메뉴 건너뛰기




Volumn 2, Issue 5, 2013, Pages 181-206

Molecular nature of voltage-gated calcium channels: Structure and species comparison

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; MESSENGER RNA; PROTEIN ZO1; RYANODINE RECEPTOR; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL; VOLTAGE GATED CALCIUM CHANNEL 1; VOLTAGE GATED CALCIUM CHANNEL 2; VOLTAGE GATED CALCIUM CHANNEL ALPHA1 SUBUNIT; VOLTAGE GATED CALCIUM CHANNEL ALPHA2DELTA SUBUNIT; VOLTAGE GATED CALCIUM CHANNEL BETA SUBUNIT;

EID: 84882643555     PISSN: 2190460X     EISSN: 21904618     Source Type: Journal    
DOI: 10.1002/wmts.91     Document Type: Review
Times cited : (25)

References (159)
  • 2
    • 0022916201 scopus 로고
    • Purification of a functional receptor for calcium-channel blockers from rabbit skeletal-muscle microsomes
    • Flockerzi V, Oeken HJ, Hofmann F. Purification of a functional receptor for calcium-channel blockers from rabbit skeletal-muscle microsomes. Eur J Biochem 1986, 161:217-224.
    • (1986) Eur J Biochem , vol.161 , pp. 217-224
    • Flockerzi, V.1    Oeken, H.J.2    Hofmann, F.3
  • 3
    • 0023198012 scopus 로고
    • The 165-kDa peptide of the purified skeletal muscle dihydropyridine receptor contains the known regulatory sites of the calcium channel
    • Sieber M, Nastainczyk W, Zubor V, Wernet W, Hofmann F. The 165-kDa peptide of the purified skeletal muscle dihydropyridine receptor contains the known regulatory sites of the calcium channel. Eur J Biochem 1987, 167:117-122.
    • (1987) Eur J Biochem , vol.167 , pp. 117-122
    • Sieber, M.1    Nastainczyk, W.2    Zubor, V.3    Wernet, W.4    Hofmann, F.5
  • 6
    • 0023656395 scopus 로고
    • Identification of a novel 1,4-dihydropyridine- and phenylalkylamine-binding polypeptide in calcium channel preparations
    • Vaghy PL, Striessnig J, Miwa K, Knaus H-J, Itagaki K, McKenna E, Glossmann H, Schwartz A. Identification of a novel 1, 4-dihydropyridine- and phenylalkylamine-binding polypeptide in calcium channel preparations. J Biol Chem 1987, 262:14337-14342.
    • (1987) J Biol Chem , vol.262 , pp. 14337-14342
    • Vaghy, P.L.1    Striessnig, J.2    Miwa, K.3    Knaus, H.-J.4    Itagaki, K.5    McKenna, E.6    Glossmann, H.7    Schwartz, A.8
  • 7
    • 0016734270 scopus 로고
    • Voltage clamp analysis of two inward current mechanisms in the egg cell membrane of a starfish
    • Hagiwara S, Ozawa S, Sand O. Voltage clamp analysis of two inward current mechanisms in the egg cell membrane of a starfish. J Gen Physiol 1975, 65:617-644.
    • (1975) J Gen Physiol , vol.65 , pp. 617-644
    • Hagiwara, S.1    Ozawa, S.2    Sand, O.3
  • 8
    • 0019393688 scopus 로고
    • Electrophysiology of mammalian inferior olivary neurones in vitro. Different types of voltage-dependent ionic conductances
    • Llinás R, Yarom Y. Electrophysiology of mammalian inferior olivary neurones in vitro. Different types of voltage-dependent ionic conductances. J Physiol (Lond) 1981, 315:549-567.
    • (1981) J Physiol (Lond) , vol.315 , pp. 549-567
    • Llinás, R.1    Yarom, Y.2
  • 9
    • 0021169994 scopus 로고
    • A low voltage-activated, fully inactivating Ca channel in vertebrate sensory neurones
    • Carbone E, Lux HD. A low voltage-activated, fully inactivating Ca channel in vertebrate sensory neurones. Nature 1984, 310:501-502.
    • (1984) Nature , vol.310 , pp. 501-502
    • Carbone, E.1    Lux, H.D.2
  • 11
    • 29844439240 scopus 로고    scopus 로고
    • International Union of Pharmacology XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels
    • Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J. International Union of Pharmacology XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels. Pharmacol Rev 2005, 57:411-425.
    • (2005) Pharmacol Rev , vol.57 , pp. 411-425
    • Catterall, W.A.1    Perez-Reyes, E.2    Snutch, T.P.3    Striessnig, J.4
  • 12
    • 0022413083 scopus 로고
    • Three types of neuronal calcium channel with different calcium agonist sensitivity
    • Nowycky MC, Fox AP, Tsien RW. Three types of neuronal calcium channel with different calcium agonist sensitivity. Nature 1985, 316:440-443.
    • (1985) Nature , vol.316 , pp. 440-443
    • Nowycky, M.C.1    Fox, A.P.2    Tsien, R.W.3
  • 13
    • 0023518468 scopus 로고
    • Kinetic and pharmacological properties distinguishing three types of calcium currents in chick sensory neurones
    • Fox AP, Nowycky MC, Tsien RW. Kinetic and pharmacological properties distinguishing three types of calcium currents in chick sensory neurones. J Physiol (Lond) 1987, 394:149-172.
    • (1987) J Physiol (Lond) , vol.394 , pp. 149-172
    • Fox, A.P.1    Nowycky, M.C.2    Tsien, R.W.3
  • 14
    • 0021749660 scopus 로고
    • Purification and sequence of a presynaptic peptide toxin from Conus geographus venom
    • Olivera BM, McIntosh JM, Cruz LJ, Luque FA, Gray WR. Purification and sequence of a presynaptic peptide toxin from Conus geographus venom. Biochemistry 1984, 23:5087-5090.
    • (1984) Biochemistry , vol.23 , pp. 5087-5090
    • Olivera, B.M.1    McIntosh, J.M.2    Cruz, L.J.3    Luque, F.A.4    Gray, W.R.5
  • 17
    • 0001492765 scopus 로고
    • Blocking and isolation of a calcium channel from neurons in mammals and cephalopods utilizing a toxin fraction (FTX) from funnel-web spider poison
    • Llinás R, Sugimori M, Lin JW, Cherksey B. Blocking and isolation of a calcium channel from neurons in mammals and cephalopods utilizing a toxin fraction (FTX) from funnel-web spider poison. Proc Natl Acad Sci U S A 1989, 86:1689-1693.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 1689-1693
    • Llinás, R.1    Sugimori, M.2    Lin, J.W.3    Cherksey, B.4
  • 18
    • 0026389190 scopus 로고
    • Properties of calcium channels isolated with spider toxin, FTX
    • Cherksey BD, Sugimori M, Llinás RR. Properties of calcium channels isolated with spider toxin, FTX. Ann N Y Acad Sci 1991, 635:80-89.
    • (1991) Ann N Y Acad Sci , vol.635 , pp. 80-89
    • Cherksey, B.D.1    Sugimori, M.2    Llinás, R.R.3
  • 20
    • 0028904492 scopus 로고
    • 2+ channel currents in rat cerebellar granule neurons
    • 2+ channel currents in rat cerebellar granule neurons. J Neurosci 1995, 15:2995-3012.
    • (1995) J Neurosci , vol.15 , pp. 2995-3012
    • Randall, A.1    Tsien, R.W.2
  • 22
    • 1642535342 scopus 로고    scopus 로고
    • Calcium channel α2δ subunits: differential expression, function, and drug binding
    • Klugbauer N, Marais E, Hofmann F. Calcium channel α2δ subunits: differential expression, function, and drug binding. J Bioenerg Biomembr 2003, 35:639-647.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 639-647
    • Klugbauer, N.1    Marais, E.2    Hofmann, F.3
  • 24
    • 0025881863 scopus 로고
    • Structural characterization of the dihydropyridine-sensitive calcium channel α 2-subunit and the associated δ peptides
    • Jay SD, Sharp AH, Kahl SD, Vedvick TS, Harpold MM, Campbell KP. Structural characterization of the dihydropyridine-sensitive calcium channel α 2-subunit and the associated δ peptides. J Biol Chem 1991, 266:3287-3293.
    • (1991) J Biol Chem , vol.266 , pp. 3287-3293
    • Jay, S.D.1    Sharp, A.H.2    Kahl, S.D.3    Vedvick, T.S.4    Harpold, M.M.5    Campbell, K.P.6
  • 26
    • 0034326854 scopus 로고    scopus 로고
    • 2+)-channel subunits and a class of prokaryotic chemotaxis receptors
    • 2+)-channel subunits and a class of prokaryotic chemotaxis receptors. Trends Biochem Sci 2000, 25:535-537.
    • (2000) Trends Biochem Sci , vol.25 , pp. 535-537
    • Anantharaman, V.1    Aravind, L.2
  • 27
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker CA, Hynes RO. Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol Biol Cell 2002, 13:3369-3387.
    • (2002) Mol Biol Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 29
    • 33845207422 scopus 로고    scopus 로고
    • Kinetics of internalization and degradation of N-type voltage-gated calcium channels: role of the α2/δ subunit
    • Bernstein GM, Jones OT. Kinetics of internalization and degradation of N-type voltage-gated calcium channels: role of the α2/δ subunit. Cell Calcium 2007, 41:27-40.
    • (2007) Cell Calcium , vol.41 , pp. 27-40
    • Bernstein, G.M.1    Jones, O.T.2
  • 31
    • 0028179146 scopus 로고
    • Calcium channel β-subunit binds to a conserved motif in the I-II cytoplasmic linker of the α 1-subunit
    • Pragnell M, De Waard M, Mori Y, Tanabe T, Snutch T, Campbell KP. Calcium channel β-subunit binds to a conserved motif in the I-II cytoplasmic linker of the α 1-subunit. Nature 1994, 368:67-70.
    • (1994) Nature , vol.368 , pp. 67-70
    • Pragnell, M.1    De Waard, M.2    Mori, Y.3    Tanabe, T.4    Snutch, T.5    Campbell, K.P.6
  • 32
    • 2942615325 scopus 로고    scopus 로고
    • Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain
    • Van Petegem F, Clark KA, Chatelain FC, Minor DL Jr. Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain. Nature 2004, 429:671-675.
    • (2004) Nature , vol.429 , pp. 671-675
    • Van Petegem, F.1    Clark, K.A.2    Chatelain, F.C.3    Minor Jr., D.L.4
  • 33
    • 0028020678 scopus 로고
    • Localization and functional properties of a rat brain α 1A calcium channel reflect similarities to neuronal Q- and P-type channels
    • Stea A, Tomlinson WJ, Soong TW, Bourinet E, Dubel SJ, Vincent SR, Snutch TP. Localization and functional properties of a rat brain α 1A calcium channel reflect similarities to neuronal Q- and P-type channels. Proc Natl Acad Sci U S A 1994, 91:10576-10580.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10576-10580
    • Stea, A.1    Tomlinson, W.J.2    Soong, T.W.3    Bourinet, E.4    Dubel, S.J.5    Vincent, S.R.6    Snutch, T.P.7
  • 34
    • 84864153599 scopus 로고    scopus 로고
    • Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond
    • Dolphin AC. Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond. Nat Rev Neurosci 2012, 13:542-555.
    • (2012) Nat Rev Neurosci , vol.13 , pp. 542-555
    • Dolphin, A.C.1
  • 39
    • 0026166996 scopus 로고
    • New insights into the structure and function of potassium channels
    • MacKinnon R. New insights into the structure and function of potassium channels. Curr Opin Neurobiol 1991, 1:14-19.
    • (1991) Curr Opin Neurobiol , vol.1 , pp. 14-19
    • MacKinnon, R.1
  • 40
    • 0026166997 scopus 로고
    • Structure and function of voltage-gated sodium and calcium channels
    • Catterall WA. Structure and function of voltage-gated sodium and calcium channels. Curr Opin Neurobiol 1991, 1:5-13.
    • (1991) Curr Opin Neurobiol , vol.1 , pp. 5-13
    • Catterall, W.A.1
  • 42
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh J, Scheuer T, Zheng N, Catterall WA. The crystal structure of a voltage-gated sodium channel. Nature 2011, 475:353-358.
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 43
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh J, El-Din TMG, Scheuer T, Zheng N, Catterall WA. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 2012, 486:135-139.
    • (2012) Nature , vol.486 , pp. 135-139
    • Payandeh, J.1    El-Din, T.M.G.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 46
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: structure, function, and pathophysiology
    • Catterall WA. Ion channel voltage sensors: structure, function, and pathophysiology. Neuron 2010, 67:915-928.
    • (2010) Neuron , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 47
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • Heinemann SH, Terlau H, Stühmer W, Imoto K, Numa S. Calcium channel characteristics conferred on the sodium channel by single mutations. Nature 1992, 356:441-443.
    • (1992) Nature , vol.356 , pp. 441-443
    • Heinemann, S.H.1    Terlau, H.2    Stühmer, W.3    Imoto, K.4    Numa, S.5
  • 51
    • 84857686131 scopus 로고    scopus 로고
    • 2+ signaling machinery in early animal and fungal evolution
    • 2+ signaling machinery in early animal and fungal evolution. Mol Biol Evol 2012, 29:91-100.
    • (2012) Mol Biol Evol , vol.29 , pp. 91-100
    • Cai, X.1    Clapham, D.E.2
  • 52
    • 0017332486 scopus 로고
    • Local anesthetics: hydrophilic and hydrophobic pathways for the drug-receptor reaction
    • Hille B. Local anesthetics: hydrophilic and hydrophobic pathways for the drug-receptor reaction. J Gen Physiol 1977, 69:497-515.
    • (1977) J Gen Physiol , vol.69 , pp. 497-515
    • Hille, B.1
  • 54
    • 0027944683 scopus 로고
    • Molecular determinants of state-dependent block of Na+ channels by local anesthetics
    • Ragsdale DS, McPhee JC, Scheuer T, Catterall WA. Molecular determinants of state-dependent block of Na+ channels by local anesthetics. Science 1994, 265:1724-1728.
    • (1994) Science , vol.265 , pp. 1724-1728
    • Ragsdale, D.S.1    McPhee, J.C.2    Scheuer, T.3    Catterall, W.A.4
  • 56
    • 22544474377 scopus 로고    scopus 로고
    • Phosphoinositide lipid second messengers: new paradigms for calcium channel modulation
    • Delmas P, Coste B, Gamper N, Shapiro MS. Phosphoinositide lipid second messengers: new paradigms for calcium channel modulation. Neuron 2005, 47:179-182.
    • (2005) Neuron , vol.47 , pp. 179-182
    • Delmas, P.1    Coste, B.2    Gamper, N.3    Shapiro, M.S.4
  • 57
    • 0033756777 scopus 로고    scopus 로고
    • μ-Conotoxin GIIIA interactions with the voltage-gated Na(+) channel predict a clockwise arrangement of the domains
    • Dudley SC Jr, Chang N, Hall J, Lipkind G, Fozzard HA, French RJ. μ-Conotoxin GIIIA interactions with the voltage-gated Na(+) channel predict a clockwise arrangement of the domains. J Gen Physiol 2000, 116:679-690.
    • (2000) J Gen Physiol , vol.116 , pp. 679-690
    • Dudley Jr., S.C.1    Chang, N.2    Hall, J.3    Lipkind, G.4    Fozzard, H.A.5    French, R.J.6
  • 58
    • 0032031204 scopus 로고    scopus 로고
    • Voltage-gated ion channels and electrical excitability
    • Armstrong CM, Hille B. Voltage-gated ion channels and electrical excitability. Neuron 1998, 20:371-380.
    • (1998) Neuron , vol.20 , pp. 371-380
    • Armstrong, C.M.1    Hille, B.2
  • 60
    • 0034643304 scopus 로고    scopus 로고
    • Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels
    • Ishibashi K, Suzuki M, Imai M. Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels. Biochem Biophys Res Commun 2000, 270:370-376.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 370-376
    • Ishibashi, K.1    Suzuki, M.2    Imai, M.3
  • 61
    • 77953916412 scopus 로고    scopus 로고
    • Two-pore channels: regulation by NAADP and customized roles in triggering calcium signals
    • Patel S, Marchant JS, Brailoiu E. Two-pore channels: regulation by NAADP and customized roles in triggering calcium signals. Cell Calcium 2010, 47:480-490.
    • (2010) Cell Calcium , vol.47 , pp. 480-490
    • Patel, S.1    Marchant, J.S.2    Brailoiu, E.3
  • 62
    • 0027497515 scopus 로고
    • Molecular evolution of voltage-sensitive ion channel genes: on the origins of electrical excitability
    • Strong M, Chandy KG, Gutman GA. Molecular evolution of voltage-sensitive ion channel genes: on the origins of electrical excitability. Mol Biol Evol 1993, 10:221-242.
    • (1993) Mol Biol Evol , vol.10 , pp. 221-242
    • Strong, M.1    Chandy, K.G.2    Gutman, G.A.3
  • 64
    • 79959328800 scopus 로고    scopus 로고
    • Evolution of sodium channels predates the origin of nervous systems in animals
    • Liebeskind BJ, Hillis DM, Zakon HH. Evolution of sodium channels predates the origin of nervous systems in animals. Proc Natl Acad Sci U S A 2011, 108:9154-9159.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9154-9159
    • Liebeskind, B.J.1    Hillis, D.M.2    Zakon, H.H.3
  • 65
    • 84866152524 scopus 로고    scopus 로고
    • Adaptive evolution of voltage-gated sodium channels: the first 800 million years
    • Zakon HH. Adaptive evolution of voltage-gated sodium channels: the first 800 million years. Proc Natl Acad Sci U S A 2012, 109(Suppl 1):10619-10625.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.SUPPL 1 , pp. 10619-10625
    • Zakon, H.H.1
  • 66
    • 84865716725 scopus 로고    scopus 로고
    • Convergent evolution of sodium ion selectivity in metazoan neuronal signaling
    • Gur Barzilai M et al. Convergent evolution of sodium ion selectivity in metazoan neuronal signaling. Cell Rep 2012, 2:242-248.
    • (2012) Cell Rep , vol.2 , pp. 242-248
    • Gur Barzilai, M.1
  • 67
    • 1342323398 scopus 로고    scopus 로고
    • Mammalian voltage-gated calcium channels are potently blocked by the pyrethroid insecticide allethrin
    • Hildebrand ME, McRory JE, Snutch TP, Stea A. Mammalian voltage-gated calcium channels are potently blocked by the pyrethroid insecticide allethrin. J Pharmacol Exp Ther 2004, 308:805-813.
    • (2004) J Pharmacol Exp Ther , vol.308 , pp. 805-813
    • Hildebrand, M.E.1    McRory, J.E.2    Snutch, T.P.3    Stea, A.4
  • 68
    • 84856949002 scopus 로고    scopus 로고
    • Molecular mechanisms of pyrethroid insecticide neurotoxicity: recent advances
    • Soderlund DM. Molecular mechanisms of pyrethroid insecticide neurotoxicity: recent advances. Arch Toxicol 2012, 86:165-181.
    • (2012) Arch Toxicol , vol.86 , pp. 165-181
    • Soderlund, D.M.1
  • 69
    • 33847403885 scopus 로고    scopus 로고
    • Modulation of insect Ca(v) channels by peptidic spider toxins
    • King GF. Modulation of insect Ca(v) channels by peptidic spider toxins. Toxicon 2007, 49:513-530.
    • (2007) Toxicon , vol.49 , pp. 513-530
    • King, G.F.1
  • 70
    • 79952546569 scopus 로고    scopus 로고
    • Mapping of dihydropyridine binding residues in a less sensitive invertebrate L-type calcium channel (LCa v 1)
    • Senatore A et al. Mapping of dihydropyridine binding residues in a less sensitive invertebrate L-type calcium channel (LCa v 1). Channels (Austin) 2011, 5:173-187.
    • (2011) Channels (Austin) , vol.5 , pp. 173-187
    • Senatore, A.1
  • 71
    • 78650842356 scopus 로고    scopus 로고
    • Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation
    • Minor DL Jr, Findeisen F. Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation. Channels (Austin) 2010, 4:459-474.
    • (2010) Channels (Austin) , vol.4 , pp. 459-474
    • Minor Jr., D.L.1    Findeisen, F.2
  • 76
  • 78
    • 0031020814 scopus 로고    scopus 로고
    • Molecular determinants of inactivation and G protein modulation in the intracellular loop connecting domains I and II of the calcium channel α1A subunit
    • Herlitze S, Hockerman GH, Scheuer T, Catterall WA. Molecular determinants of inactivation and G protein modulation in the intracellular loop connecting domains I and II of the calcium channel α1A subunit. Proc Natl Acad Sci U S A 1997, 94:1512-1516.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1512-1516
    • Herlitze, S.1    Hockerman, G.H.2    Scheuer, T.3    Catterall, W.A.4
  • 79
    • 0035138426 scopus 로고    scopus 로고
    • Molecular determinants of inactivation within the I-II linker of α1E (CaV2.3) calcium channels
    • Berrou L, Bernatchez G, Parent L. Molecular determinants of inactivation within the I-II linker of α1E (CaV2.3) calcium channels. Biophys J 2001, 80:215-228.
    • (2001) Biophys J , vol.80 , pp. 215-228
    • Berrou, L.1    Bernatchez, G.2    Parent, L.3
  • 80
    • 0345185172 scopus 로고    scopus 로고
    • β Subunits of voltage-gated calcium channels
    • Dolphin AC. β Subunits of voltage-gated calcium channels. J Bioenerg Biomembr 2003, 35:599-620.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 599-620
    • Dolphin, A.C.1
  • 81
    • 0031033757 scopus 로고    scopus 로고
    • Direct binding of G-protein β γ complex to voltage-dependent calcium channels
    • De Waard M, Liu H, Walker D, Scott VE, Gurnett CA, Campbell KP. Direct binding of G-protein β γ complex to voltage-dependent calcium channels. Nature 1997, 385:446-450.
    • (1997) Nature , vol.385 , pp. 446-450
    • De Waard, M.1    Liu, H.2    Walker, D.3    Scott, V.E.4    Gurnett, C.A.5    Campbell, K.P.6
  • 82
    • 0031022543 scopus 로고    scopus 로고
    • Crosstalk between G proteins and protein kinase C mediated by the calcium channel α1 subunit
    • Zamponi GW, Bourinet E, Nelson D, Nargeot J, Snutch TP. Crosstalk between G proteins and protein kinase C mediated by the calcium channel α1 subunit. Nature 1997, 385:442-446.
    • (1997) Nature , vol.385 , pp. 442-446
    • Zamponi, G.W.1    Bourinet, E.2    Nelson, D.3    Nargeot, J.4    Snutch, T.P.5
  • 85
    • 0033566706 scopus 로고    scopus 로고
    • Identification of residues in the N terminus of α1B critical for inhibition of the voltage-dependent calcium channel by Gβγ
    • Cantí C, Page KM, Stephens GJ, Dolphin AC. Identification of residues in the N terminus of α1B critical for inhibition of the voltage-dependent calcium channel by Gβγ. J Neurosci 1999, 19:6855-6864.
    • (1999) J Neurosci , vol.19 , pp. 6855-6864
    • Cantí, C.1    Page, K.M.2    Stephens, G.J.3    Dolphin, A.C.4
  • 86
    • 4944261526 scopus 로고    scopus 로고
    • Functional role of a C-terminal Gβγ-binding domain of Ca(v)2.2 channels
    • Li B, Zhong H, Scheuer T, Catterall WA. Functional role of a C-terminal Gβγ-binding domain of Ca(v)2.2 channels. Mol Pharmacol 2004, 66:761-769.
    • (2004) Mol Pharmacol , vol.66 , pp. 761-769
    • Li, B.1    Zhong, H.2    Scheuer, T.3    Catterall, W.A.4
  • 88
    • 0028595727 scopus 로고
    • Identification of a syntaxin-binding site on N-type calcium channels
    • Sheng ZH, Rettig J, Takahashi M, Catterall WA. Identification of a syntaxin-binding site on N-type calcium channels. Neuron 1994, 13:1303-1313.
    • (1994) Neuron , vol.13 , pp. 1303-1313
    • Sheng, Z.H.1    Rettig, J.2    Takahashi, M.3    Catterall, W.A.4
  • 90
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof TC. The synaptic vesicle cycle. Annu Rev Neurosci 2004, 27:509-547.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 92
    • 77956632647 scopus 로고    scopus 로고
    • RIM proteins and their role in synapse function
    • Mittelstaedt T, Alvaréz-Baron E, Schoch S. RIM proteins and their role in synapse function. Biol Chem 2010, 391:599-606.
    • (2010) Biol Chem , vol.391 , pp. 599-606
    • Mittelstaedt, T.1    Alvaréz-Baron, E.2    Schoch, S.3
  • 94
    • 70849088180 scopus 로고    scopus 로고
    • An atypical role for collapsin response mediator protein 2 (CRMP-2) in neurotransmitter release via interaction with presynaptic voltage-gated calcium channels
    • Brittain JM, Piekarz AD, Wang Y, Kondo T, Cummins TR, Khanna R. An atypical role for collapsin response mediator protein 2 (CRMP-2) in neurotransmitter release via interaction with presynaptic voltage-gated calcium channels. J Biol Chem 2009, 284:31375-31390.
    • (2009) J Biol Chem , vol.284 , pp. 31375-31390
    • Brittain, J.M.1    Piekarz, A.D.2    Wang, Y.3    Kondo, T.4    Cummins, T.R.5    Khanna, R.6
  • 95
    • 84859912593 scopus 로고    scopus 로고
    • Regulation of voltage-gated calcium channels by synaptic proteins
    • Weiss N, Zamponi GW. Regulation of voltage-gated calcium channels by synaptic proteins. Adv Exp Med Biol 2012, 740:759-775.
    • (2012) Adv Exp Med Biol , vol.740 , pp. 759-775
    • Weiss, N.1    Zamponi, G.W.2
  • 100
    • 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
  • 103
    • 0028297589 scopus 로고
    • Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells
    • McDonald TF, Pelzer S, Trautwein W, Pelzer DJ. Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells. Physiol Rev 1994, 74:365-507.
    • (1994) Physiol Rev , vol.74 , pp. 365-507
    • McDonald, T.F.1    Pelzer, S.2    Trautwein, W.3    Pelzer, D.J.4
  • 104
    • 33750433556 scopus 로고    scopus 로고
    • The C terminus of the L-type voltage-gated calcium channel Ca(V)1.2 encodes a transcription factor
    • Gomez-Ospina N, Tsuruta F, Barreto-Chang O, Hu L, Dolmetsch R. The C terminus of the L-type voltage-gated calcium channel Ca(V)1.2 encodes a transcription factor. Cell 2006, 127:591-606.
    • (2006) Cell , vol.127 , pp. 591-606
    • Gomez-Ospina, N.1    Tsuruta, F.2    Barreto-Chang, O.3    Hu, L.4    Dolmetsch, R.5
  • 105
    • 33750067680 scopus 로고    scopus 로고
    • The role of voltage-gated calcium channels in pancreatic β-cell physiology and pathophysiology
    • Yang S-N, Berggren P-O. The role of voltage-gated calcium channels in pancreatic β-cell physiology and pathophysiology. Endocr Rev 2006, 27:621-676.
    • (2006) Endocr Rev , vol.27 , pp. 621-676
    • Yang, S.-N.1    Berggren, P.-O.2
  • 108
    • 78649863650 scopus 로고    scopus 로고
    • β-Adrenergic-regulated phosphorylation of the skeletal muscle Ca(V)1.1 channel in the fight-or-flight response
    • Emrick MA, Sadilek M, Konoki K, Catterall WA. β-Adrenergic-regulated phosphorylation of the skeletal muscle Ca(V)1.1 channel in the fight-or-flight response. Proc Natl Acad Sci U S A 2010, 107:18712-18717.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18712-18717
    • Emrick, M.A.1    Sadilek, M.2    Konoki, K.3    Catterall, W.A.4
  • 110
    • 17044424577 scopus 로고    scopus 로고
    • Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle
    • Hulme JT, Konoki K, Lin TW, Gritsenko MA, Camp DG 2nd, Bigelow DJ, Catterall WA. Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle. Proc Natl Acad Sci U S A 2005, 102:5274-5279.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5274-5279
    • Hulme, J.T.1    Konoki, K.2    Lin, T.W.3    Gritsenko, M.A.4    Camp II, D.G.5    Bigelow, D.J.6    Catterall, W.A.7
  • 111
    • 33748098546 scopus 로고    scopus 로고
    • Autoinhibitory control of the CaV1.2 channel by its proteolytically processed distal C-terminal domain
    • Hulme JT, Yarov-Yarovoy V, Lin TW-C, Scheuer T, Catterall WA. Autoinhibitory control of the CaV1.2 channel by its proteolytically processed distal C-terminal domain. J Physiol (Lond) 2006, 576:87-102.
    • (2006) J Physiol (Lond) , vol.576 , pp. 87-102
    • Hulme, J.T.1    Yarov-Yarovoy, V.2    Lin, T.-C.3    Scheuer, T.4    Catterall, W.A.5
  • 128
    • 23044459076 scopus 로고    scopus 로고
    • Modulation of CaV2.1 channels by the neuronal calcium-binding protein visinin-like protein-2
    • Lautermilch NJ, Few AP, Scheuer T, Catterall WA. Modulation of CaV2.1 channels by the neuronal calcium-binding protein visinin-like protein-2. J Neurosci 2005, 25:7062-7070.
    • (2005) J Neurosci , vol.25 , pp. 7062-7070
    • Lautermilch, N.J.1    Few, A.P.2    Scheuer, T.3    Catterall, W.A.4
  • 129
    • 0347224274 scopus 로고    scopus 로고
    • Cell-specific alternative splicing increases calcium channel current density in the pain pathway
    • Bell TJ, Thaler C, Castiglioni AJ, Helton TD, Lipscombe D. Cell-specific alternative splicing increases calcium channel current density in the pain pathway. Neuron 2004, 41:127-138.
    • (2004) Neuron , vol.41 , pp. 127-138
    • Bell, T.J.1    Thaler, C.2    Castiglioni, A.J.3    Helton, T.D.4    Lipscombe, D.5
  • 130
    • 3242732124 scopus 로고    scopus 로고
    • 2+ channels
    • 2+ channels. J Neurosci 2004, 24:6334-6342.
    • (2004) J Neurosci , vol.24 , pp. 6334-6342
    • Chaudhuri, D.1
  • 131
    • 0036337915 scopus 로고    scopus 로고
    • A genomic view of alternative splicing
    • Modrek B, Lee C. A genomic view of alternative splicing. Nat Genet 2002, 30:13-19.
    • (2002) Nat Genet , vol.30 , pp. 13-19
    • Modrek, B.1    Lee, C.2
  • 132
    • 0032247416 scopus 로고    scopus 로고
    • Evolutionary fates and origins of U12-type introns
    • Burge CB, Padgett RA, Sharp PA. Evolutionary fates and origins of U12-type introns. Mol Cell 1998, 2:773-785.
    • (1998) Mol Cell , vol.2 , pp. 773-785
    • Burge, C.B.1    Padgett, R.A.2    Sharp, P.A.3
  • 133
    • 0034326362 scopus 로고    scopus 로고
    • Analysis of canonical and non-canonical splice sites in mammalian genomes
    • Burset M, Seledtsov IA, Solovyev VV. Analysis of canonical and non-canonical splice sites in mammalian genomes. Nucleic Acids Res 2000, 28:4364-4375.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4364-4375
    • Burset, M.1    Seledtsov, I.A.2    Solovyev, V.V.3
  • 134
    • 77951120000 scopus 로고    scopus 로고
    • Alternative splicing and evolution: diversification, exon definition and function
    • Keren H, Lev-Maor G, Ast G. Alternative splicing and evolution: diversification, exon definition and function. Nat Rev Genet 2010, 11:345-355.
    • (2010) Nat Rev Genet , vol.11 , pp. 345-355
    • Keren, H.1    Lev-Maor, G.2    Ast, G.3
  • 135
    • 0025785489 scopus 로고
    • Distinct calcium channels are generated by alternative splicing and are differentially expressed in the mammalian CNS
    • Snutch TP, Tomlinson WJ, Leonard JP, Gilbert MM. Distinct calcium channels are generated by alternative splicing and are differentially expressed in the mammalian CNS. Neuron 1991, 7:45-57.
    • (1991) Neuron , vol.7 , pp. 45-57
    • Snutch, T.P.1    Tomlinson, W.J.2    Leonard, J.P.3    Gilbert, M.M.4
  • 136
    • 0036700498 scopus 로고    scopus 로고
    • Functional diversity in neuronal voltage-gated calcium channels by alternative splicing of Ca(v)α1
    • Lipscombe D, Pan JQ, Gray AC. Functional diversity in neuronal voltage-gated calcium channels by alternative splicing of Ca(v)α1. Mol Neurobiol 2002, 26:21-44.
    • (2002) Mol Neurobiol , vol.26 , pp. 21-44
    • Lipscombe, D.1    Pan, J.Q.2    Gray, A.C.3
  • 137
    • 84876889067 scopus 로고    scopus 로고
    • Alternative splicing: functional diversity among voltage-gated calcium channels and behavioral consequences
    • Lipscombe D, Andrade A, Allen SE. Alternative splicing: functional diversity among voltage-gated calcium channels and behavioral consequences. Biochim Biophys Acta-Biomembranes 2013, 1828:1522-1529.
    • (2013) Biochim Biophys Acta-Biomembranes , vol.1828 , pp. 1522-1529
    • Lipscombe, D.1    Andrade, A.2    Allen, S.E.3
  • 138
    • 34547928340 scopus 로고    scopus 로고
    • Neuronal calcium channels: splicing for optimal performance
    • Gray AC, Raingo J, Lipscombe D. Neuronal calcium channels: splicing for optimal performance. Cell Calcium 2007, 42:409-417.
    • (2007) Cell Calcium , vol.42 , pp. 409-417
    • Gray, A.C.1    Raingo, J.2    Lipscombe, D.3
  • 139
    • 77957745671 scopus 로고    scopus 로고
    • Splice-variant changes of the Ca(V)3.2 T-type calcium channel mediate voltage-dependent facilitation and associate with cardiac hypertrophy and development
    • David LS, Garcia E, Cain SM, Thau E, Tyson JR, Snutch TP. Splice-variant changes of the Ca(V)3.2 T-type calcium channel mediate voltage-dependent facilitation and associate with cardiac hypertrophy and development. Channels (Austin) 2010, 4:375-389.
    • (2010) Channels (Austin) , vol.4 , pp. 375-389
    • David, L.S.1    Garcia, E.2    Cain, S.M.3    Thau, E.4    Tyson, J.R.5    Snutch, T.P.6
  • 141
    • 36849031680 scopus 로고    scopus 로고
    • A smooth muscle Cav1.2 calcium channel splice variant underlies hyperpolarized window current and enhanced state-dependent inhibition by nifedipine
    • Liao P, Yu D, Li G, Yong TF, Soon JL, Chua YL, Soong TW. A smooth muscle Cav1.2 calcium channel splice variant underlies hyperpolarized window current and enhanced state-dependent inhibition by nifedipine. J Biol Chem 2007, 282:35133-35142.
    • (2007) J Biol Chem , vol.282 , pp. 35133-35142
    • Liao, P.1    Yu, D.2    Li, G.3    Yong, T.F.4    Soon, J.L.5    Chua, Y.L.6    Soong, T.W.7
  • 142
    • 35748981784 scopus 로고    scopus 로고
    • A novel Ca(V)1.2 N terminus expressed in smooth muscle cells of resistance size arteries modifies channel regulation by auxiliary subunits
    • Cheng X, Liu J, Asuncion-Chin M, Blaskova E, Bannister JP, Dopico AM, Jaggar JH. A novel Ca(V)1.2 N terminus expressed in smooth muscle cells of resistance size arteries modifies channel regulation by auxiliary subunits. J Biol Chem 2007, 282:29211-29221.
    • (2007) J Biol Chem , vol.282 , pp. 29211-29221
    • Cheng, X.1    Liu, J.2    Asuncion-Chin, M.3    Blaskova, E.4    Bannister, J.P.5    Dopico, A.M.6    Jaggar, J.H.7
  • 146
    • 84862971753 scopus 로고    scopus 로고
    • Alternative splicing at C terminus of Ca(V)1.4 calcium channel modulates calcium-dependent inactivation, activation potential, and current density
    • Tan GMY, Yu D, Wang J, Soong TW. Alternative splicing at C terminus of Ca(V)1.4 calcium channel modulates calcium-dependent inactivation, activation potential, and current density. J Biol Chem 2012, 287:832-847.
    • (2012) J Biol Chem , vol.287 , pp. 832-847
    • Tan, G.M.Y.1    Yu, D.2    Wang, J.3    Soong, T.W.4
  • 150
    • 0032826784 scopus 로고    scopus 로고
    • Structure and alternative splicing of the gene encoding α1G, a human brain T calcium channel α1 subunit
    • Mittman S, Guo J, Agnew WS. Structure and alternative splicing of the gene encoding α1G, a human brain T calcium channel α1 subunit. Neurosci Lett 1999, 274:143-146.
    • (1999) Neurosci Lett , vol.274 , pp. 143-146
    • Mittman, S.1    Guo, J.2    Agnew, W.S.3
  • 151
    • 33646159973 scopus 로고    scopus 로고
    • A profile of alternative RNA splicing and transcript variation of CACNA1H, a human T-channel gene candidate for idiopathic generalized epilepsies
    • Zhong X, Liu JR, Kyle JW, Hanck DA, Agnew WS. A profile of alternative RNA splicing and transcript variation of CACNA1H, a human T-channel gene candidate for idiopathic generalized epilepsies. Hum Mol Genet 2006, 15:1497-1512.
    • (2006) Hum Mol Genet , vol.15 , pp. 1497-1512
    • Zhong, X.1    Liu, J.R.2    Kyle, J.W.3    Hanck, D.A.4    Agnew, W.S.5
  • 152
    • 0033575449 scopus 로고    scopus 로고
    • Structure and alternative splicing of the gene encoding α1I, a human brain T calcium channel α1 subunit
    • Mittman S, Guo J, Emerick MC, Agnew WS. Structure and alternative splicing of the gene encoding α1I, a human brain T calcium channel α1 subunit. Neurosci Lett 1999, 269:121-124.
    • (1999) Neurosci Lett , vol.269 , pp. 121-124
    • Mittman, S.1    Guo, J.2    Emerick, M.C.3    Agnew, W.S.4
  • 153
    • 0028063942 scopus 로고
    • Critical roles of the S3 segment and S3-S4 linker of repeat I in activation of L-type calcium channels
    • Nakai J, Adams BA, Imoto K, Beam KG. Critical roles of the S3 segment and S3-S4 linker of repeat I in activation of L-type calcium channels. Proc Natl Acad Sci U S A 1994, 91:1014-1018.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1014-1018
    • Nakai, J.1    Adams, B.A.2    Imoto, K.3    Beam, K.G.4
  • 155
  • 156
    • 84862504084 scopus 로고    scopus 로고
    • Gene transcription and splicing of T-type channels are evolutionarily-conserved strategies for regulating channel expression and gating
    • Senatore A, Spafford JD. Gene transcription and splicing of T-type channels are evolutionarily-conserved strategies for regulating channel expression and gating. PLoS One 2012, 7:e37409.
    • (2012) PLoS One , vol.7
    • Senatore, A.1    Spafford, J.D.2
  • 157
    • 68849112458 scopus 로고    scopus 로고
    • Developmental control of CaV1.2 L-type calcium channel splicing by Fox proteins
    • Tang ZZ, Zheng S, Nikolic J, Black DL. Developmental control of CaV1.2 L-type calcium channel splicing by Fox proteins. Mol Cell Biol 2009, 29:4757-4765.
    • (2009) Mol Cell Biol , vol.29 , pp. 4757-4765
    • Tang, Z.Z.1    Zheng, S.2    Nikolic, J.3    Black, D.L.4
  • 158
    • 79953165803 scopus 로고    scopus 로고
    • Regulation of the mutually exclusive exons 8a and 8 in the CaV1.2 calcium channel transcript by polypyrimidine tract-binding protein
    • Tang ZZ, Sharma S, Zheng S, Chawla G, Nikolic J, Black DL. Regulation of the mutually exclusive exons 8a and 8 in the CaV1.2 calcium channel transcript by polypyrimidine tract-binding protein. J Biol Chem 2011, 286:10007-10016.
    • (2011) J Biol Chem , vol.286 , pp. 10007-10016
    • Tang, Z.Z.1    Sharma, S.2    Zheng, S.3    Chawla, G.4    Nikolic, J.5    Black, D.L.6
  • 159
    • 78650828094 scopus 로고    scopus 로고
    • The neuronal splicing factor Nova controls alternative splicing in N-type and P-type CaV2 calcium channels
    • Allen SE, Darnell RB, Lipscombe D. The neuronal splicing factor Nova controls alternative splicing in N-type and P-type CaV2 calcium channels. Channels (Austin) 2010, 4:483-489.
    • (2010) Channels (Austin) , vol.4 , pp. 483-489
    • Allen, S.E.1    Darnell, R.B.2    Lipscombe, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.