메뉴 건너뛰기




Volumn 114, Issue 4, 2014, Pages 706-716

Erratum: Trimeric Intracellular Cation Channels and Sarcoplasmic/Endoplasmic Reticulum Calcium Homeostasis (Circulation Research (2014) 114 (706-716) DOI: 10.1161/CIRCRESAHA.114.301816);Trimeric intracellular cation channels and sarcoplasmic/endoplasmic reticulum calcium homeostasis

Author keywords

inositol 1,4,5 trisphosphate receptors; ryanodine receptor calcium release channel

Indexed keywords

CATION CHANNEL; RYANODINE RECEPTOR; RYANODINE RECEPTOR 2; TRIMERIC INTRACELLULAR CATION CHANNEL A; TRIMERIC INTRACELLULAR CATION CHANNEL B; UNCLASSIFIED DRUG;

EID: 84894437193     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/RES.0000000000000350     Document Type: Erratum
Times cited : (43)

References (96)
  • 1
    • 79960672046 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca(2+) handling in excitable cells in health and disease
    • Stutzmann GE, Mattson MP. Endoplasmic reticulum Ca(2+) handling in excitable cells in health and disease. Pharmacol Rev. 2011;63:700-727
    • (2011) Pharmacol Rev , vol.63 , pp. 700-727
    • Stutzmann, G.E.1    Mattson, M.P.2
  • 2
    • 0033624484 scopus 로고    scopus 로고
    • Ca2+ signalling and muscle disease
    • MacLennan DH. Ca2+ signalling and muscle disease. Eur J Biochem. 2000;267:5291-5297
    • (2000) Eur J Biochem , vol.267 , pp. 5291-5297
    • MacLennan, D.H.1
  • 3
    • 0037059457 scopus 로고    scopus 로고
    • Calcium and cardiac rhythms: Physiological and pathophysiological
    • Bers DM. Calcium and cardiac rhythms: Physiological and pathophysiological. Circ Res. 2002;90:14-17
    • (2002) Circ Res , vol.90 , pp. 14-17
    • Bers, D.M.1
  • 4
    • 79954594124 scopus 로고    scopus 로고
    • Inherited dysfunction of sarcoplasmic reticulum Ca2+ handling and arrhythmogenesis
    • Priori SG, Chen SR. Inherited dysfunction of sarcoplasmic reticulum Ca2+ handling and arrhythmogenesis. Circ Res. 2011;108:871-883
    • (2011) Circ Res , vol.108 , pp. 871-883
    • Priori, S.G.1    Chen, S.R.2
  • 6
    • 60849117498 scopus 로고    scopus 로고
    • New molecular components supporting ryanodine receptor-mediated Ca(2+) release: Roles of junctophilin and TRIC channel in embryonic cardiomyocytes
    • Yamazaki D, Yamazaki T, Takeshima H. New molecular components supporting ryanodine receptor-mediated Ca(2+) release: Roles of junctophilin and TRIC channel in embryonic cardiomyocytes. Pharmacol Ther. 2009;121:265-272
    • (2009) Pharmacol Ther , vol.121 , pp. 265-272
    • Yamazaki, D.1    Yamazaki, T.2    Takeshima, H.3
  • 7
    • 0037205752 scopus 로고    scopus 로고
    • Deficiency of triad formation in developing skeletal muscle cells lacking junctophilin type 1
    • Komazaki S, Ito K, Takeshima H, Nakamura H. Deficiency of triad formation in developing skeletal muscle cells lacking junctophilin type 1. FEBS Lett. 2002;524:225-229
    • (2002) FEBS Lett , vol.524 , pp. 225-229
    • Komazaki, S.1    Ito, K.2    Takeshima, H.3    Nakamura, H.4
  • 8
    • 19244382700 scopus 로고    scopus 로고
    • Intracellular Ca2+ store in embryonic cardiac myocytes
    • Takeshima H. Intracellular Ca2+ store in embryonic cardiac myocytes. Front Biosci. 2002;7:d1642-d1652
    • (2002) Front Biosci , vol.7
    • Takeshima, H.1
  • 9
    • 0038412004 scopus 로고    scopus 로고
    • Junctional membrane structure and store operated calcium entry in muscle cells
    • Ma J, Pan Z. Junctional membrane structure and store operated calcium entry in muscle cells. Front Biosci. 2003;8:d242-d255
    • (2003) Front Biosci , vol.8
    • Ma, J.1    Pan, Z.2
  • 10
    • 34548050205 scopus 로고    scopus 로고
    • Excitation-contraction coupling and mitochondrial energetics
    • Maack C, O'Rourke B. Excitation-contraction coupling and mitochondrial energetics. Basic Res Cardiol. 2007;102:369-392
    • (2007) Basic Res Cardiol , vol.102 , pp. 369-392
    • Maack, C.1    O'Rourke, B.2
  • 11
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers DM. Cardiac excitation-contraction coupling. Nature. 2002;415:198-205
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 12
    • 84855997901 scopus 로고    scopus 로고
    • Local control in cardiac E-C coupling
    • Cannell MB, Kong CH. Local control in cardiac E-C coupling. J Mol Cell Cardiol. 2012;52:298-303
    • (2012) J Mol Cell Cardiol , vol.52 , pp. 298-303
    • Cannell, M.B.1    Kong, C.H.2
  • 14
    • 0025869296 scopus 로고
    • The mechanical hypothesis of excitation-contraction (EC) coupling in skeletal muscle
    • Ríos E, Ma JJ, González A. The mechanical hypothesis of excitation-contraction (EC) coupling in skeletal muscle. J Muscle Res Cell Motil. 1991;12:127-135
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 127-135
    • Ríos, E.1    Ma, J.J.2    González, A.3
  • 15
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill M, Copello JA. Ryanodine receptor calcium release channels. Physiol Rev. 2002;82:893-922
    • (2002) Physiol Rev , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 17
    • 0019275433 scopus 로고
    • Decamethonium and hexamethonium block K+ channels of sarcoplasmic reticulum
    • Coronado R, Miller C. Decamethonium and hexamethonium block K+ channels of sarcoplasmic reticulum. Nature. 1980;288:495-497
    • (1980) Nature , vol.288 , pp. 495-497
    • Coronado, R.1    Miller, C.2
  • 18
    • 0021074418 scopus 로고
    • Spontaneous calcium release from sarcoplasmic reticulum. Effect of local anesthetics
    • Volpe P, Palade P, Costello B, Mitchell RD, Fleischer S. Spontaneous calcium release from sarcoplasmic reticulum. Effect of local anesthetics. J Biol Chem. 1983;258:12434-12442
    • (1983) J Biol Chem , vol.258 , pp. 12434-12442
    • Volpe, P.1    Palade, P.2    Costello, B.3    Mitchell, R.D.4    Fleischer, S.5
  • 19
    • 0022337165 scopus 로고
    • Potassium efflux from single skinned skeletal muscle fibers
    • Best PM, Abramcheck CW. Potassium efflux from single skinned skeletal muscle fibers. Biophys J. 1985;48:907-913
    • (1985) Biophys J. , vol.48 , pp. 907-913
    • Best, P.M.1    Abramcheck, C.W.2
  • 20
    • 0021227253 scopus 로고
    • The characterization of a monovalent cation-selective channel of mammalian cardiac muscle sarcoplasmic reticulum
    • Tomlins B, Williams AJ, Montgomery RA. The characterization of a monovalent cation-selective channel of mammalian cardiac muscle sarcoplasmic reticulum. J Membr Biol. 1984;80:191-199
    • (1984) J Membr Biol , vol.80 , pp. 191-199
    • Tomlins, B.1    Williams, A.J.2    Montgomery, R.A.3
  • 21
    • 0029986039 scopus 로고    scopus 로고
    • Calcium uptake and release modulated by counter-ion conductances in the sarcoplasmic reticulum of skeletal muscle
    • Fink RH, Veigel C. Calcium uptake and release modulated by counter-ion conductances in the sarcoplasmic reticulum of skeletal muscle. Acta Physiol Scand. 1996;156:387-396
    • (1996) Acta Physiol Scand , vol.156 , pp. 387-396
    • Fink, R.H.1    Veigel, C.2
  • 22
    • 0023389773 scopus 로고
    • Ca2+-movements in muscle modulated by the state of K+-channels in the sarcoplasmic reticulum membranes
    • Fink RH, Stephenson DG. Ca2+-movements in muscle modulated by the state of K+-channels in the sarcoplasmic reticulum membranes. Pflugers Arch. 1987;409:374-380
    • (1987) Pflugers Arch , vol.409 , pp. 374-380
    • Fink, R.H.1    Stephenson, D.G.2
  • 23
    • 0020035598 scopus 로고
    • Conduction and block by organic cations in a K+-selective channel from sarcoplasmic reticulum incorporated into planar phospholipid bilayers
    • Coronado R, Miller C. Conduction and block by organic cations in a K+-selective channel from sarcoplasmic reticulum incorporated into planar phospholipid bilayers. J Gen Physiol. 1982;79:529-547
    • (1982) J Gen Physiol , vol.79 , pp. 529-547
    • Coronado, R.1    Miller, C.2
  • 24
    • 0018958019 scopus 로고
    • Ionic selectivity, saturation, and block in a K+-selective channel from sarcoplasmic reticulum
    • Coronado R, Rosenberg RL, Miller C. Ionic selectivity, saturation, and block in a K+-selective channel from sarcoplasmic reticulum. J Gen Physiol. 1980;76:425-446
    • (1980) J Gen Physiol , vol.76 , pp. 425-446
    • Coronado, R.1    Rosenberg, R.L.2    Miller, C.3
  • 25
    • 0025971604 scopus 로고
    • Electrophysiological analysis of structural aspects of voltage-dependent SR K+ channel
    • Sokabe M, Kasai M, Nomura K, Naruse K. Electrophysiological analysis of structural aspects of voltage-dependent SR K+ channel. Comp Biochem Physiol C. 1991;98:23-30
    • (1991) Comp Biochem Physiol C. , vol.98 , pp. 23-30
    • Sokabe, M.1    Kasai, M.2    Nomura, K.3    Naruse, K.4
  • 26
    • 37849031506 scopus 로고    scopus 로고
    • Immuno-proteomic approach to excitation-contraction coupling in skeletal and cardiac muscle: Molecular insights revealed by the mitsugumins
    • Weisleder N, Takeshima H, Ma J. Immuno-proteomic approach to excitation-contraction coupling in skeletal and cardiac muscle: Molecular insights revealed by the mitsugumins. Cell Calcium. 2008;43:1-8
    • (2008) Cell Calcium , vol.43 , pp. 1-8
    • Weisleder, N.1    Takeshima, H.2    Ma, J.3
  • 27
    • 0032055099 scopus 로고    scopus 로고
    • Mitsugumin29, a novel synaptophysin family member from the triad junction in skeletal muscle
    • Takeshima H, Shimuta M, Komazaki S, Ohmi K, Nishi M, Iino M, Miyata A, Kangawa K. Mitsugumin29, a novel synaptophysin family member from the triad junction in skeletal muscle. Biochem J. 1998;331(Pt 1):317-322
    • (1998) Biochem J. , vol.331 , Issue.PART 1 , pp. 317-322
    • Takeshima, H.1    Shimuta, M.2    Komazaki, S.3    Ohmi, K.4    Nishi, M.5    Iino, M.6    Miyata, A.7    Kangawa, K.8
  • 28
    • 0035163660 scopus 로고    scopus 로고
    • Abnormal formation of sarcoplasmic reticulum networks and triads during early development of skeletal muscle cells in mitsugumin29-deficient mice
    • Komazaki S, Nishi M, Takeshima H, Nakamura H. Abnormal formation of sarcoplasmic reticulum networks and triads during early development of skeletal muscle cells in mitsugumin29-deficient mice. Dev Growth Differ. 2001;43:717-723
    • (2001) Dev Growth Differ , vol.43 , pp. 717-723
    • Komazaki, S.1    Nishi, M.2    Takeshima, H.3    Nakamura, H.4
  • 32
    • 51649127565 scopus 로고    scopus 로고
    • Altered Ca2+ sparks in aging skeletal and cardiac muscle
    • Weisleder N, Ma J. Altered Ca2+ sparks in aging skeletal and cardiac muscle. Ageing Res Rev. 2008;7:177-188
    • (2008) Ageing Res Rev , vol.7 , pp. 177-188
    • Weisleder, N.1    Ma, J.2
  • 34
    • 0035802106 scopus 로고    scopus 로고
    • Deficiency of triad junction and contraction in mutant skeletal muscle lacking junctophilin type 1
    • Ito K, Komazaki S, Sasamoto K, Yoshida M, Nishi M, Kitamura K, Takeshima H. Deficiency of triad junction and contraction in mutant skeletal muscle lacking junctophilin type 1. J Cell Biol. 2001;154:1059-1067
    • (2001) J Cell Biol , vol.154 , pp. 1059-1067
    • Ito, K.1    Komazaki, S.2    Sasamoto, K.3    Yoshida, M.4    Nishi, M.5    Kitamura, K.6    Takeshima, H.7
  • 36
    • 0033636778 scopus 로고    scopus 로고
    • Junctophilins: A novel family of junctional membrane complex proteins
    • Takeshima H, Komazaki S, Nishi M, Iino M, Kangawa K. Junctophilins: A novel family of junctional membrane complex proteins. Mol Cell. 2000;6:11-22
    • (2000) Mol Cell , vol.6 , pp. 11-22
    • Takeshima, H.1    Komazaki, S.2    Nishi, M.3    Iino, M.4    Kangawa, K.5
  • 37
    • 67650234246 scopus 로고    scopus 로고
    • Glutamate at position 227 of junctophilin-2 is involved in binding to TRPC3
    • Woo JS, Hwang JH, Ko JK, Kim do H, Ma J, Lee EH. Glutamate at position 227 of junctophilin-2 is involved in binding to TRPC3. Mol Cell Biochem. 2009;328:25-32
    • (2009) Mol Cell Biochem , vol.328 , pp. 25-32
    • Woo, J.S.1    Hwang, J.H.2    Ko, J.K.3    Kim Do, H.4    Ma, J.5    Lee, E.H.6
  • 44
    • 84862907349 scopus 로고    scopus 로고
    • Recombinant MG53 protein modulates therapeutic cell membrane repair in treatment of muscular dystrophy
    • Weisleder N, Takizawa N, Lin P, et al. Recombinant MG53 protein modulates therapeutic cell membrane repair in treatment of muscular dystrophy. Sci Transl Med. 2012;4:139ra85
    • (2012) Sci Transl Med , vol.4
    • Weisleder, N.1    Takizawa, N.2    Lin, P.3
  • 45
    • 77953587163 scopus 로고    scopus 로고
    • Mitsugumin 53 (MG53) facilitates vesicle trafficking in striated muscle to contribute to cell membrane repair
    • Weisleder N, Takeshima H, Ma J. Mitsugumin 53 (MG53) facilitates vesicle trafficking in striated muscle to contribute to cell membrane repair. Commun Integr Biol. 2009;2:225-226
    • (2009) Commun Integr Biol , vol.2 , pp. 225-226
    • Weisleder, N.1    Takeshima, H.2    Ma, J.3
  • 46
    • 67650133653 scopus 로고    scopus 로고
    • Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin
    • Cai C, Weisleder N, Ko JK, Komazaki S, Sunada Y, Nishi M, Takeshima H, Ma J. Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin. J Biol Chem. 2009;284:15894-15902
    • (2009) J Biol Chem , vol.284 , pp. 15894-15902
    • Cai, C.1    Weisleder, N.2    Ko, J.K.3    Komazaki, S.4    Sunada, Y.5    Nishi, M.6    Takeshima, H.7    Ma, J.8
  • 49
    • 79953836217 scopus 로고    scopus 로고
    • Polymerase transcriptase release factor (PTRF) anchors MG53 protein to cell injury site for initiation of membrane repair
    • Zhu H, Lin P, De G, Choi KH, Takeshima H, Weisleder N, Ma J. Polymerase transcriptase release factor (PTRF) anchors MG53 protein to cell injury site for initiation of membrane repair. J Biol Chem. 2011;286:12820-12824
    • (2011) J Biol Chem , vol.286 , pp. 12820-12824
    • Zhu, H.1    Lin, P.2    De G Choi, K.H.3    Takeshima, H.4    Weisleder, N.5    Ma, J.6
  • 50
    • 77953812567 scopus 로고    scopus 로고
    • MG53 constitutes a primary determinant of cardiac ischemic preconditioning
    • Cao CM, Zhang Y, Weisleder N, et al. MG53 constitutes a primary determinant of cardiac ischemic preconditioning. Circulation. 2010;121:2565-2574
    • (2010) Circulation , vol.121 , pp. 2565-2574
    • Cao, C.M.1    Zhang, Y.2    Weisleder, N.3
  • 53
    • 34447133622 scopus 로고    scopus 로고
    • TRIC channels are essential for Ca2+ handling in intracellular stores
    • Yazawa M, Ferrante C, Feng J, et al. TRIC channels are essential for Ca2+ handling in intracellular stores. Nature. 2007;448:78-82
    • (2007) Nature , vol.448 , pp. 78-82
    • Yazawa, M.1    Ferrante, C.2    Feng, J.3
  • 55
    • 84873445805 scopus 로고    scopus 로고
    • TRIC channels supporting efficient Ca(2+) release from intracellular stores
    • Venturi E, Sitsapesan R, Yamazaki D, Takeshima H. TRIC channels supporting efficient Ca(2+) release from intracellular stores. Pflugers Arch. 2013;465:187-195
    • (2013) Pflugers Arch , vol.465 , pp. 187-195
    • Venturi, E.1    Sitsapesan, R.2    Yamazaki, D.3    Takeshima, H.4
  • 57
    • 84883646491 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum K(+) (TRIC) channel does not carry essential countercurrent during Ca(2+) release
    • Guo T, Nani A, Shonts S, Perryman M, Chen H, Shannon T, Gillespie D, Fill M. Sarcoplasmic reticulum K(+) (TRIC) channel does not carry essential countercurrent during Ca(2+) release. Biophys J. 2013;105:1151-1160
    • (2013) Biophys J. , vol.105 , pp. 1151-1160
    • Guo, T.1    Nani, A.2    Shonts, S.3    Perryman, M.4    Chen, H.5    Shannon, T.6    Gillespie, D.7    Fill, M.8
  • 58
    • 84862783111 scopus 로고    scopus 로고
    • Is ryanodine receptor a calcium or magnesium channel? Roles of K+ and Mg2+ during Ca2+ release
    • Gillespie D, Chen H, Fill M. Is ryanodine receptor a calcium or magnesium channel? Roles of K+ and Mg2+ during Ca2+ release. Cell Calcium. 2012;51:427-433
    • (2012) Cell Calcium , vol.51 , pp. 427-433
    • Gillespie, D.1    Chen, H.2    Fill, M.3
  • 59
    • 56049089848 scopus 로고    scopus 로고
    • Intracellular calcium release channels mediate their own countercurrent: The ryanodine receptor case study
    • Gillespie D, Fill M. Intracellular calcium release channels mediate their own countercurrent: The ryanodine receptor case study. Biophys J. 2008;95:3706-3714
    • (2008) Biophys J. , vol.95 , pp. 3706-3714
    • Gillespie, D.1    Fill, M.2
  • 60
    • 0029072385 scopus 로고
    • Structure and function of glutamate and nicotinic acetylcholine receptors
    • Dani JA, Mayer ML. Structure and function of glutamate and nicotinic acetylcholine receptors. Curr Opin Neurobiol. 1995;5:310-317
    • (1995) Curr Opin Neurobiol , vol.5 , pp. 310-317
    • Dani, J.A.1    Mayer, M.L.2
  • 61
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining reentrant membrane loop
    • Bennett JA, Dingledine R. Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining reentrant membrane loop. Neuron. 1995;14:373-384
    • (1995) Neuron , vol.14 , pp. 373-384
    • Bennett, J.A.1    Dingledine, R.2
  • 62
    • 56049098367 scopus 로고    scopus 로고
    • Homotrimeric complexes are the dominant assembly state of native P2X7 subunits
    • Nicke A. Homotrimeric complexes are the dominant assembly state of native P2X7 subunits. Biochem Biophys Res Commun. 2008;377:803-808
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 803-808
    • Nicke, A.1
  • 63
    • 84880788993 scopus 로고    scopus 로고
    • A 3-dimensional trimeric β-barrel model for Chlamydia MOMP contains conserved and novel elements of Gram-negative bacterial porins
    • Feher VA, Randall A, Baldi P, Bush RM, de la Maza LM, Amaro RE. A 3-dimensional trimeric β-barrel model for Chlamydia MOMP contains conserved and novel elements of Gram-negative bacterial porins. PLoS One. 2013;8:e68934
    • (2013) PLoS One , vol.8
    • Feher, V.A.1    Randall, A.2    Baldi, P.3    Bush, R.M.4    De La Maza, L.M.5    Amaro, R.E.6
  • 65
    • 0021262493 scopus 로고
    • Channel-mediated monovalent cation fluxes in isolated sarcoplasmic reticulum vesicles
    • Garcia AM, Miller C. Channel-mediated monovalent cation fluxes in isolated sarcoplasmic reticulum vesicles. J Gen Physiol. 1984;83:819-839
    • (1984) J Gen Physiol , vol.83 , pp. 819-839
    • Garcia, A.M.1    Miller, C.2
  • 68
    • 0027234743 scopus 로고
    • Spontaneous myocardial calcium oscillations are they linked to ventricular fibrillation?
    • Lakatta EG, Guarnieri T. Spontaneous myocardial calcium oscillations: Are they linked to ventricular fibrillation? J Cardiovasc Electrophysiol. 1993;4:473-489
    • (1993) J Cardiovasc Electrophysiol , vol.4 , pp. 473-489
    • Lakatta, E.G.1    Guarnieri, T.2
  • 70
    • 0022968995 scopus 로고
    • Mechanisms of arrhythmogenic delayed and early afterdepolarizations in ferret ventricular muscle
    • Marban E, Robinson SW, Wier WG. Mechanisms of arrhythmogenic delayed and early afterdepolarizations in ferret ventricular muscle. J Clin Invest. 1986;78:1185-1192
    • (1986) J Clin Invest , vol.78 , pp. 1185-1192
    • Marban, E.1    Robinson, S.W.2    Wier, W.G.3
  • 71
    • 1542613385 scopus 로고    scopus 로고
    • Cellular basis of triggered arrhythmias in heart failure
    • Pogwizd SM, Bers DM. Cellular basis of triggered arrhythmias in heart failure. Trends Cardiovasc Med. 2004;14:61-66
    • (2004) Trends Cardiovasc Med , vol.14 , pp. 61-66
    • Pogwizd, S.M.1    Bers, D.M.2
  • 72
    • 0020642781 scopus 로고
    • Oscillations of intracellular Ca2+ in mammalian cardiac muscle
    • Orchard CH, Eisner DA, Allen DG. Oscillations of intracellular Ca2+ in mammalian cardiac muscle. Nature. 1983;304:735-738
    • (1983) Nature , vol.304 , pp. 735-738
    • Orchard, C.H.1    Eisner, D.A.2    Allen, D.G.3
  • 73
    • 79960943895 scopus 로고    scopus 로고
    • TRIC-A channels in vascular smooth muscle contribute to blood pressure maintenance
    • Yamazaki D, Tabara Y, Kita S, et al. TRIC-A channels in vascular smooth muscle contribute to blood pressure maintenance. Cell Metab. 2011;14:231-241
    • (2011) Cell Metab , vol.14 , pp. 231-241
    • Yamazaki, D.1    Tabara, Y.2    Kita, S.3
  • 74
    • 11144307984 scopus 로고    scopus 로고
    • Endothelin-1 and IP3 induced Ca2+ sparks in pulmonary arterial smooth muscle cells
    • Zhang WM, Lin MJ, Sham JS. Endothelin-1 and IP3 induced Ca2+ sparks in pulmonary arterial smooth muscle cells. J Cardiovasc Pharmacol. 2004;44(suppl 1):S121-S124
    • (2004) J Cardiovasc Pharmacol , vol.44 , Issue.SUPPL. 1
    • Zhang, W.M.1    Lin, M.J.2    Sham, J.S.3
  • 78
    • 0032526717 scopus 로고    scopus 로고
    • Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2
    • Takeshima H, Komazaki S, Hirose K, Nishi M, Noda T, Iino M. Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2. EMBO J. 1998;17:3309-3316
    • (1998) EMBO J. , vol.17 , pp. 3309-3316
    • Takeshima, H.1    Komazaki, S.2    Hirose, K.3    Nishi, M.4    Noda, T.5    Iino, M.6
  • 79
    • 84869462913 scopus 로고    scopus 로고
    • Does the 'coupled clock' make the heart tick?
    • Billman GE. Does the 'coupled clock' make the heart tick? Cardiovasc Res. 2012;96:343-344
    • (2012) Cardiovasc Res , vol.96 , pp. 343-344
    • Billman, G.E.1
  • 80
    • 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. 1992;311:245-262
    • (1992) Adv Exp Med Biol , vol.311 , pp. 245-262
    • Fabiato, A.1
  • 81
    • 85047679986 scopus 로고
    • Functional implications of spontaneous sarcoplasmic reticulum Ca2+ release in the heart
    • Lakatta EG. Functional implications of spontaneous sarcoplasmic reticulum Ca2+ release in the heart. Cardiovasc Res. 1992;26:193-214
    • (1992) Cardiovasc Res , vol.26 , pp. 193-214
    • Lakatta, E.G.1
  • 82
    • 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, Wang R, Xiao B, Kong H, Hunt DJ, Choi P, Zhang L, Chen SR. 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. 2005;97:1173-1181
    • (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
  • 83
    • 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, Xiao B, Yang D, Wang R, Choi P, Zhang L, Cheng H, Chen SR. RyR2 mutations linked to ventricular tachycardia and sudden death reduce the threshold for store-overload-induced Ca2+ release (SOICR). Proc Natl Acad Sci U S A. 2004;101:13062-13067
    • (2004) Proc Natl Acad Sci U S A. , vol.101 , pp. 13062-13067
    • Jiang, D.1    Xiao, B.2    Yang, D.3    Wang, R.4    Choi, P.5    Zhang, L.6    Cheng, H.7    Chen, S.R.8
  • 84
    • 0034721607 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum Ca(2+) release causes myocyte depolarization Underlying mechanism and threshold for triggered action potentials
    • Schlotthauer K, Bers DM. Sarcoplasmic reticulum Ca(2+) release causes myocyte depolarization. Underlying mechanism and threshold for triggered action potentials. Circ Res. 2000;87:774-780
    • (2000) Circ Res , vol.87 , pp. 774-780
    • Schlotthauer, K.1    Bers, D.M.2
  • 85
    • 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 SR. Loss of luminal Ca2+ activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death. Proc Natl Acad Sci U S A. 2007;104:18309-18314
    • (2007) Proc Natl Acad Sci U S A. , vol.104 , pp. 18309-18314
    • Jiang, D.1    Chen, W.2    Wang, R.3    Zhang, L.4    Chen, S.R.5
  • 86
    • 34347230164 scopus 로고    scopus 로고
    • Measuring calcium signaling using genetically targetable fluorescent indicators
    • Palmer AE, Tsien RY. Measuring calcium signaling using genetically targetable fluorescent indicators. Nat Protoc. 2006;1:1057-1065
    • (2006) Nat Protoc , vol.1 , pp. 1057-1065
    • Palmer, A.E.1    Tsien, R.Y.2
  • 87
    • 10644234677 scopus 로고    scopus 로고
    • Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor
    • Palmer AE, Jin C, Reed JC, Tsien RY. Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor. Proc Natl Acad Sci U S A. 2004;101:17404-17409
    • (2004) Proc Natl Acad Sci U S A. , vol.101 , pp. 17404-17409
    • Palmer, A.E.1    Jin, C.2    Reed, J.C.3    Tsien, R.Y.4
  • 88
    • 84870166972 scopus 로고    scopus 로고
    • Recessively inherited forms of osteogenesis imperfecta
    • Byers PH, Pyott SM. Recessively inherited forms of osteogenesis imperfecta. Annu Rev Genet. 2012;46:475-497
    • (2012) Annu Rev Genet , vol.46 , pp. 475-497
    • Byers, P.H.1    Pyott, S.M.2
  • 92
    • 1642524970 scopus 로고    scopus 로고
    • Inositol-1 4,5-Trisphosphate-dependent Ca(2+) signalling in cat atrial excitation-contraction coupling and arrhythmias
    • Zima AV, Blatter LA. Inositol-1,4,5-Trisphosphate-dependent Ca(2+) signalling in cat atrial excitation-contraction coupling and arrhythmias. J Physiol. 2004;555:607-615
    • (2004) J Physiol , vol.555 , pp. 607-615
    • Zima, A.V.1    Blatter, L.A.2
  • 95
    • 21844436786 scopus 로고    scopus 로고
    • Endothelin-1-induced arrhythmogenic Ca2+ signaling is abolished in atrial myocytes of inositol-1 4,5-Trisphosphate(IP3)-receptor type 2-deficient mice
    • Li X, Zima AV, Sheikh F, Blatter LA, Chen J. Endothelin-1-induced arrhythmogenic Ca2+ signaling is abolished in atrial myocytes of inositol-1,4,5-Trisphosphate(IP3)-receptor type 2-deficient mice. Circ Res. 2005;96:1274-1281
    • (2005) Circ Res , vol.96 , pp. 1274-1281
    • Li, X.1    Zima, A.V.2    Sheikh, F.3    Blatter, L.A.4    Chen, J.5
  • 96
    • 84873854873 scopus 로고    scopus 로고
    • Type 1 inositol 1,4,5)-Trisphosphate receptor activates ryanodine receptor 1 to mediate calcium spark signaling in adult mammalian skeletal muscle
    • Tjondrokoesoemo A, Li N, Lin PH, Pan Z, Ferrante CJ, Shirokova N, Brotto M, Weisleder N, Ma J. Type 1 inositol (1,4,5)-Trisphosphate receptor activates ryanodine receptor 1 to mediate calcium spark signaling in adult mammalian skeletal muscle. J Biol Chem. 2013;288:2103-2109
    • (2013) J Biol Chem , vol.288 , pp. 2103-2109
    • Tjondrokoesoemo, A.1    Li, N.2    Lin, P.H.3    Pan, Z.4    Ferrante, C.J.5    Shirokova, N.6    Brotto, M.7    Weisleder, N.8    Ma, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.