia: insights from a RyR2 R4496C knock-in mouse model. Circ. Res. 99, 292-298 (2006).
    • (2006) Circ. Res. , vol.99 , pp. 292-298
    • Liu, N.1
  • 52
    • 77955161545 scopus 로고    scopus 로고
    • Na+-dependent SR Ca2+ overload induces arrhythmogenic events in mouse cardiomyocytes with a human CPVT mutation
    • Sedej, S. et al. Na+-dependent SR Ca2+ overload induces arrhythmogenic events in mouse cardiomyocytes with a human CPVT mutation. Cardiovasc. Res. 87, 50-59 (2010).
    • (2010) Cardiovasc. Res. , vol.87 , pp. 50-59
    • Sedej, S.1
  • 53
    • 0021324453 scopus 로고
    • Spontaneous calcium release from sarcoplasmic reticulum. Assessment of other ionic influences
    • Mitchell, R.D., Palade, P. & Fleischer, S. Spontaneous calcium release from sarcoplasmic reticulum. Assessment of other ionic influences. J. Biol. Chem. 259, 1073-1081 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 1073-1081
    • Mitchell, R.D.1    Palade, P.2    Fleischer, S.3
  • 54
    • 0026377463 scopus 로고
    • Two kinds of calcium-induced release of calcium from the sarcoplasmic reticulum of skinned cardiac cells
    • Fabiato, A. Two kinds of calcium-induced release of calcium from the sarcoplasmic reticulum of skinned cardiac cells. Adv. Exp. Med. Biol. 311, 245-262 (1992).
    • (1992) Adv. Exp. Med. Biol. , vol.311 , pp. 245-262
    • Fabiato, A.1
  • 55
    • 64149085800 scopus 로고    scopus 로고
    • Flecainide prevents catecholaminergic polymorphic ventricular tachycardia in mice and humans
    • Watanabe, H. et al. Flecainide prevents catecholaminergic polymorphic ventricular tachycardia in mice and humans. Nat. Med. 15, 380-383 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 380-383
    • Watanabe, H.1
  • 56
    • 74149094943 scopus 로고    scopus 로고
    • Flecainide inhibits arrhythmogenic Ca2+ waves by open state block of ryanodine receptor Ca2+ release channels and reduction of Ca2+ spark mass
    • Hilliard, F.A. et al. Flecainide inhibits arrhythmogenic Ca2+ waves by open state block of ryanodine receptor Ca2+ release channels and reduction of Ca2+ spark mass. J. Mol. Cell. Cardiol. 48, 293-301 (2010).
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 293-301
    • Hilliard, F.A.1
  • 57
    • 0029130052 scopus 로고
    • The gating of the sheep skeletal sarcoplasmic reticulum Ca2+-release channel is regulated by luminal Ca2+
    • Sitsapesan, R. & Williams, A. The gating of the sheep skeletal sarcoplasmic reticulum Ca2+-release channel is regulated by luminal Ca2+. J. Membr. Biol. 146, 133-144 (1995).
    • (1995) J. Membr. Biol. , vol.146 , pp. 133-144
    • Sitsapesan, R.1    Williams, A.2
  • 58
    • 5144228939 scopus 로고    scopus 로고
    • Regulation of Ca2+ sparks by Ca2+ and Mg2+ in mammalian and amphibian muscle. An RyR isoform-specific role in excitation-contraction coupling?
    • Zhou, J., Launikonis, B.S., Rios, E. & Brum, G. Regulation of Ca2+ sparks by Ca2+ and Mg2+ in mammalian and amphibian muscle. An RyR isoform-specific role in excitation-contraction coupling? J. Gen. Physiol. 124, 409-428 (2004).
    • (2004) J. Gen. Physiol. , vol.124 , pp. 409-428
    • Zhou, J.1    Launikonis, B.S.2    Rios, E.3    Brum, G.4
  • 59
    • 45049087942 scopus 로고    scopus 로고
    • Full length ryanodine receptor subtype 3 encodes spontaneous calcium oscillations in native duodenal smooth muscle cells
    • Dabertrand, F., Mironneau, J., Macrez, N. & Morel, J.L. Full length ryanodine receptor subtype 3 encodes spontaneous calcium oscillations in native duodenal smooth muscle cells. Cell Calcium 44, 180-189 (2008).
    • (2008) Cell Calcium , vol.44 , pp. 180-189
    • Dabertrand, F.1    Mironneau, J.2    MacRez, N.3    Morel, J.L.4
  • 60
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 61
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato, A. & Fabiato, F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. (Paris) 75, 463-505 (1979).
    • (1979) J. Physiol. (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 62
    • 0037047646 scopus 로고    scopus 로고
    • Enhanced basal activity of a cardiac Ca2+ release channel (ryanodine receptor) mutant associated with ventricular tachycardia and sudden death
    • Jiang, D., Xiao, B., Zhang, L. & Chen, S.R. Enhanced basal activity of a cardiac Ca2+ release channel (ryanodine receptor) mutant associated with ventricular tachycardia and sudden death. Circ. Res. 91, 218-225 (2002).
    • (2002) Circ. Res. , vol.91 , pp. 218-225
    • Jiang, D.1    Xiao, B.2    Zhang, L.3    Chen, S.R.4
  • 63
    • 34250772834 scopus 로고    scopus 로고
    • K201 (JTV519) suppresses spontaneous Ca2+ release and [3H]ryanodine binding to RyR2 irrespective of FKBP12.6 association
    • Hunt, D.J. et al. K201 (JTV519) suppresses spontaneous Ca2+ release and [3H]ryanodine binding to RyR2 irrespective of FKBP12.6 association. Biochem. J. 404, 431-438 (2007).
    • (2007) Biochem. J. , vol.404 , pp. 431-438
    • Hunt, D.J.1
  • 65
    • 77956230883 scopus 로고    scopus 로고
    • T-tubule remodeling during transition from hypertrophy to heart failure
    • Wei, S. et al. T-tubule remodeling during transition from hypertrophy to heart failure. Circ. Res. 107, 520-531 (2010).
    • (2010) Circ. Res. , vol.107 , pp. 520-531
    • Wei, S.1
  • 66
    • 0036353834 scopus 로고    scopus 로고
    • Echocardiographic assessment of cardiac function in diabetic db/db and transgenic db/db-hGLUT4 mice
    • Semeniuk, L.M., Kryski, A.J. & Severson, D.L. Echocardiographic assessment of cardiac function in diabetic db/db and transgenic db/db-hGLUT4 mice. Am. J. Physiol. Heart Circ. Physiol. 283, H976-H982 (2002).
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283
    • Semeniuk, L.M.1    Kryski, A.J.2    Severson, D.L.3
  • 67
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-65 (1970).
    • (1970) Nature , vol.227 , pp. 680-765
    • Laemmli, U.K.1
  • 68
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-434 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4434
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 69
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. & Gibson, T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 70
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y. et al. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417, 515-522 (2002).
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1
  • 71
    • 0042622380 scopus 로고    scopus 로고
    • Swiss-model: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N. & Peitsch, M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 72
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.