메뉴 건너뛰기




Volumn 587, Issue 18, 2009, Pages 4523-4541

The Qγ component of intra-membrane charge movement is present in mammalian muscle fibres, but suppressed in the absence of S100A1

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM CHANNEL L TYPE; DANTROLENE; RYANODINE RECEPTOR 1; S100A1 PROTEIN; UNCLASSIFIED DRUG; PROTEIN S 100; RYANODINE RECEPTOR; CADMIUM; CALGRANULIN C; COBALT;

EID: 70450172741     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2009.177238     Document Type: Article
Times cited : (29)

References (63)
  • 2
    • 0016886087 scopus 로고
    • Charge movement in the membrane of striated muscle
    • Adrian RH, Almers W. Charge movement in the membrane of striated muscle. J Physiol 1976, 254:339-360.
    • (1976) J Physiol , vol.254 , pp. 339-360
    • Adrian, R.H.1    Almers, W.2
  • 3
    • 0017786466 scopus 로고
    • A gating signal for the potassium channel?
    • Adrian RH, Peres AR. A gating signal for the potassium channel?. Nature 1977, 267:800-804.
    • (1977) Nature , vol.267 , pp. 800-804
    • Adrian, R.H.1    Peres, A.R.2
  • 4
    • 0025597928 scopus 로고
    • Modification of sodium channel gating by lanthanum. Some effects that cannot be explained by surface charge theory
    • Armstrong CM, Cota G. Modification of sodium channel gating by lanthanum. Some effects that cannot be explained by surface charge theory. J Gen Physiol 1990, 96:1129-1140.
    • (1990) J Gen Physiol , vol.96 , pp. 1129-1140
    • Armstrong, C.M.1    Cota, G.2
  • 5
    • 0034113889 scopus 로고    scopus 로고
    • Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca2+ channel
    • Avila G, Dirksen RT. Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca2+ channel. J Gen Physiol 2000, 115:467-480.
    • (2000) J Gen Physiol , vol.115 , pp. 467-480
    • Avila, G.1    Dirksen, R.T.2
  • 6
    • 24344463053 scopus 로고    scopus 로고
    • The α1S N-terminus is not essential for bi-directional coupling with RyR1
    • Bannister RA, Beam KG. The α1S N-terminus is not essential for bi-directional coupling with RyR1. Biochem Biophys Res Commun 2005, 336:134-141.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 134-141
    • Bannister, R.A.1    Beam, K.G.2
  • 7
    • 41649094851 scopus 로고    scopus 로고
    • Rem inhibits skeletal muscle EC coupling by reducing the number of functional L-type Ca2+ channels
    • Bannister RA, Colecraft HM, Beam KG. Rem inhibits skeletal muscle EC coupling by reducing the number of functional L-type Ca2+ channels. Biophys J 2008, 94:2631-2638.
    • (2008) Biophys J , vol.94 , pp. 2631-2638
    • Bannister, R.A.1    Colecraft, H.M.2    Beam, K.G.3
  • 8
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • Block BA, Imagawa T, Campbell KP, 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 1988, 107:2587-2600.
    • (1988) J Cell Biol , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 9
    • 0016870470 scopus 로고
    • A non-linear voltage dependent charge movement in frog skeletal muscle
    • Chandler WK, Rakowski RF, Schneider MF. A non-linear voltage dependent charge movement in frog skeletal muscle. J Physiol 1976, 254:245-283.
    • (1976) J Physiol , vol.254 , pp. 245-283
    • Chandler, W.K.1    Rakowski, R.F.2    Schneider, M.F.3
  • 10
    • 0025850997 scopus 로고
    • Interfering with calcium release suppresses Iγ, the 'hump' component of intramembranous charge movement in skeletal muscle
    • Csernoch L, Pizarro G, Uribe I, Rodríguez M, Ríos E. Interfering with calcium release suppresses Iγ, the 'hump' component of intramembranous charge movement in skeletal muscle. J Gen Physiol 1991, 97:845-884.
    • (1991) J Gen Physiol , vol.97 , pp. 845-884
    • Csernoch, L.1    Pizarro, G.2    Uribe, I.3    Rodríguez, M.4    Ríos, E.5
  • 11
    • 0026323792 scopus 로고
    • Calcium current and charge movement of mammalian muscle: action of amyotrophic lateral sclerosis immunoglobulins
    • Delbono O, García J, Appel SH, Stefani E. Calcium current and charge movement of mammalian muscle: action of amyotrophic lateral sclerosis immunoglobulins. J Physiol 1991, 444:723-742.
    • (1991) J Physiol , vol.444 , pp. 723-742
    • Delbono, O.1    García, J.2    Appel, S.H.3    Stefani, E.4
  • 13
    • 0035890173 scopus 로고    scopus 로고
    • Separation of charge movement components in mammalian skeletal muscle fibres
    • Francini F, Bencini C, Piperio C, Squecco R. Separation of charge movement components in mammalian skeletal muscle fibres. J Physiol 2001, 537:45-56.
    • (2001) J Physiol , vol.537 , pp. 45-56
    • Francini, F.1    Bencini, C.2    Piperio, C.3    Squecco, R.4
  • 14
    • 0025785721 scopus 로고
    • Effect of the calcium buffer EGTA on the 'hump' component of charge movement in skeletal muscle
    • García J, Pizarro G, Ríos E, Stefani E. Effect of the calcium buffer EGTA on the 'hump' component of charge movement in skeletal muscle. J Gen Physiol 1991, 97:885-896.
    • (1991) J Gen Physiol , vol.97 , pp. 885-896
    • García, J.1    Pizarro, G.2    Ríos, E.3    Stefani, E.4
  • 15
    • 0027371768 scopus 로고
    • Perchlorate enhances transmission in skeletal muscle excitation-contraction coupling
    • Gonzalez A, Rios E. Perchlorate enhances transmission in skeletal muscle excitation-contraction coupling. J Gen Physiol 1993, 102:373-421.
    • (1993) J Gen Physiol , vol.102 , pp. 373-421
    • Gonzalez, A.1    Rios, E.2
  • 17
    • 0023165042 scopus 로고
    • S100a0 (alpha alpha) protein, a calcium-binding protein, is localized in the slow-twitch muscle fibre
    • Haimoto H, Kato K. S100a0 (alpha alpha) protein, a calcium-binding protein, is localized in the slow-twitch muscle fibre. J Neurochem 1987, 48:917-923.
    • (1987) J Neurochem , vol.48 , pp. 917-923
    • Haimoto, H.1    Kato, K.2
  • 18
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill OP, Marty A, Neher E, Sakmann B, Sigworth FJ. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch 1981, 391:85-100.
    • (1981) Pflugers Arch , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 19
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin AL, Huxley AF. A quantitative description of membrane current and its application to conduction and excitation in nerve. J Physiol 1952, 117:500-544.
    • (1952) J Physiol , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 20
    • 0019731776 scopus 로고
    • A comparative study of charge movement in rat and frog skeletal muscle fibres
    • Hollingworth S, Marshall MW. A comparative study of charge movement in rat and frog skeletal muscle fibres. J Physiol 1981, 321:583-602.
    • (1981) J Physiol , vol.321 , pp. 583-602
    • Hollingworth, S.1    Marshall, M.W.2
  • 21
    • 0025055721 scopus 로고
    • The effects of tetracaine on charge movement in fast twitch rat skeletal muscle fibres
    • Hollingworth S, Marshall MW, Robson E. The effects of tetracaine on charge movement in fast twitch rat skeletal muscle fibres. J Physiol 1990, 421:633-644.
    • (1990) J Physiol , vol.421 , pp. 633-644
    • Hollingworth, S.1    Marshall, M.W.2    Robson, E.3
  • 22
    • 0019393649 scopus 로고
    • Membrane charge moved at contraction thresholds in skeletal muscle fibres
    • Horowicz P, Schneider MF. Membrane charge moved at contraction thresholds in skeletal muscle fibres. J Physiol 1981a, 314:595-633.
    • (1981) J Physiol , vol.314 , pp. 595-633
    • Horowicz, P.1    Schneider, M.F.2
  • 23
    • 0019393653 scopus 로고
    • Membrane charge movement in contracting and non-contracting skeletal muscle fibres
    • Horowicz P, Schneider MF. Membrane charge movement in contracting and non-contracting skeletal muscle fibres. J Physiol 1981b, 314:565-593.
    • (1981) J Physiol , vol.314 , pp. 565-593
    • Horowicz, P.1    Schneider, M.F.2
  • 24
    • 0023716276 scopus 로고
    • Intramembrane charge movements in skeletal muscle
    • Huang CL. Intramembrane charge movements in skeletal muscle. Physiol Rev 1988, 68:1197-1147.
    • (1988) Physiol Rev , vol.68 , pp. 1197-11147
    • Huang, C.L.1
  • 25
    • 0020646051 scopus 로고
    • Differential properties of two charge components in frog skeletal muscle
    • Hui CS. Differential properties of two charge components in frog skeletal muscle. J Physiol 1983, 337:531-552.
    • (1983) J Physiol , vol.337 , pp. 531-552
    • Hui, C.S.1
  • 26
    • 0024410004 scopus 로고
    • Postulated role of calsequestrin in the regulation of calcium release from sarcoplasmic reticulum
    • Ikemoto N, Ronjat M, Meszaros LG, Koshita M. Postulated role of calsequestrin in the regulation of calcium release from sarcoplasmic reticulum. Biochemistry 1989, 28:6764-6771.
    • (1989) Biochemistry , vol.28 , pp. 6764-6771
    • Ikemoto, N.1    Ronjat, M.2    Meszaros, L.G.3    Koshita, M.4
  • 28
    • 0028802685 scopus 로고
    • Effect of sarcoplasmic reticulum calcium depletion on intramembranous charge movement in frog cut muscle fibres
    • Jong DS, Pape PC, Chandler WK. Effect of sarcoplasmic reticulum calcium depletion on intramembranous charge movement in frog cut muscle fibres. J Gen Physiol 1995, 106:659-704.
    • (1995) J Gen Physiol , vol.106 , pp. 659-704
    • Jong, D.S.1    Pape, P.C.2    Chandler, W.K.3
  • 29
    • 0018413294 scopus 로고
    • Calcium transients and intramembrane charge movement in skeletal muscle fibres
    • Kovacs L, Rios E, Schneider MF. Calcium transients and intramembrane charge movement in skeletal muscle fibres. Nature 1979, 279:391-396.
    • (1979) Nature , vol.279 , pp. 391-396
    • Kovacs, L.1    Rios, E.2    Schneider, M.F.3
  • 30
    • 0022558494 scopus 로고
    • Asymmetric charge movement in contracting muscle fibres in the rabbit
    • Lamb GD. Asymmetric charge movement in contracting muscle fibres in the rabbit. J Physiol 1986a, 376:63-83.
    • (1986) J Physiol , vol.376 , pp. 63-83
    • Lamb, G.D.1
  • 31
    • 0022558497 scopus 로고
    • Components of charge movement in rabbit skeletal muscle: the effect of tetracaine and nifedipine
    • Lamb GD. Components of charge movement in rabbit skeletal muscle: the effect of tetracaine and nifedipine. J Physiol 1986b, 376:85-100.
    • (1986) J Physiol , vol.376 , pp. 85-100
    • Lamb, G.D.1
  • 32
    • 0030851552 scopus 로고    scopus 로고
    • Calcium transients and calcium homeostasis in adult mouse fast-twitch skeletal muscle fibres in culture
    • Liu Y, Carroll SL, Klein MG, Schneider MF. Calcium transients and calcium homeostasis in adult mouse fast-twitch skeletal muscle fibres in culture. Am J Physiol Cell Physiol 1997, 272:C1919-1927.
    • (1997) Am J Physiol Cell Physiol , vol.272
    • Liu, Y.1    Carroll, S.L.2    Klein, M.G.3    Schneider, M.F.4
  • 33
    • 61649094240 scopus 로고    scopus 로고
    • α-Adrenergic signalling activates protein kinase D and causes nuclear efflux of the transcriptional repressor HDAC5 in cultured adult mouse soleus skeletal muscle fibres
    • Liu Y, Contreras M, Shen T, Randall WR, Schneider MF. α-Adrenergic signalling activates protein kinase D and causes nuclear efflux of the transcriptional repressor HDAC5 in cultured adult mouse soleus skeletal muscle fibres. J Physiol 2009, 587:1101-1115.
    • (2009) J Physiol , vol.587 , pp. 1101-1115
    • Liu, Y.1    Contreras, M.2    Shen, T.3    Randall, W.R.4    Schneider, M.F.5
  • 34
    • 0028180422 scopus 로고
    • Ryanodine receptor/Ca2+ release channels and their regulation by endogenous effectors
    • Meissner G. Ryanodine receptor/Ca2+ release channels and their regulation by endogenous effectors. Annu Rev Physiol 1994, 56:485-508.
    • (1994) Annu Rev Physiol , vol.56 , pp. 485-508
    • Meissner, G.1
  • 35
    • 0022557258 scopus 로고
    • Intramembrane charge movement and calcium release in frog skeletal muscle
    • Melzer W, Schneider MF, Simon BJ, Szucs G. Intramembrane charge movement and calcium release in frog skeletal muscle. J Physiol 1986, 373:481-511.
    • (1986) J Physiol , vol.373 , pp. 481-511
    • Melzer, W.1    Schneider, M.F.2    Simon, B.J.3    Szucs, G.4
  • 36
  • 37
    • 0038374450 scopus 로고    scopus 로고
    • The C terminus (amino acids 75-94) and the linker region (amino acids 42-54) of the Ca2+-binding protein S100A1 differentially enhance sarcoplasmic Ca2+ release in murine skinned skeletal muscle fibres
    • Most P, Remppis A, Weber C, Bernotat J, Ehlermann P, Pleger ST, Kirsch W, Weber M, Uttenweiler D, Smith GL, Katus HA, Fink RH. The C terminus (amino acids 75-94) and the linker region (amino acids 42-54) of the Ca2+-binding protein S100A1 differentially enhance sarcoplasmic Ca2+ release in murine skinned skeletal muscle fibres. J Biol Chem 2003, 278:26356-26364.
    • (2003) J Biol Chem , vol.278 , pp. 26356-26364
    • Most, P.1    Remppis, A.2    Weber, C.3    Bernotat, J.4    Ehlermann, P.5    Pleger, S.T.6    Kirsch, W.7    Weber, M.8    Uttenweiler, D.9    Smith, G.L.10    Katus, H.A.11    Fink, R.H.12
  • 38
    • 34249882040 scopus 로고    scopus 로고
    • S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance
    • Most P, Remppis A, Pleger S, Katus H, Koch W. S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance. Am J Physiol Regul Integr Comp Physiol 2007, 293:R568-R577.
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.293
    • Most, P.1    Remppis, A.2    Pleger, S.3    Katus, H.4    Koch, W.5
  • 39
    • 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, Allen PD. Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature 1996, 380:72-75.
    • (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
  • 40
    • 0032577476 scopus 로고    scopus 로고
    • Two regions of the ryanodine receptor involved in coupling with L-type Ca2+ channels
    • Nakai J, Sekiguchi N, Rando TA, Allen PD, Beam KG. Two regions of the ryanodine receptor involved in coupling with L-type Ca2+ channels. J Biol Chem 1998, 273:13403-13406.
    • (1998) J Biol Chem , vol.273 , pp. 13403-13406
    • Nakai, J.1    Sekiguchi, N.2    Rando, T.A.3    Allen, P.D.4    Beam, K.G.5
  • 41
    • 0025800390 scopus 로고
    • The relationship between Qγ and Ca release from the sarcoplasmic reticulum in skeletal muscle
    • Pizarro G, Csernoch L, Uribe I, Rodríguez M, Ríos E. The relationship between Qγ and Ca release from the sarcoplasmic reticulum in skeletal muscle. J Gen Physiol 1991, 97:913-947.
    • (1991) J Gen Physiol , vol.97 , pp. 913-947
    • Pizarro, G.1    Csernoch, L.2    Uribe, I.3    Rodríguez, M.4    Ríos, E.5
  • 42
    • 0024359120 scopus 로고
    • The voltage sensor of excitation-contraction coupling in skeletal muscle. Ion dependence and selectivity
    • Pizarro G, Fitts R, Uribe I, Ríos E. The voltage sensor of excitation-contraction coupling in skeletal muscle. Ion dependence and selectivity. J Gen Physiol 1989, 94:405-428.
    • (1989) J Gen Physiol , vol.94 , pp. 405-428
    • Pizarro, G.1    Fitts, R.2    Uribe, I.3    Ríos, E.4
  • 44
    • 41949112396 scopus 로고    scopus 로고
    • S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling
    • Prosser B, Wright N, Hernandez-Ochoa E, Varney K, Liu Y, Olojo R, Zimmer D, Weber D, Schneider M. S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling. J Biol Chem 2007, 283:5046-5057.
    • (2007) J Biol Chem , vol.283 , pp. 5046-5057
    • Prosser, B.1    Wright, N.2    Hernandez-Ochoa, E.3    Varney, K.4    Liu, Y.5    Olojo, R.6    Zimmer, D.7    Weber, D.8    Schneider, M.9
  • 45
    • 70450189285 scopus 로고    scopus 로고
    • Simultaneous recording of intramembrane charge movement components and calcium release in wild-type and S100A-/- muscle fibres
    • Prosser B, Hernandez-Ochoa E, Zimmer D, Schneider M. Simultaneous recording of intramembrane charge movement components and calcium release in wild-type and S100A-/- muscle fibres. J Physiol 2009, 587:4543-4559.
    • (2009) J Physiol , vol.587 , pp. 4543-4559
    • Prosser, B.1    Hernandez-Ochoa, E.2    Zimmer, D.3    Schneider, M.4
  • 46
    • 0036930754 scopus 로고    scopus 로고
    • Multiple regions of RyR1 mediate functional and structural interactions with α1S-dihydropyridine receptors in skeletal muscle
    • Protasi F, Paolini C, Nakai J, Beam KG, Franzini-Armstrong C, Allen PD. Multiple regions of RyR1 mediate functional and structural interactions with α1S-dihydropyridine receptors in skeletal muscle. Biophys J 2002, 83:3230-3244.
    • (2002) Biophys J , vol.83 , pp. 3230-3244
    • Protasi, F.1    Paolini, C.2    Nakai, J.3    Beam, K.G.4    Franzini-Armstrong, C.5    Allen, P.D.6
  • 48
    • 0025809446 scopus 로고
    • Voltage sensor of excitation-contraction coupling in skeletal muscle
    • Ríos E, Pizarro G. Voltage sensor of excitation-contraction coupling in skeletal muscle. Physiol Rev 1991, 71:849-908.
    • (1991) Physiol Rev , vol.71 , pp. 849-908
    • Ríos, E.1    Pizarro, G.2
  • 49
    • 0042845835 scopus 로고    scopus 로고
    • Calmodulin modulates initiation but not termination of spontaneous Ca2+ sparks in frog skeletal muscle
    • Rodney GG, Schneider MF. Calmodulin modulates initiation but not termination of spontaneous Ca2+ sparks in frog skeletal muscle. Biophys J 2003, 85:921-932.
    • (2003) Biophys J , vol.85 , pp. 921-932
    • Rodney, G.G.1    Schneider, M.F.2
  • 50
    • 53249134525 scopus 로고    scopus 로고
    • Evolution and modulation of intracellular calcium release during long-lasting, depleting depolarization in mouse muscle
    • Royer L, Pouvreau S, Ríos E. Evolution and modulation of intracellular calcium release during long-lasting, depleting depolarization in mouse muscle. J Physiol 2008, 586:4609-4629.
    • (2008) J Physiol , vol.586 , pp. 4609-4629
    • Royer, L.1    Pouvreau, S.2    Ríos, E.3
  • 51
    • 0015856482 scopus 로고
    • Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling
    • Schneider MF, Chandler WK. Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling. Nature 1973, 242:244-246.
    • (1973) Nature , vol.242 , pp. 244-246
    • Schneider, M.F.1    Chandler, W.K.2
  • 52
    • 59449093461 scopus 로고    scopus 로고
    • Proper restoration of excitation-contraction coupling in the dihydropyridine receptor β1-null zebrafish relaxed is an exclusive function of the β1a subunit
    • Schredelseker J, Dayal A, Schwerte T, Franzini-Armstrong C, Grabner M. Proper restoration of excitation-contraction coupling in the dihydropyridine receptor β1-null zebrafish relaxed is an exclusive function of the β1a subunit. J Biol Chem 2009, 284:1242-1251.
    • (2009) J Biol Chem , vol.284 , pp. 1242-1251
    • Schredelseker, J.1    Dayal, A.2    Schwerte, T.3    Franzini-Armstrong, C.4    Grabner, M.5
  • 54
    • 0021961154 scopus 로고
    • Slow charge movement in mammalian skeletal muscle
    • Simon BJ, Beam KG. Slow charge movement in mammalian skeletal muscle. J Gen Physiol 1985, 85:1-19.
    • (1985) J Gen Physiol , vol.85 , pp. 1-19
    • Simon, B.J.1    Beam, K.G.2
  • 55
    • 0023723765 scopus 로고
    • Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA
    • Tanabe T, Beam KG, Powell JA, Numa S. Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA. Nature 1988, 336:134-139.
    • (1988) Nature , vol.336 , pp. 134-139
    • Tanabe, T.1    Beam, K.G.2    Powell, J.A.3    Numa, S.4
  • 57
    • 0029006108 scopus 로고
    • Calmodulin activation and inhibition of skeletal muscle Ca2+ release channel (ryanodine receptor)
    • Tripathy A, Xu L, Mann G, Meissner G. Calmodulin activation and inhibition of skeletal muscle Ca2+ release channel (ryanodine receptor). Biophys J 1995, 69:106-119.
    • (1995) Biophys J , vol.69 , pp. 106-119
    • Tripathy, A.1    Xu, L.2    Mann, G.3    Meissner, G.4
  • 58
    • 0031052246 scopus 로고    scopus 로고
    • Effect of lanthanum on voltage-dependent gating of a cloned mammalian neuronal potassium channel
    • Tytgat J, Daenens P. Effect of lanthanum on voltage-dependent gating of a cloned mammalian neuronal potassium channel. Brain Res 1997, 749:232-237.
    • (1997) Brain Res , vol.749 , pp. 232-237
    • Tytgat, J.1    Daenens, P.2
  • 59
    • 48249116367 scopus 로고    scopus 로고
    • Gene therapy in heart failure
    • Vinge LE, Raake PW, Koch WJ. Gene therapy in heart failure. Circ Res 2008, 102:1458-1470.
    • (2008) Circ Res , vol.102 , pp. 1458-1470
    • Vinge, L.E.1    Raake, P.W.2    Koch, W.J.3
  • 60
    • 0032750498 scopus 로고    scopus 로고
    • Patch-clamp recording of charge movement, Ca2+ current, and Ca2+ transients in adult skeletal muscle fibres
    • Wang ZM, Messi ML, Delbono O. Patch-clamp recording of charge movement, Ca2+ current, and Ca2+ transients in adult skeletal muscle fibres. Biophys J 1999, 77:2709-2716.
    • (1999) Biophys J , vol.77 , pp. 2709-2716
    • Wang, Z.M.1    Messi, M.L.2    Delbono, O.3
  • 61
    • 0036200714 scopus 로고    scopus 로고
    • Sustained overexpression of IGF-1 prevents age-dependent decrease in charge movement and intracellular Ca2+ in mouse skeletal muscle
    • Wang ZM, Messi ML, Delbono O. Sustained overexpression of IGF-1 prevents age-dependent decrease in charge movement and intracellular Ca2+ in mouse skeletal muscle. Biophys J 2002, 82:1338-1344.
    • (2002) Biophys J , vol.82 , pp. 1338-1344
    • Wang, Z.M.1    Messi, M.L.2    Delbono, O.3
  • 63
    • 0025943211 scopus 로고
    • Isolation of a rat S100 α cDNA and distribution of its mRNA in rat tissues
    • Zimmer DB, Song W, Zimmer WE. Isolation of a rat S100 α cDNA and distribution of its mRNA in rat tissues. Brain Res Bull 1991, 27:157-162.
    • (1991) Brain Res Bull , vol.27 , pp. 157-162
    • Zimmer, D.B.1    Song, W.2    Zimmer, W.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.