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Volumn 508, Issue 3, 1998, Pages 647-657

Structure and function of voltage-gated sodium channels

Author keywords

[No Author keywords available]

Indexed keywords

SODIUM CHANNEL; SODIUM ION; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; VOLTAGE GATED POTASSIUM CHANNEL; VOLTAGE GATED SODIUM CHANNEL;

EID: 0031896768     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1469-7793.1998.647bp.x     Document Type: Review
Times cited : (276)

References (102)
  • 1
    • 0014608851 scopus 로고
    • The effects of external potassium and long duration voltage conditioning on the amplitude of sodium currents in the giant axon of the squid, Loligo pealei
    • ADELMAN, W. J. & PALTI, Y. (1969). The effects of external potassium and long duration voltage conditioning on the amplitude of sodium currents in the giant axon of the squid, Loligo pealei. Journal of General Physiology 54, 589-606.
    • (1969) Journal of General Physiology , vol.54 , pp. 589-606
    • Adelman, W.J.1    Palti, Y.2
  • 2
    • 0021086246 scopus 로고
    • A reinterpretation of mammalian sodium channel gating based on single channel recording
    • ALDRICH, R. W., COREY, D. P. & STEVENS, C. F. (1983). A reinterpretation of mammalian sodium channel gating based on single channel recording. Nature 306, 436-441.
    • (1983) Nature , vol.306 , pp. 436-441
    • Aldrich, R.W.1    Corey, D.P.2    Stevens, C.F.3
  • 3
    • 0026755899 scopus 로고
    • Molecular localization of an ion-binding site within the pore of mammalian sodium channels
    • BACKX, P., YUE, D., LAWRENCE, J., MARBAN, E. & TOMASELLI, G. (1992). Molecular localization of an ion-binding site within the pore of mammalian sodium channels. Science 257, 248-251.
    • (1992) Science , vol.257 , pp. 248-251
    • Backx, P.1    Yue, D.2    Lawrence, J.3    Marban, E.4    Tomaselli, G.5
  • 9
    • 0030933457 scopus 로고    scopus 로고
    • Contribution of sialic acid to the voltage dependence of sodium channel gating. A possible electrostatic mechanism
    • BENNETT, E., URCAN, M., TINKLE, S., KOSZOWSKI, A. & LEVINSON, S. (1997). Contribution of sialic acid to the voltage dependence of sodium channel gating. A possible electrostatic mechanism. Journal of General Physiology 109, 327-343.
    • (1997) Journal of General Physiology , vol.109 , pp. 327-343
    • Bennett, E.1    Urcan, M.2    Tinkle, S.3    Koszowski, A.4    Levinson, S.5
  • 11
    • 0029914689 scopus 로고    scopus 로고
    • Sodium channel defects in myotonia and periodic paralysis
    • CANNON, S. (1996). Sodium channel defects in myotonia and periodic paralysis. Annual Review of Neuroscience 19, 141-164.
    • (1996) Annual Review of Neuroscience , vol.19 , pp. 141-164
    • Cannon, S.1
  • 12
    • 0027462342 scopus 로고
    • + current conducted by the rat skeletal muscle alpha subunit by coexpression with a human brain β subunit
    • + current conducted by the rat skeletal muscle alpha subunit by coexpression with a human brain β subunit. Pflügers Archiv 423, 155-157.
    • (1993) Pflügers Archiv , vol.423 , pp. 155-157
    • Cannon, S.1    McClatchey, A.2    Gusella, J.3
  • 13
    • 0030880487 scopus 로고    scopus 로고
    • Dopaminergic modulation of sodium current in hippocampal neurons via cAMP-dependent phosphorylation of specific sites in the sodium channel α subunit
    • CANTRELL, A., SMITH, R., GOLDIN, A., SCHEUER, T. & CATTERALL, W. (1997). Dopaminergic modulation of sodium current in hippocampal neurons via cAMP-dependent phosphorylation of specific sites in the sodium channel α subunit. Journal of Neuroscience 17, 7330-7338.
    • (1997) Journal of Neuroscience , vol.17 , pp. 7330-7338
    • Cantrell, A.1    Smith, R.2    Goldin, A.3    Scheuer, T.4    Catterall, W.5
  • 14
    • 0019276817 scopus 로고
    • Interaction of polypeptide neurotoxins with a receptor site associated with voltage-sensitive sodium channels
    • CATTERALL, W. & BENESKI, D. (1980). Interaction of polypeptide neurotoxins with a receptor site associated with voltage-sensitive sodium channels. Journal of Supramolecular Structure 14, 295-303.
    • (1980) Journal of Supramolecular Structure , vol.14 , pp. 295-303
    • Catterall, W.1    Beneski, D.2
  • 15
    • 0029417234 scopus 로고
    • Characterizing the μ-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations
    • CHAHINE, M., CHEN, L., FOTOUHI, N., WALSKY, R., FRY, D., SANTARELLI, V., HORN, R. & KALLEN, R. (1995). Characterizing the μ-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations. Receptors and Channels 3, 161-174.
    • (1995) Receptors and Channels , vol.3 , pp. 161-174
    • Chahine, M.1    Chen, L.2    Fotouhi, N.3    Walsky, R.4    Fry, D.5    Santarelli, V.6    Horn, R.7    Kallen, R.8
  • 16
    • 0030740722 scopus 로고    scopus 로고
    • Myotonic dystrophy kinase modulates skeletal muscle but not cardiac voltage-gated sodium channels
    • CHAHINE, M. & GEORGE, A. JR (1997). Myotonic dystrophy kinase modulates skeletal muscle but not cardiac voltage-gated sodium channels. FEBS Letters 412, 621-624.
    • (1997) FEBS Letters , vol.412 , pp. 621-624
    • Chahine, M.1    George Jr., A.2
  • 17
    • 0014901241 scopus 로고
    • Slow changes in membrane permeability and long lasting action potentials in axons perfused with fluoride solutions
    • CHANDLER, W. K. & MEVES, H. (1970). Slow changes in membrane permeability and long lasting action potentials in axons perfused with fluoride solutions. Journal of Physiology 211, 707-728.
    • (1970) Journal of Physiology , vol.211 , pp. 707-728
    • Chandler, W.K.1    Meves, H.2
  • 18
    • 0030453610 scopus 로고    scopus 로고
    • A unique role for the S4 segment of domain 4 in the inactivation of sodium channels
    • CHEN, L., SANTARELLI, V., HORN, R. & KALLEN, R. (1996). A unique role for the S4 segment of domain 4 in the inactivation of sodium channels. Journal of General Physiology 108, 549-556.
    • (1996) Journal of General Physiology , vol.108 , pp. 549-556
    • Chen, L.1    Santarelli, V.2    Horn, R.3    Kallen, R.4
  • 20
    • 0030062943 scopus 로고    scopus 로고
    • Control of ion flux and selectivity by negatively charged residues in the outer mouth of rat sodium channels
    • CHIAMVIMONVAT, N., PÉREZ-GARCÍA, M., TOMASELLI, G. & MARBAN, E. (1996b). Control of ion flux and selectivity by negatively charged residues in the outer mouth of rat sodium channels. Journal of Physiology 491, 51-59.
    • (1996) Journal of Physiology , vol.491 , pp. 51-59
    • Chiamvimonvat, N.1    Pérez-García, M.2    Tomaselli, G.3    Marban, E.4
  • 22
    • 0027171497 scopus 로고
    • Partial characterization of the rH1 sodium channel protein from rat heart using subtype-specific antibodies
    • COHEN, S. & LEVITT, L. (1993). Partial characterization of the rH1 sodium channel protein from rat heart using subtype-specific antibodies. Circulation Research 73, 735-742.
    • (1993) Circulation Research , vol.73 , pp. 735-742
    • Cohen, S.1    Levitt, L.2
  • 25
    • 0027053927 scopus 로고
    • Class I and IV antiarrhythmic drugs and cytosolic calcium regulate mRNA encoding the sodium channel α subunit in rat cardiac muscle
    • DUFF, H., OFFORD, J., WEST, J. & CATTERALL, W. (1992). Class I and IV antiarrhythmic drugs and cytosolic calcium regulate mRNA encoding the sodium channel α subunit in rat cardiac muscle. Molecular Pharmacology 42, 570-574.
    • (1992) Molecular Pharmacology , vol.42 , pp. 570-574
    • Duff, H.1    Offord, J.2    West, J.3    Catterall, W.4
  • 26
    • 0031045141 scopus 로고    scopus 로고
    • Regulation of sodium channel gene expression by transcriptional silencing
    • EGGEN, B. & MANDEL, G. (1997). Regulation of sodium channel gene expression by transcriptional silencing. Developmental Neuroscience 19, 25-26.
    • (1997) Developmental Neuroscience , vol.19 , pp. 25-26
    • Eggen, B.1    Mandel, G.2
  • 27
    • 0029838677 scopus 로고    scopus 로고
    • Structure and function of voltage-dependent sodium channels: Comparison of brain II and cardiac isoforms
    • FOZZARD, H. & HANCK, D. (1996). Structure and function of voltage-dependent sodium channels: comparison of brain II and cardiac isoforms. Physiological Reviews 76, 887-926.
    • (1996) Physiological Reviews , vol.76 , pp. 887-926
    • Fozzard, H.1    Hanck, D.2
  • 28
    • 0030058733 scopus 로고    scopus 로고
    • Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: An electrostatic approach to channel geometry
    • FRENCH, R., PRUSAK-SOCHACZEWSKI, E., ZAMPONI, G., BECKER, S., KULARATNA, A. & HORN, R. (1996). Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: an electrostatic approach to channel geometry. Neuron 16, 407-413.
    • (1996) Neuron , vol.16 , pp. 407-413
    • French, R.1    Prusak-Sochaczewski, E.2    Zamponi, G.3    Becker, S.4    Kularatna, A.5    Horn, R.6
  • 29
    • 0031015604 scopus 로고    scopus 로고
    • Modulation of the human cardiac sodium channel α-subunit by cAMP-dependent protein kinase and the responsible sequence domain
    • FROHNWIESER, B., CHEN, L., SCHREIBMAYER, W. & KALLEN, R. (1997). Modulation of the human cardiac sodium channel α-subunit by cAMP-dependent protein kinase and the responsible sequence domain. Journal of Physiology 498, 309-318.
    • (1997) Journal of Physiology , vol.498 , pp. 309-318
    • Frohnwieser, B.1    Chen, L.2    Schreibmayer, W.3    Kallen, R.4
  • 30
    • 0028807579 scopus 로고
    • Modulation of cardiac sodium channel isoform by cyclic AMP dependent protein kinase does not depend on phosphorylation of serine 1504 in the cytosolic loop interconnecting transmembrane domains III and IV
    • FROHNWIESER, B., WEIGL, L. & SCHREIBMAYER, W. (1995). Modulation of cardiac sodium channel isoform by cyclic AMP dependent protein kinase does not depend on phosphorylation of serine 1504 in the cytosolic loop interconnecting transmembrane domains III and IV. Pflügers Archiv 430, 751-753.
    • (1995) Pflügers Archiv , vol.430 , pp. 751-753
    • Frohnwieser, B.1    Weigl, L.2    Schreibmayer, W.3
  • 32
    • 0020464124 scopus 로고
    • The saxitoxin receptor of the sodium channel from rat brain. Evidence for two nonidentical β subunits
    • HARTSHORNE, R., MESSNER, D., COPPERSMITH, J. & CATTERALL, W. (1982). The saxitoxin receptor of the sodium channel from rat brain. Evidence for two nonidentical β subunits. Journal of Biological Chemistry 257, 13888-13891.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 13888-13891
    • Hartshorne, R.1    Messner, D.2    Coppersmith, J.3    Catterall, W.4
  • 33
    • 0031052231 scopus 로고    scopus 로고
    • Slow inactivation differs among mutant Na channels associated with myotonia and periodic paralysis
    • HAYWARD, L. J., BROWN, R. H. JR & CANNON, S. C. (1997). Slow inactivation differs among mutant Na channels associated with myotonia and periodic paralysis. Biophysical Journal 72, 1204-1219.
    • (1997) Biophysical Journal , vol.72 , pp. 1204-1219
    • Hayward, L.J.1    Brown Jr., R.H.2    Cannon, S.C.3
  • 34
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • HEINEMANN, S., TERLAU, H., STÜHMER, W., IMOTO, K. & NUMA, S. (1992). Calcium channel characteristics conferred on the sodium channel by single mutations. Nature 356, 441-443.
    • (1992) Nature , vol.356 , pp. 441-443
    • Heinemann, S.1    Terlau, H.2    Stühmer, W.3    Imoto, K.4    Numa, S.5
  • 35
    • 0030016085 scopus 로고    scopus 로고
    • Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels
    • HILL, J., ALEWOOD, P. & CRAIK, D. (1996). Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels. Biochemistry 35, 8824-8835.
    • (1996) Biochemistry , vol.35 , pp. 8824-8835
    • Hill, J.1    Alewood, P.2    Craik, D.3
  • 36
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • HODGKIN, A. L. & HUXLEY, A. F. (1952). A quantitative description of membrane current and its application to conduction and excitation in nerve. Journal of Physiology 117, 500-544.
    • (1952) Journal of Physiology , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 39
    • 0028972374 scopus 로고
    • Structure and function of the β2 subunit of brain sodium channels, a transmembrane glycoprotein with a CAM motif
    • ISOM, L., RAGSDALE, D., DE JONGH, K., WESTENBROEK, R., REBER, B., SCHEUER, T. & CATTERALL, W. (1995). Structure and function of the β2 subunit of brain sodium channels, a transmembrane glycoprotein with a CAM motif. Cell 83, 433-442.
    • (1995) Cell , vol.83 , pp. 433-442
    • Isom, L.1    Ragsdale, D.2    De Jongh, K.3    Westenbroek, R.4    Reber, B.5    Scheuer, T.6    Catterall, W.7
  • 40
    • 0024976490 scopus 로고
    • Alpha-(2-8)-polysialic acid immunoreactivity in voltage-sensitive sodium channel of eel electric organ
    • JAMES, W. & AGNEW, W. (1989). Alpha-(2-8)-polysialic acid immunoreactivity in voltage-sensitive sodium channel of eel electric organ. Proceedings of the Royal Society B 237, 233-245.
    • (1989) Proceedings of the Royal Society B , vol.237 , pp. 233-245
    • James, W.1    Agnew, W.2
  • 41
    • 0025344712 scopus 로고
    • Primary structure and expression of a sodium channel characteristic of denervated and immature rat skeletal muscle
    • KALLEN, R., SHENG, Z., YANG, J., CHEN, L., ROGART, R. & BARCHI, R. (1990). Primary structure and expression of a sodium channel characteristic of denervated and immature rat skeletal muscle. Neuron 4, 233-242.
    • (1990) Neuron , vol.4 , pp. 233-242
    • Kallen, R.1    Sheng, Z.2    Yang, J.3    Chen, L.4    Rogart, R.5    Barchi, R.6
  • 42
    • 0032562192 scopus 로고    scopus 로고
    • Phenotypic characterization of a novel long-QT syndrome mutation (R1623Q) in the cardiac sodium channel
    • KAMBOURIS, N., NUSS, H., JOHNS, D., TOMASELLI, G., MARBAN, E. & BALSER, J. (1998). Phenotypic characterization of a novel long-QT syndrome mutation (R1623Q) in the cardiac sodium channel. Circulation 97, 640-644.
    • (1998) Circulation , vol.97 , pp. 640-644
    • Kambouris, N.1    Nuss, H.2    Johns, D.3    Tomaselli, G.4    Marban, E.5    Balser, J.6
  • 43
    • 0030885219 scopus 로고    scopus 로고
    • Sodium channel inactivation is altered by substitution of voltage sensor positive charges
    • KONTIS, K. & GOLDIN, A. (1997). Sodium channel inactivation is altered by substitution of voltage sensor positive charges. Journal of General Physiology 110, 403-413.
    • (1997) Journal of General Physiology , vol.110 , pp. 403-413
    • Kontis, K.1    Goldin, A.2
  • 44
    • 0030963793 scopus 로고    scopus 로고
    • Sodium channel activation gating is affected by substitutions of voltage sensor positive charges in all four domains
    • KONTIS, K., ROUNAGHI, A. & GOLDIN, A. (1997). Sodium channel activation gating is affected by substitutions of voltage sensor positive charges in all four domains. Journal of General Physiology 110, 391-401.
    • (1997) Journal of General Physiology , vol.110 , pp. 391-401
    • Kontis, K.1    Rounaghi, A.2    Goldin, A.3
  • 45
    • 0026018120 scopus 로고
    • Sodium channel inactivation from resting states in guinea-pig ventricular myocytes
    • LAWRENCE, J., YUE, D., ROSE, W. & MARBAN, E. (1991). Sodium channel inactivation from resting states in guinea-pig ventricular myocytes. Journal of Physiology 443, 629-650.
    • (1991) Journal of Physiology , vol.443 , pp. 629-650
    • Lawrence, J.1    Yue, D.2    Rose, W.3    Marban, E.4
  • 46
    • 0027496454 scopus 로고
    • Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinase
    • LI, M., WEST, J., NUMANN, R., MURPHY, B., SCHEUER, T. & CATTERALL, W. (1993). Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinase. Science 261, 1439-1442.
    • (1993) Science , vol.261 , pp. 1439-1442
    • Li, M.1    West, J.2    Numann, R.3    Murphy, B.4    Scheuer, T.5    Catterall, W.6
  • 49
    • 0029044707 scopus 로고
    • A critical role for transmembrane segment IVS6 of the sodium channel α subunit in fast inactivation
    • MCPHEE, J., RAGSDALE, D., SCHEUER, T. & CATTERALL, W. (1995). A critical role for transmembrane segment IVS6 of the sodium channel α subunit in fast inactivation. Journal of Biological Chemistry 270, 12025-12034.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 12025-12034
    • McPhee, J.1    Ragsdale, D.2    Scheuer, T.3    Catterall, W.4
  • 51
    • 0030068030 scopus 로고    scopus 로고
    • Coexpression of β1 with cardiac sodium channel α subunits in oocytes decreases lidocaine block
    • MAKIELSKI, J., LIMBERIS, J., CHANG, S., FAN, Z. & KYLE, J. (1996). Coexpression of β1 with cardiac sodium channel α subunits in oocytes decreases lidocaine block. Molecular Pharmacology 49 30-39.
    • (1996) Molecular Pharmacology , vol.49 , pp. 30-39
    • Makielski, J.1    Limberis, J.2    Chang, S.3    Fan, Z.4    Kyle, J.5
  • 52
    • 0023377689 scopus 로고
    • Sodium current in voltage clamped internally perfused canine cardiac Purkinje cells
    • MAKIELSKI, J., SHEETS, M., HANCK, D., JANUARY, C. & FOZZARD, H. (1987). Sodium current in voltage clamped internally perfused canine cardiac Purkinje cells. Biophysical Journal 52, 1-11.
    • (1987) Biophysical Journal , vol.52 , pp. 1-11
    • Makielski, J.1    Sheets, M.2    Hanck, D.3    January, C.4    Fozzard, H.5
  • 53
    • 0028365479 scopus 로고
    • + channel β1 subunit mRNA expressed in adult human skeletal muscle, heart, and brain is encoded by a single gene
    • + channel β1 subunit mRNA expressed in adult human skeletal muscle, heart, and brain is encoded by a single gene. Journal of Biological Chemistry 269, 7571-7578.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 7571-7578
    • Makita, N.1    Bennett Jr., P.2    George Jr., A.3
  • 54
    • 0022244856 scopus 로고
    • The sodium channel from rat brain. Separation and characterization of subunits
    • MESSNER, D. & CATTERALL, W. (1985). The sodium channel from rat brain. Separation and characterization of subunits. Journal of Biological Chemistry 260, 10597-10604.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 10597-10604
    • Messner, D.1    Catterall, W.2
  • 55
    • 0025226105 scopus 로고
    • Changes in sodium channel gating produced by point mutations in a cytoplasmic linker
    • MOORMAN, J. R., KIRSCH, G. E., BROWN, A. M. & JOHO, R. H. (1990). Changes in sodium channel gating produced by point mutations in a cytoplasmic linker. Science 250, 688-691.
    • (1990) Science , vol.250 , pp. 688-691
    • Moorman, J.R.1    Kirsch, G.E.2    Brown, A.M.3    Joho, R.H.4
  • 57
    • 0029802816 scopus 로고    scopus 로고
    • cAMP-dependent phosphorylation of two sites in the α subunit of the cardiac sodium channel
    • MURPHY, B., ROGERS, J., PERDICHIZZI, A., COLVIN, A. & CATTERALL, W. (1996). cAMP-dependent phosphorylation of two sites in the α subunit of the cardiac sodium channel. Journal of Biological Chemistry 271, 28837-28843.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 28837-28843
    • Murphy, B.1    Rogers, J.2    Perdichizzi, A.3    Colvin, A.4    Catterall, W.5
  • 61
    • 0026079765 scopus 로고
    • Functional modulation of brain sodium channels by protein kinase C phosphorylation
    • NUMANN, R., CATTERALL, W. & SCHEUER, T. (1991). Functional modulation of brain sodium channels by protein kinase C phosphorylation. Science 254, 115-118.
    • (1991) Science , vol.254 , pp. 115-118
    • Numann, R.1    Catterall, W.2    Scheuer, T.3
  • 62
    • 0028341896 scopus 로고
    • Modulation of skeletal muscle sodium channels in a satellite cell line by protein kinase C
    • NUMANN, R., HAUSCHKA, S., CATTERALL, W. & SCHEUER, T. (1994). Modulation of skeletal muscle sodium channels in a satellite cell line by protein kinase C. Journal of Neuroscience 14, 4226-4236.
    • (1994) Journal of Neuroscience , vol.14 , pp. 4226-4236
    • Numann, R.1    Hauschka, S.2    Catterall, W.3    Scheuer, T.4
  • 63
    • 0029417096 scopus 로고
    • Functional association of the β1 subunit with human cardiac (hH1) and rat skeletal muscle (μ1) sodium channel α subunits expressed in Xenopus oocytes
    • NUSS, H., CHIAMVIMONVAT, N., PÉREZ-GARCÍA, M., TOMASELLI, G. & MARBAN, E. (1995). Functional association of the β1 subunit with human cardiac (hH1) and rat skeletal muscle (μ1) sodium channel α subunits expressed in Xenopus oocytes. Journal of General Physiology 106, 1171-1191.
    • (1995) Journal of General Physiology , vol.106 , pp. 1171-1191
    • Nuss, H.1    Chiamvimonvat, N.2    Pérez-García, M.3    Tomaselli, G.4    Marban, E.5
  • 64
    • 0028820660 scopus 로고
    • A molecular link between activation and inactivation of sodium channels
    • O'LEARY, M., CHEN, L., KALLEN, R. & HORN, R. (1995). A molecular link between activation and inactivation of sodium channels. Journal of General Physiology 106, 641-658.
    • (1995) Journal of General Physiology , vol.106 , pp. 641-658
    • O'Leary, M.1    Chen, L.2    Kallen, R.3    Horn, R.4
  • 65
    • 0028242712 scopus 로고
    • The adult rat brain β1 subunit modifies activation and inactivation gating of multiple sodium channel α subunits
    • PATTON, D., ISOM, L., CATTERALL, W. & GOLDIN, A. (1994). The adult rat brain β1 subunit modifies activation and inactivation gating of multiple sodium channel α subunits. Journal of Biological Chemistry 269, 17649-17655.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 17649-17655
    • Patton, D.1    Isom, L.2    Catterall, W.3    Goldin, A.4
  • 68
    • 0342276136 scopus 로고    scopus 로고
    • Mechanisms of sodium/calcium selectivity in sodium channels probed by cysteine mutagenesis and sulfhydryl modification
    • PÉREZ-GARCÍA, M., CHIAMVIMONVAT, N., RANJAN, R., BALSER, J., TOMASELLI, G. & MARBAN, E. (1997). Mechanisms of sodium/calcium selectivity in sodium channels probed by cysteine mutagenesis and sulfhydryl modification. Biophysical Journal 72, 989-996.
    • (1997) Biophysical Journal , vol.72 , pp. 989-996
    • Pérez-García, M.1    Chiamvimonvat, N.2    Ranjan, R.3    Balser, J.4    Tomaselli, G.5    Marban, E.6
  • 72
    • 0023918980 scopus 로고
    • Sodium-channel turnover in rabbit cultured Schwann cells
    • RITCHIE, J. (1988). Sodium-channel turnover in rabbit cultured Schwann cells. Proceedings of the Royal Society B 233, 423-430.
    • (1988) Proceedings of the Royal Society B , vol.233 , pp. 423-430
    • Ritchie, J.1
  • 73
    • 0023654028 scopus 로고
    • The voltage-sensitive sodium channel from rabbit skeletal muscle. Chemical characterization of subunits
    • ROBERTS, R. & BARCHI, R. (1987). The voltage-sensitive sodium channel from rabbit skeletal muscle. Chemical characterization of subunits. Journal of Biological Chemistry 262, 2298-2303.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 2298-2303
    • Roberts, R.1    Barchi, R.2
  • 74
    • 0029847602 scopus 로고    scopus 로고
    • Multiple mechanisms in the long-QT syndrome. Current knowledge, gaps, and future directions
    • RODEN, D., LAZZARA, R., ROSEN, M., SCHWARTZ, P., TOWBIN, J. & VINCENT, G. (1996). Multiple mechanisms in the long-QT syndrome. Current knowledge, gaps, and future directions. Circulation 94, 1996-1202.
    • (1996) Circulation , vol.94 , pp. 1996-11202
    • Roden, D.1    Lazzara, R.2    Rosen, M.3    Schwartz, P.4    Towbin, J.5    Vincent, G.6
  • 77
    • 0026637366 scopus 로고
    • A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties
    • SATIN, J., KYLE, J., CHEN, M., BELL, P., CRIBBS, L., FOZZARD, H. & ROGART, R. (1992). A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties. Science 256, 1202-1205.
    • (1992) Science , vol.256 , pp. 1202-1205
    • Satin, J.1    Kyle, J.2    Chen, M.3    Bell, P.4    Cribbs, L.5    Fozzard, H.6    Rogart, R.7
  • 78
    • 0023645640 scopus 로고
    • Palmitylation, sulfation, and glycosylation of the α subunit of the sodium channel. Role of posttranslational modifications in channel assembly
    • SCHMIDT, J. & CATTERALL, W. (1987). Palmitylation, sulfation, and glycosylation of the α subunit of the sodium channel. Role of posttranslational modifications in channel assembly. Journal of Biological Chemistry 262, 13713-13723.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 13713-13723
    • Schmidt, J.1    Catterall, W.2
  • 80
    • 0026644838 scopus 로고
    • Protein kinase A phosphorylation enhances sodium channel currents in Xenopus oocytes
    • SMITH, R. & GOLDIN, A. (1992). Protein kinase A phosphorylation enhances sodium channel currents in Xenopus oocytes. American Journal of Physiology 263, C660-666.
    • (1992) American Journal of Physiology , vol.263
    • Smith, R.1    Goldin, A.2
  • 81
    • 0029963312 scopus 로고
    • Phosphorylation of brain sodium channels in the I-II linker modulates channel function in Xenopus oocytes
    • SMITH, R. & GOLDIN, A. (1995). Phosphorylation of brain sodium channels in the I-II linker modulates channel function in Xenopus oocytes. Journal of Neuroscience 16, 1965-1974.
    • (1995) Journal of Neuroscience , vol.16 , pp. 1965-1974
    • Smith, R.1    Goldin, A.2
  • 82
    • 0030742101 scopus 로고    scopus 로고
    • Phosphorylation at a single site in the rat brain sodium channel is necessary and sufficient for current reduction by protein kinase A
    • SMITH, R. & GOLDIN, A. (1997). Phosphorylation at a single site in the rat brain sodium channel is necessary and sufficient for current reduction by protein kinase A. Journal of Neuroscience 17, 6086-6093.
    • (1997) Journal of Neuroscience , vol.17 , pp. 6086-6093
    • Smith, R.1    Goldin, A.2
  • 83
    • 0028180093 scopus 로고
    • The μI skeletal muscle sodium channel: Mutation E403Q eliminates sensitivity to tetrodotoxin but not to μ-conotoxins GIIIA and GIIIB
    • STEPHAN, M., POTTS, J. & AGNEW, W. (1994). The μI skeletal muscle sodium channel: mutation E403Q eliminates sensitivity to tetrodotoxin but not to μ-conotoxins GIIIA and GIIIB. Journal of Membrane Biology 137, 1-8.
    • (1994) Journal of Membrane Biology , vol.137 , pp. 1-8
    • Stephan, M.1    Potts, J.2    Agnew, W.3
  • 84
    • 0024368695 scopus 로고
    • Structural parts involved in activation and inactivation of the sodium channel
    • STÜHMER, W., CONTI, F., SUZUKI, H., WANG, X., NODA, M., YAHAGI, N., KUBO, H. & NUMA, S. (1989). Structural parts involved in activation and inactivation of the sodium channel. Nature 339, 597-603.
    • (1989) Nature , vol.339 , pp. 597-603
    • Stühmer, W.1    Conti, F.2    Suzuki, H.3    Wang, X.4    Noda, M.5    Yahagi, N.6    Kubo, H.7    Numa, S.8
  • 89
    • 0020582852 scopus 로고
    • Glycosylation is required for maintenance of functional sodium channels in neuroblastoma cells
    • WAECHTER, C., SCHMIDT, J. & CATTERALL, W. (1983). Glycosylation is required for maintenance of functional sodium channels in neuroblastoma cells. Journal of Biological Chemistry 258, 5117-5123.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 5117-5123
    • Waechter, C.1    Schmidt, J.2    Catterall, W.3
  • 94
    • 0030983156 scopus 로고    scopus 로고
    • Topology of the P segments in the sodium channel pore revealed by cysteine mutagenesis
    • YAMAGISHI, T., JANECKI, M., MARBAN, E. & TOMASELLI, G. (1997). Topology of the P segments in the sodium channel pore revealed by cysteine mutagenesis. Biophysical Journal 73, 195-204.
    • (1997) Biophysical Journal , vol.73 , pp. 195-204
    • Yamagishi, T.1    Janecki, M.2    Marban, E.3    Tomaselli, G.4
  • 95
    • 0025229019 scopus 로고
    • Phosphorylation of the rat skeletal muscle sodium channel by cyclic AMP-dependent protein kinase
    • YANG, J. & BARCHI, R. (1990). Phosphorylation of the rat skeletal muscle sodium channel by cyclic AMP-dependent protein kinase. Journal of Neurochemistry 54, 954-962.
    • (1990) Journal of Neurochemistry , vol.54 , pp. 954-962
    • Yang, J.1    Barchi, R.2
  • 96
    • 0025950694 scopus 로고
    • TTX-sensitive and TTX-insensitive sodium channel mRNA transcripts are independently regulated in adult skeletal muscle after denervation
    • YANG, J., SLADKY, J., KALLEN, R. & BARCHI, R. (1991). TTX-sensitive and TTX-insensitive sodium channel mRNA transcripts are independently regulated in adult skeletal muscle after denervation. Neuron 7, 421-427.
    • (1991) Neuron , vol.7 , pp. 421-427
    • Yang, J.1    Sladky, J.2    Kallen, R.3    Barchi, R.4
  • 97
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • YANG, N., GEORGE, A. JR & HORN, R. (1996). Molecular basis of charge movement in voltage-gated sodium channels. Neuron 16, 113-122.
    • (1996) Neuron , vol.16 , pp. 113-122
    • Yang, N.1    George Jr., A.2    Horn, R.3
  • 98
    • 0030731887 scopus 로고    scopus 로고
    • Probing the outer vestibule fo a sodium channel voltage sensor
    • YANG, N., GEORGE, A. & HORN, R. (1997). Probing the outer vestibule fo a sodium channel voltage sensor. Biophysical Journal 73, 2260-2268.
    • (1997) Biophysical Journal , vol.73 , pp. 2260-2268
    • Yang, N.1    George, A.2    Horn, R.3
  • 99
    • 0029084477 scopus 로고
    • Evidence for voltage-dependent S4 movement in sodium channels
    • YANG, N. & HORN, R. (1995). Evidence for voltage-dependent S4 movement in sodium channels. Neuron 15, 213-218.
    • (1995) Neuron , vol.15 , pp. 213-218
    • Yang, N.1    Horn, R.2
  • 101
    • 0024516593 scopus 로고
    • Two molecular transitions influence cardiac sodium channel gating
    • YUE, D., LAWRENCE, J. & MARBAN, E. (1989). Two molecular transitions influence cardiac sodium channel gating. Science 244, 349-352.
    • (1989) Science , vol.244 , pp. 349-352
    • Yue, D.1    Lawrence, J.2    Marban, E.3
  • 102
    • 0025212639 scopus 로고
    • Glycosylation is required for maintenance of functional voltage-activated channels in growing neocortical neurons of the rat
    • ZONA, C., EUSEBI, F. & MILEDI, R. (1990). Glycosylation is required for maintenance of functional voltage-activated channels in growing neocortical neurons of the rat. Proceedings of the Royal Society B 239, 119-127.
    • (1990) Proceedings of the Royal Society B , vol.239 , pp. 119-127
    • Zona, C.1    Eusebi, F.2    Miledi, R.3


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