메뉴 건너뛰기




Volumn 58, Issue 18, 2015, Pages 7093-7118

Voltage-Gated Sodium Channels: Structure, Function, Pharmacology, and Clinical Indications

Author keywords

[No Author keywords available]

Indexed keywords

AZD 3161; BATRACHOTOXIN; BREVETOXIN; CIGUATOXIN; CNV 1014802; CONOTOXIN; DSP 2230; ELECLAZINE; GS 6614; GSK 2339345; NATURAL PRODUCT; NKTR 171; PF 04531083; SCORPION VENOM; SODIUM CHANNEL BLOCKING AGENT; SPIDER VENOM; UNCLASSIFIED DRUG; VERATRIDINE; VOLTAGE GATED SODIUM CHANNEL; XEN 402; BIOLOGICAL PRODUCT; LIGAND; PROTEIN SUBUNIT; VOLTAGE GATED SODIUM CHANNEL BLOCKING AGENT;

EID: 84942284225     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501981g     Document Type: Review
Times cited : (388)

References (226)
  • 2
    • 84866754503 scopus 로고    scopus 로고
    • Advances in targeting voltage-gated sodium channels with small molecules
    • Nardi, A.; Damann, N.; Hertrampf, T.; Kless, A. Advances in targeting voltage-gated sodium channels with small molecules ChemMedChem 2012, 7, 1-30
    • (2012) ChemMedChem , vol.7 , pp. 1-30
    • Nardi, A.1    Damann, N.2    Hertrampf, T.3    Kless, A.4
  • 3
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin, A. L.; Huxley, A. F. A quantitative description of membrane current and its application to conduction and excitation in nerve J. Physiol. 1952, 117 (4) 500-544
    • (1952) J. Physiol. , vol.117 , Issue.4 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 4
    • 0009345298 scopus 로고
    • Purification of the tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from Electrophorus electricus electroplax membrane
    • Agnew, W. S.; Levinson, S. R.; Brabson, J. S.; Raftery, M. A. Purification of the tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from Electrophorus electricus electroplax membrane Proc. Natl. Acad. Sci. U. S. A. 1978, 75, 2606-2610
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 2606-2610
    • Agnew, W.S.1    Levinson, S.R.2    Brabson, J.S.3    Raftery, M.A.4
  • 6
    • 29844438166 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels
    • Catterall, W. A.; Goldin, A. L.; Waxman, S. G. International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels Pharmacol. Rev. 2005, 57 (4) 397-409
    • (2005) Pharmacol. Rev. , vol.57 , Issue.4 , pp. 397-409
    • Catterall, W.A.1    Goldin, A.L.2    Waxman, S.G.3
  • 7
    • 0033044832 scopus 로고    scopus 로고
    • Diversity of mammalian voltage-gated sodium channels
    • Goldin, A. L. Diversity of mammalian voltage-gated sodium channels Ann. N. Y. Acad. Sci. 1999, 868, 38-50
    • (1999) Ann. N. Y. Acad. Sci. , vol.868 , pp. 38-50
    • Goldin, A.L.1
  • 8
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestèle, S.; Catterall, W. A. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels Biochimie 2000, 82 (9-10) 883-892
    • (2000) Biochimie , vol.82 , Issue.910 , pp. 883-892
    • Cestèle, S.1    Catterall, W.A.2
  • 10
    • 0005769753 scopus 로고
    • Covalent labeling of protein components of the sodium channel with a photoactivable derivative of a scorpion toxin
    • Beneski, D. A.; Catterall, W. A. Covalent labeling of protein components of the sodium channel with a photoactivable derivative of a scorpion toxin Proc. Natl. Acad. Sci. U. S. A. 1980, 77, 639-643
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 639-643
    • Beneski, D.A.1    Catterall, W.A.2
  • 11
    • 0012616825 scopus 로고
    • Purification of the saxitoxin receptor of the sodium channel from rat brain
    • Hartshorne, R. P.; Catterall, W. A. Purification of the saxitoxin receptor of the sodium channel from rat brain Proc. Natl. Acad. Sci. U. S. A. 1981, 78, 4620-4624
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 4620-4624
    • Hartshorne, R.P.1    Catterall, W.A.2
  • 12
    • 0020464124 scopus 로고
    • The saxitoxin receptor of the sodium channel from rat brain. Evidence for two nonidentical β subunits
    • Hartshorne, R. P.; Messner, D. J.; Coppersmith, J. C.; Catterall, W. A. The saxitoxin receptor of the sodium channel from rat brain. Evidence for two nonidentical β subunits J. Biol. Chem. 1982, 257, 13888-13891
    • (1982) J. Biol. Chem. , vol.257 , pp. 13888-13891
    • Hartshorne, R.P.1    Messner, D.J.2    Coppersmith, J.C.3    Catterall, W.A.4
  • 13
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J.; Scheuer, T.; Zheng, N.; Catterall, W. A. The crystal structure of a voltage-gated sodium channel Nature 2011, 475 (7356) 353-358
    • (2011) Nature , vol.475 , Issue.7356 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 14
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J.; Gamal, T. M.; Scheuer, T.; Zheng, N.; Catterall, W. A. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states Nature 2012, 486 (7401) 135-139
    • (2012) Nature , vol.486 , Issue.7401 , pp. 135-139
    • Payandeh, J.1    Gamal, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 17
    • 84892438148 scopus 로고    scopus 로고
    • Structure and function of voltage-gated sodium channels at atomic resolution
    • Catterall, W. A. Structure and function of voltage-gated sodium channels at atomic resolution Exp. Physiol. 2014, 99 (1) 35-51
    • (2014) Exp. Physiol. , vol.99 , Issue.1 , pp. 35-51
    • Catterall, W.A.1
  • 21
    • 84895794573 scopus 로고    scopus 로고
    • Ion conduction and conformational flexibility of a bacterial voltage-gated sodium channel
    • Boiteus, C.; Vorobyov, I.; Allen, T. W. Ion conduction and conformational flexibility of a bacterial voltage-gated sodium channel Proc. Natl. Acad. Sci. U. S. A. 2014, 111 (9) 3454-3459
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , Issue.9 , pp. 3454-3459
    • Boiteus, C.1    Vorobyov, I.2    Allen, T.W.3
  • 22
    • 84893077319 scopus 로고    scopus 로고
    • Sodium channel selectivity and conduction: Prokaryotes have devised their own molecular strategy
    • Finol-Urdaneta, R. K.; Wang, Y.; Al-Sabi, A.; Zhao, C.; Noskov, S. Y.; French, R. J. Sodium channel selectivity and conduction: prokaryotes have devised their own molecular strategy J. Gen. Physiol. 2014, 143 (2) 157-171
    • (2014) J. Gen. Physiol. , vol.143 , Issue.2 , pp. 157-171
    • Finol-Urdaneta, R.K.1    Wang, Y.2    Al-Sabi, A.3    Zhao, C.4    Noskov, S.Y.5    French, R.J.6
  • 24
    • 84912140592 scopus 로고    scopus 로고
    • Asymmetric functional contributions of acidic and aromatic side chains in sodium channel voltage-sensor domains
    • Pless, S. A.; Elstone, F. D.; Niciforovic, A. P.; Galpin, J. D.; Yang, R.; Kurata, H. T.; Ahern, C. A. Asymmetric functional contributions of acidic and aromatic side chains in sodium channel voltage-sensor domains J. Gen. Physiol. 2014, 143 (5) 645-656
    • (2014) J. Gen. Physiol. , vol.143 , Issue.5 , pp. 645-656
    • Pless, S.A.1    Elstone, F.D.2    Niciforovic, A.P.3    Galpin, J.D.4    Yang, R.5    Kurata, H.T.6    Ahern, C.A.7
  • 25
    • 84905483057 scopus 로고    scopus 로고
    • Investigating the size and dynamics of voltage-gated sodium channel fenestrations
    • Kaczmarski, J. A.; Corry, B. Investigating the size and dynamics of voltage-gated sodium channel fenestrations Channels 2014, 8 (3) 264-277
    • (2014) Channels , vol.8 , Issue.3 , pp. 264-277
    • Kaczmarski, J.A.1    Corry, B.2
  • 27
    • 84891835113 scopus 로고    scopus 로고
    • Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels
    • Shaya, D.; Findeisen, F.; Abderemane-Ali, F.; Arrigoni, C.; Wong, S.; Nurva, S. R.; Loussouarn, G.; Minor, D. L., Jr. Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels J. Mol. Biol. 2014, 426, 467-483
    • (2014) J. Mol. Biol. , vol.426 , pp. 467-483
    • Shaya, D.1    Findeisen, F.2    Abderemane-Ali, F.3    Arrigoni, C.4    Wong, S.5    Nurva, S.R.6    Loussouarn, G.7    Minor, Jr.D.L.8
  • 28
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • Heinemann, S. H.; 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
  • 29
    • 84878842713 scopus 로고    scopus 로고
    • + selectivity in mammalian voltage-gated sodium channels based on molecular dynamics simulation
    • + selectivity in mammalian voltage-gated sodium channels based on molecular dynamics simulation Biophys. J. 2013, 104, 2401-2409
    • (2013) Biophys. J. , vol.104 , pp. 2401-2409
    • Xia, M.1    Liu, H.2    Li, Y.3    Yan, N.4    Gong, H.5
  • 31
    • 0033694833 scopus 로고    scopus 로고
    • From ionic currents to molecular mechanisms: The structure and function of voltage-gated sodium channels
    • Catterall, W. A. From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels Neuron 2000, 26, 13-25
    • (2000) Neuron , vol.26 , pp. 13-25
    • Catterall, W.A.1
  • 32
    • 84877708815 scopus 로고    scopus 로고
    • Molecular architecture of a sodium channel S6 helix
    • Yang, Y.; Estacion, M.; Dib-Hajj, S. D.; Waxman, S. G. Molecular architecture of a sodium channel S6 helix J. Biol. Chem. 2013, 288 (19) 13741-13747
    • (2013) J. Biol. Chem. , vol.288 , Issue.19 , pp. 13741-13747
    • Yang, Y.1    Estacion, M.2    Dib-Hajj, S.D.3    Waxman, S.G.4
  • 33
  • 34
    • 84896299188 scopus 로고    scopus 로고
    • Evolutionarily conserved intracellular gate of voltage-dependent sodium channels
    • Oelstrom, K.; Goldschen-Ohm, M. P.; Holmgren, M.; Chanda, B. Evolutionarily conserved intracellular gate of voltage-dependent sodium channels Nature Commun. 2014, 5, 3420
    • (2014) Nature Commun. , vol.5 , pp. 3420
    • Oelstrom, K.1    Goldschen-Ohm, M.P.2    Holmgren, M.3    Chanda, B.4
  • 35
    • 84874068206 scopus 로고    scopus 로고
    • Proton sensors in the pore domain of the cardiac voltage-gated sodium channel
    • Jones, D. K.; Peters, C. H.; Allard, C. R.; Claydon, T. W.; Ruben, P. C. Proton sensors in the pore domain of the cardiac voltage-gated sodium channel J. Biol. Chem. 2013, 288 (7) 4782-4791
    • (2013) J. Biol. Chem. , vol.288 , Issue.7 , pp. 4782-4791
    • Jones, D.K.1    Peters, C.H.2    Allard, C.R.3    Claydon, T.W.4    Ruben, P.C.5
  • 36
    • 84857211318 scopus 로고    scopus 로고
    • + channel β subunits: Overachievers of the ion channel family
    • + channel β subunits: overachievers of the ion channel family Front. Pharmacol. 2011, 2, 53
    • (2011) Front. Pharmacol. , vol.2 , pp. 53
    • Brackenbury, W.J.1    Isom, L.L.2
  • 40
    • 84883207988 scopus 로고    scopus 로고
    • vβ4 open-channel blocking peptide
    • vβ4 open-channel blocking peptide J. Gen. Physiol. 2013, 142 (3) 191-206
    • (2013) J. Gen. Physiol. , vol.142 , Issue.3 , pp. 191-206
    • Lewis, A.H.1    Raman, I.M.2
  • 42
    • 84903906262 scopus 로고    scopus 로고
    • Altered sodium channel gating as molecular basis for pain: Contribution of activation, inactivation, and resurgent currents
    • Lampert, A.; Eberhardt, M.; Waxman, S. G. Altered sodium channel gating as molecular basis for pain: contribution of activation, inactivation, and resurgent currents Handb. Exp. Pharmacol. 2014, 221, 91-110
    • (2014) Handb. Exp. Pharmacol. , vol.221 , pp. 91-110
    • Lampert, A.1    Eberhardt, M.2    Waxman, S.G.3
  • 43
    • 74949144432 scopus 로고    scopus 로고
    • Human voltage-gated sodium channel mutations that cause inherited neuronal and muscle channelopathies increase resurgent sodium currents
    • Jarecki, B. W.; Piekarz, A. D.; Jackson, J. O.; Cummins, T. R. Human voltage-gated sodium channel mutations that cause inherited neuronal and muscle channelopathies increase resurgent sodium currents J. Clin. Invest. 2010, 120 (1) 369-378
    • (2010) J. Clin. Invest. , vol.120 , Issue.1 , pp. 369-378
    • Jarecki, B.W.1    Piekarz, A.D.2    Jackson, J.O.3    Cummins, T.R.4
  • 44
    • 84901008873 scopus 로고    scopus 로고
    • Tetrodotoxin-resistant sodium channels in sensory neurons generate slow resurgent currents that are enhanced by inflammatory mediators
    • Tan, Z. Y.; Piekarz, A. D.; Priest, B. T.; Knopp, K. L.; Krajewski, J. L.; McDermott, J. S.; Nisenbaum, E. S.; Cummins, T. R. Tetrodotoxin-resistant sodium channels in sensory neurons generate slow resurgent currents that are enhanced by inflammatory mediators J. Neurosci. 2014, 34 (21) 7190-7197
    • (2014) J. Neurosci. , vol.34 , Issue.21 , pp. 7190-7197
    • Tan, Z.Y.1    Piekarz, A.D.2    Priest, B.T.3    Knopp, K.L.4    Krajewski, J.L.5    McDermott, J.S.6    Nisenbaum, E.S.7    Cummins, T.R.8
  • 45
    • 84866179225 scopus 로고    scopus 로고
    • Pathophysiological role of omega pore current in channelopathies
    • Jurkat-Rott, K.; Groome, J.; Lehmann-Horn, F. Pathophysiological role of omega pore current in channelopathies Front. Pharmacol. 2012, 11, 3-112
    • (2012) Front. Pharmacol. , vol.11 , pp. 3-112
    • Jurkat-Rott, K.1    Groome, J.2    Lehmann-Horn, F.3
  • 46
    • 84901059842 scopus 로고    scopus 로고
    • Biophysics, pathophysiology, and pharmacology of ion channel gating pores
    • Moreau, A.; Gosselin-Badaroudine, P.; Chahine, M. Biophysics, pathophysiology, and pharmacology of ion channel gating pores Front. Pharmacol. 2014, 3, 5-53
    • (2014) Front. Pharmacol. , vol.3 , pp. 5-53
    • Moreau, A.1    Gosselin-Badaroudine, P.2    Chahine, M.3
  • 47
    • 84885751310 scopus 로고    scopus 로고
    • Noncanonical roles of voltage-gated sodium channels
    • Black, J. A.; Waxman, S. G. Noncanonical roles of voltage-gated sodium channels Neuron 2013, 80 (2) 280-291
    • (2013) Neuron , vol.80 , Issue.2 , pp. 280-291
    • Black, J.A.1    Waxman, S.G.2
  • 48
    • 77955568196 scopus 로고    scopus 로고
    • Sodium channelopathies of skeletal muscle result from gain or loss of function
    • Jurkat-Rott, K.; Holzherr, B.; Fauler, M.; Lehmann-Horn, F. Sodium channelopathies of skeletal muscle result from gain or loss of function Pflugers Arch. 2010, 460 (2) 239-248
    • (2010) Pflugers Arch. , vol.460 , Issue.2 , pp. 239-248
    • Jurkat-Rott, K.1    Holzherr, B.2    Fauler, M.3    Lehmann-Horn, F.4
  • 50
    • 84882729458 scopus 로고    scopus 로고
    • Regulation of cough and action potentials by voltage-gated Na channels
    • Carr, M. J. Regulation of cough and action potentials by voltage-gated Na channels Pulm. Pharmacol. Ther. 2013, 26 (5) 508-509
    • (2013) Pulm. Pharmacol. Ther. , vol.26 , Issue.5 , pp. 508-509
    • Carr, M.J.1
  • 51
    • 84875466657 scopus 로고    scopus 로고
    • Persistent current blockers of voltage-gated sodium channels: A clinical opportunity for controlling metastatic disease
    • Djamgoz, M. B.; Onkal, R. Persistent current blockers of voltage-gated sodium channels: a clinical opportunity for controlling metastatic disease Recent Pat. Anti-Cancer Drug Discovery 2013, 8 (1) 66-84
    • (2013) Recent Pat. Anti-Cancer Drug Discovery , vol.8 , Issue.1 , pp. 66-84
    • Djamgoz, M.B.1    Onkal, R.2
  • 52
    • 84890256389 scopus 로고    scopus 로고
    • Channelopathy pathogenesis in autism spectrum disorders
    • Schmunk, G.; Gargus, J. J. Channelopathy pathogenesis in autism spectrum disorders Front. Genet. 2013, 4, 222
    • (2013) Front. Genet. , vol.4 , pp. 222
    • Schmunk, G.1    Gargus, J.J.2
  • 55
    • 84891854608 scopus 로고    scopus 로고
    • Sodium channels, inherited epilepsy, and antiepileptic drugs
    • Catterall, W. A. Sodium channels, inherited epilepsy, and antiepileptic drugs Annu. Rev. Pharmacol. Toxicol. 2014, 54, 317-338
    • (2014) Annu. Rev. Pharmacol. Toxicol. , vol.54 , pp. 317-338
    • Catterall, W.A.1
  • 56
    • 84921998193 scopus 로고    scopus 로고
    • Channelopathies, painful neuropathy, and diabetes: Which way does the causal arrow point?
    • Hoeijmakers, J. G.; Faber, C. G.; Merkies, I. S.; Waxman, S. G. Channelopathies, painful neuropathy, and diabetes: which way does the causal arrow point? Trends Mol. Med. 2014, 20, 544-550 10.1016/j.molmed.2014.06.003
    • (2014) Trends Mol. Med. , vol.20 , pp. 544-550
    • Hoeijmakers, J.G.1    Faber, C.G.2    Merkies, I.S.3    Waxman, S.G.4
  • 59
    • 84901234337 scopus 로고    scopus 로고
    • Painful and painless channelopathies
    • Bennett, D. L.; Woods, C. G. Painful and painless channelopathies Lancet Neurol. 2014, 13 (6) 587-599
    • (2014) Lancet Neurol. , vol.13 , Issue.6 , pp. 587-599
    • Bennett, D.L.1    Woods, C.G.2
  • 69
    • 83755171750 scopus 로고    scopus 로고
    • The molecular basis of acid insensitivity in the African naked mole-rat
    • Smith, E. S.; Omerbašić, D.; Lechner, S. G.; Anirudhan, G.; Lapatsina, L.; Lewin, G. R. The molecular basis of acid insensitivity in the African naked mole-rat Science 2011, 334 (6062) 1557-1560
    • (2011) Science , vol.334 , Issue.6062 , pp. 1557-1560
    • Smith, E.S.1    Omerbašić, D.2    Lechner, S.G.3    Anirudhan, G.4    Lapatsina, L.5    Lewin, G.R.6
  • 74
    • 84886246352 scopus 로고    scopus 로고
    • Voltage-gated sodium channel in grasshopper mice defends against bark scorpion toxin
    • Rowe, A. H.; Xiao, Y.; Rowe, M. P.; Cummins, T. R.; Zakon, H. H. Voltage-gated sodium channel in grasshopper mice defends against bark scorpion toxin Science 2013, 342 (6157) 441-446
    • (2013) Science , vol.342 , Issue.6157 , pp. 441-446
    • Rowe, A.H.1    Xiao, Y.2    Rowe, M.P.3    Cummins, T.R.4    Zakon, H.H.5
  • 78
    • 0141529982 scopus 로고    scopus 로고
    • v1.3 and functional involvement in neuronal hyperexcitability associated with central neuropathic pain after spinal cord injury
    • v1.3 and functional involvement in neuronal hyperexcitability associated with central neuropathic pain after spinal cord injury J. Neurosci. 2003, 23 (26) 8881-8892
    • (2003) J. Neurosci. , vol.23 , Issue.26 , pp. 8881-8892
    • Hains, B.C.1    Klein, J.P.2    Saab, C.Y.3    Craner, M.J.4    Black, J.A.5    Waxman, S.G.6
  • 82
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • Catterall, W. A. Ion channel voltage sensors: structure, function, and pathophysiology Neuron 2010, 67 (6) 915-928
    • (2010) Neuron , vol.67 , Issue.6 , pp. 915-928
    • Catterall, W.A.1
  • 84
    • 40849142344 scopus 로고    scopus 로고
    • Inhibition of sodium channel gating by trapping the domain II voltage sensor with protoxin II
    • Sokolov, S.; Kraus, R. L.; Scheuer, T.; Catterall, W. A. Inhibition of sodium channel gating by trapping the domain II voltage sensor with protoxin II Mol. Pharmacol. 2008, 73 (3) 1020-1028
    • (2008) Mol. Pharmacol. , vol.73 , Issue.3 , pp. 1020-1028
    • Sokolov, S.1    Kraus, R.L.2    Scheuer, T.3    Catterall, W.A.4
  • 89
    • 37349071555 scopus 로고    scopus 로고
    • The investigational anticonvulsant lacosamide selectively enhances slow inactivation of voltage-gated sodium channels
    • Errington, A. C.; Stöhr, T.; Heers, C.; Lees, G. The investigational anticonvulsant lacosamide selectively enhances slow inactivation of voltage-gated sodium channels Mol. Pharmacol. 2008, 73 (1) 157-169
    • (2008) Mol. Pharmacol. , vol.73 , Issue.1 , pp. 157-169
    • Errington, A.C.1    Stöhr, T.2    Heers, C.3    Lees, G.4
  • 90
    • 84897421326 scopus 로고    scopus 로고
    • Block of human cardiac sodium channels by lacosamide: Evidence for slow drug binding along the activation pathway
    • Wang, G. K.; Wang, S. Y. Block of human cardiac sodium channels by lacosamide: evidence for slow drug binding along the activation pathway Mol. Pharmacol. 2014, 85 (5) 692-702
    • (2014) Mol. Pharmacol. , vol.85 , Issue.5 , pp. 692-702
    • Wang, G.K.1    Wang, S.Y.2
  • 91
    • 33847344389 scopus 로고    scopus 로고
    • Gating pore current in an inherited ion channelopathy
    • Sokolov, S.; Scheuer, T.; Catterall, W. A. Gating pore current in an inherited ion channelopathy Nature 2007, 446 (7131) 76-78
    • (2007) Nature , vol.446 , Issue.7131 , pp. 76-78
    • Sokolov, S.1    Scheuer, T.2    Catterall, W.A.3
  • 96
    • 84894089580 scopus 로고    scopus 로고
    • v1.9 for treatment of pathological cough
    • v1.9 for treatment of pathological cough Lung 2014, 192 (1) 15-20
    • (2014) Lung , vol.192 , Issue.1 , pp. 15-20
    • Muroiaaa, Y.1    Undem, B.J.2
  • 97
    • 0014274924 scopus 로고
    • The failure of respiration in death by tetrodotoxin poisoning
    • Cheng, K. K.; Ling, Y. L.; Wang, J. C. The failure of respiration in death by tetrodotoxin poisoning Exp. Physiol. Cognit. Med. Sci. 1968, 53 (2) 119-128
    • (1968) Exp. Physiol. Cognit. Med. Sci. , vol.53 , Issue.2 , pp. 119-128
    • Cheng, K.K.1    Ling, Y.L.2    Wang, J.C.3
  • 98
    • 84868150677 scopus 로고    scopus 로고
    • Voltage-gated sodium channels and metastatic disease
    • Brackenbury, W. J. Voltage-gated sodium channels and metastatic disease Channels (Austin) 2012, 6 (5) 352-361
    • (2012) Channels (Austin) , vol.6 , Issue.5 , pp. 352-361
    • Brackenbury, W.J.1
  • 100
    • 84901228346 scopus 로고    scopus 로고
    • Voltage-gated sodium channels were differentially expressed in human normal prostate, benign prostatic hyperplasia and prostate cancer cells
    • Shan, B.; Dong, M.; Tang, H.; Wang, N.; Zhang, J.; Yan, C.; Jiao, X.; Zhang, H.; Wang, C. Voltage-gated sodium channels were differentially expressed in human normal prostate, benign prostatic hyperplasia and prostate cancer cells Oncol. Lett. 2014, 8 (1) 345-350
    • (2014) Oncol. Lett. , vol.8 , Issue.1 , pp. 345-350
    • Shan, B.1    Dong, M.2    Tang, H.3    Wang, N.4    Zhang, J.5    Yan, C.6    Jiao, X.7    Zhang, H.8    Wang, C.9
  • 101
    • 84909946510 scopus 로고    scopus 로고
    • The sodium channel β1 subunit mediates outgrowth of neurite-like processes on breast cancer cells and promotes tumor growth and metastasis
    • Nelson, M.; Millican-Slater, R.; Forrest, L. C.; Brackenbury, W. J. The sodium channel β1 subunit mediates outgrowth of neurite-like processes on breast cancer cells and promotes tumor growth and metastasis Int. J. Cancer 2014, 135 (10) 2338-2351
    • (2014) Int. J. Cancer , vol.135 , Issue.10 , pp. 2338-2351
    • Nelson, M.1    Millican-Slater, R.2    Forrest, L.C.3    Brackenbury, W.J.4
  • 108
    • 40549135991 scopus 로고    scopus 로고
    • Mechanisms of disease: Sodium channels and neuroprotection in multiple sclerosis-current status
    • Waxman, S. G. Mechanisms of disease: sodium channels and neuroprotection in multiple sclerosis-current status Nature Clin. Pract. Neurol. 2008, 4 (3) 159-169
    • (2008) Nature Clin. Pract. Neurol. , vol.4 , Issue.3 , pp. 159-169
    • Waxman, S.G.1
  • 110
    • 84872419608 scopus 로고    scopus 로고
    • The molecular mystique of tetrodotoxin
    • For a recent review: Moczydlowski, E. G. The molecular mystique of tetrodotoxin Toxicon 2013, 63, 165-183
    • (2013) Toxicon , vol.63 , pp. 165-183
    • Moczydlowski, E.G.1
  • 112
    • 84897998566 scopus 로고    scopus 로고
    • Mechanism of tetrodotoxin block and resistance in sodium channels
    • Chen, R.; Chung, S.-H. Mechanism of tetrodotoxin block and resistance in sodium channels Biochem. Biophys. Res. Commun. 2014, 446, 370-374
    • (2014) Biochem. Biophys. Res. Commun. , vol.446 , pp. 370-374
    • Chen, R.1    Chung, S.-H.2
  • 114
    • 1842481343 scopus 로고    scopus 로고
    • The structure of Zetekitoxin AB, a saxitoxin analog from the Panamanian golden frog Azelopus zeteki: A potent sodium channel blocker
    • Yotsu-Yamashita, M.; Kim, Y. H.; Dudley, S. C.; Choudhary, G.; Pfahnl, A.; Oshima, Y.; Daly, J. W. The structure of Zetekitoxin AB, a saxitoxin analog from the Panamanian golden frog Azelopus zeteki: a potent sodium channel blocker Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 4346-4351
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4346-4351
    • Yotsu-Yamashita, M.1    Kim, Y.H.2    Dudley, S.C.3    Choudhary, G.4    Pfahnl, A.5    Oshima, Y.6    Daly, J.W.7
  • 115
    • 84899502699 scopus 로고    scopus 로고
    • Isolation of 6-deoxytetrodotoxin from the pufferfish, Takfugu padalis, and a comparison of the effects of the C-6 and C-11 hydroxy groups of tetrodotoxin on its activity
    • Kudo, Y.; Finn, J.; Fukushima, K.; Sakugawa, S.; Cho, Y.; Konoki, K.; Yotsu-Yamashita, M. Isolation of 6-deoxytetrodotoxin from the pufferfish, Takfugu padalis, and a comparison of the effects of the C-6 and C-11 hydroxy groups of tetrodotoxin on its activity J. Nat. Prod. 2014, 77, 1000-1004
    • (2014) J. Nat. Prod. , vol.77 , pp. 1000-1004
    • Kudo, Y.1    Finn, J.2    Fukushima, K.3    Sakugawa, S.4    Cho, Y.5    Konoki, K.6    Yotsu-Yamashita, M.7
  • 118
    • 0000708326 scopus 로고
    • Conformational analysis of the sodium channel modulator, brevetoxin A, comparison with brevetoxin B. Conformations, and a hypothesis about the common pharmacophore of the "site 5" toxins
    • Rein, K. S.; Baden, D. G.; Gawley, R. E. Conformational analysis of the sodium channel modulator, brevetoxin A, comparison with brevetoxin B. Conformations, and a hypothesis about the common pharmacophore of the "site 5" toxins J. Org. Chem. 1994, 59, 2101-2106
    • (1994) J. Org. Chem. , vol.59 , pp. 2101-2106
    • Rein, K.S.1    Baden, D.G.2    Gawley, R.E.3
  • 120
    • 33749556457 scopus 로고    scopus 로고
    • Species selective resistance of cardiac muscle voltage gated sodium channels: Characterization of brevetoxin and ciguatoxin binding sites in rat and fish
    • Bottein Dechraoui, M.-Y.; Wacksman, J. J.; Ramsdell, J. S. Species selective resistance of cardiac muscle voltage gated sodium channels: characterization of brevetoxin and ciguatoxin binding sites in rat and fish Toxicon 2006, 48, 702-712
    • (2006) Toxicon , vol.48 , pp. 702-712
    • Bottein Dechraoui, M.-Y.1    Wacksman, J.J.2    Ramsdell, J.S.3
  • 121
    • 84877742621 scopus 로고    scopus 로고
    • Neurotoxicity and reactive astrogliosis in the anterior cingulate cortex in acute ciguatera poisoning
    • Zhang, X.; Cao, B.; Wang, J.; Liu, J.; Vian Tung, V. O.; Sing Lam, P. K.; Chan, L. L.; Li, Y. Neurotoxicity and reactive astrogliosis in the anterior cingulate cortex in acute ciguatera poisoning Neuromol. Med. 2013, 15, 310-323
    • (2013) Neuromol. Med. , vol.15 , pp. 310-323
    • Zhang, X.1    Cao, B.2    Wang, J.3    Liu, J.4    Vian Tung, V.O.5    Sing Lam, P.K.6    Chan, L.L.7    Li, Y.8
  • 122
    • 84901756047 scopus 로고    scopus 로고
    • Ciguatera fish poisoning and climate change: Analysis of national poison center data in the United States 2001-2011
    • Gingold, D. B.; Strickland, M. J.; Hess, J. J. Ciguatera fish poisoning and climate change: analysis of national poison center data in the united states 2001-2011 Environ. Health Perspect. 2014, 122 (6) 580-586
    • (2014) Environ. Health Perspect. , vol.122 , Issue.6 , pp. 580-586
    • Gingold, D.B.1    Strickland, M.J.2    Hess, J.J.3
  • 123
    • 84902186723 scopus 로고    scopus 로고
    • Ciguatera fish poisoning in Hong Kong-A 10 year perspective on the class of ciguatoxins
    • Wong, C.-K.; Hung, P.; Lo, J. Y. C. Ciguatera fish poisoning in Hong Kong-a 10 year perspective on the class of ciguatoxins Toxicon 2014, 86, 96-106
    • (2014) Toxicon , vol.86 , pp. 96-106
    • Wong, C.-K.1    Hung, P.2    Lo, J.Y.C.3
  • 124
    • 84898488456 scopus 로고    scopus 로고
    • Preparation of anti-ciguatoxin monoclonal antibodies using synthetic haptens: Sandwich ELISA detection of ciguatoxins
    • Tsumuraya, T.; Fujii, I.; Hirama, M. Preparation of anti-ciguatoxin monoclonal antibodies using synthetic haptens: sandwich ELISA detection of ciguatoxins J. AOAC Int. 2014, 97 (2) 373-379
    • (2014) J. AOAC Int. , vol.97 , Issue.2 , pp. 373-379
    • Tsumuraya, T.1    Fujii, I.2    Hirama, M.3
  • 125
    • 84891837732 scopus 로고    scopus 로고
    • Neuroprotective effects of rosmarinic acid on ciguatoxin in primary human neurons
    • Braidy, N.; Matin, A.; Rossi, F.; Chinain, M.; Laurent, D.; Guillemin, G. J. Neuroprotective effects of rosmarinic acid on ciguatoxin in primary human neurons Neurotox. Res. 2014, 25, 226-234
    • (2014) Neurotox. Res. , vol.25 , pp. 226-234
    • Braidy, N.1    Matin, A.2    Rossi, F.3    Chinain, M.4    Laurent, D.5    Guillemin, G.J.6
  • 126
    • 33947484123 scopus 로고
    • Batrachotoxin. the active principle of the Colombian arrow poison frog, Phyllobates bicolor
    • Daly, J. W.; Witkop, B.; Bommer, P.; Biemann, K. Batrachotoxin. The active principle of the Colombian arrow poison frog, Phyllobates bicolor J. Am. Chem. Soc. 1965, 87 (1) 124-126
    • (1965) J. Am. Chem. Soc. , vol.87 , Issue.1 , pp. 124-126
    • Daly, J.W.1    Witkop, B.2    Bommer, P.3    Biemann, K.4
  • 127
    • 67651089983 scopus 로고    scopus 로고
    • Discovery of batrachotoxin: The launch of the frog alkaloid program at NIH
    • Garraffo, H. M.; Spande, T. F. Discovery of batrachotoxin: the launch of the frog alkaloid program at NIH Heterocycles 2009, 79, 195-205
    • (2009) Heterocycles , vol.79 , pp. 195-205
    • Garraffo, H.M.1    Spande, T.F.2
  • 128
    • 84893841638 scopus 로고    scopus 로고
    • Poor alkaloid sequestration by arrow poison frogs of the genus Phyllobates from Costa Rica
    • Mebs, D.; Alvarez, J. V.; Pogoda, W.; Toennes, S. W.; Kóhler, G. Poor alkaloid sequestration by arrow poison frogs of the genus Phyllobates from Costa Rica Toxicon 2014, 80, 73-77
    • (2014) Toxicon , vol.80 , pp. 73-77
    • Mebs, D.1    Alvarez, J.V.2    Pogoda, W.3    Toennes, S.W.4    Kóhler, G.5
  • 130
    • 0031639628 scopus 로고    scopus 로고
    • Effects of veratridine on sodium currents and fluxes
    • Ulbricht, W. Effects of veratridine on sodium currents and fluxes Rev. Physiol. Biochem. Pharmacol. 1998, 133, 1-54
    • (1998) Rev. Physiol. Biochem. Pharmacol. , vol.133 , pp. 1-54
    • Ulbricht, W.1
  • 131
    • 84859894614 scopus 로고    scopus 로고
    • Solution NMR analysis of the binding mechanism of DIVS6 model peptides of voltage-gated sodium channels and the lipid soluble alkaloid veratridine
    • Yoshinaka-Niitsu, A.; Yamagaki, T.; Harada, M.; Tachibana, K. Solution NMR analysis of the binding mechanism of DIVS6 model peptides of voltage-gated sodium channels and the lipid soluble alkaloid veratridine Bioorg. Med. Chem. 2012, 20, 2796-2802
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 2796-2802
    • Yoshinaka-Niitsu, A.1    Yamagaki, T.2    Harada, M.3    Tachibana, K.4
  • 133
    • 77953229584 scopus 로고    scopus 로고
    • In vitro and in vivo effects of water extract of white cocoa tea (Camellia ptilophylla) against human prostate cancer
    • Peng, L.; Khan, N.; Afaq, F.; Ye, C.; Mukhtar, H. In vitro and in vivo effects of water extract of white cocoa tea (Camellia ptilophylla) against human prostate cancer Pharm. Res. 2010, 27, 1128-1137
    • (2010) Pharm. Res. , vol.27 , pp. 1128-1137
    • Peng, L.1    Khan, N.2    Afaq, F.3    Ye, C.4    Mukhtar, H.5
  • 135
    • 84877722928 scopus 로고    scopus 로고
    • Effects of (-)-gallocatechin-3-gallate on tetrodotoxin-resistant voltage-gated sodium channels in rat dorsal root ganglion neurons
    • Zhang, Y.; Jia, Y.-Y.; Guo, J.-L.; Liu, P.-Q.; Jiang, J.-M. Effects of (-)-gallocatechin-3-gallate on tetrodotoxin-resistant voltage-gated sodium channels in rat dorsal root ganglion neurons Int. J. Mol. Sci. 2013, 14, 9779-9789
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 9779-9789
    • Zhang, Y.1    Jia, Y.-Y.2    Guo, J.-L.3    Liu, P.-Q.4    Jiang, J.-M.5
  • 136
    • 0029096389 scopus 로고
    • Antillatoxin: An exceptionally ichthyotoxic cyclic lipopeptide from the tropical cyanobacterium Lyngbya majuscula
    • Orjala, J.; Nagle, D. G.; Hsu, V. L.; Gerwick, W. H. Antillatoxin: an exceptionally ichthyotoxic cyclic lipopeptide from the tropical cyanobacterium Lyngbya majuscula J. Am. Chem. Soc. 1995, 117, 8281-8282
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8281-8282
    • Orjala, J.1    Nagle, D.G.2    Hsu, V.L.3    Gerwick, W.H.4
  • 137
    • 0033231630 scopus 로고    scopus 로고
    • Antillatoxin and kalkitoxin, ichthyotoxins from the tropical cyanobacterium Lyngbya majuscula, induce distinct temporal paterns of NMDA receptor-mediated neurotoxicity
    • Berman, F. W.; Gerwick, W. H.; Murray, T. F. Antillatoxin and kalkitoxin, ichthyotoxins from the tropical cyanobacterium Lyngbya majuscula, induce distinct temporal paterns of NMDA receptor-mediated neurotoxicity Toxicon 1999, 37 (11) 1645-1648
    • (1999) Toxicon , vol.37 , Issue.11 , pp. 1645-1648
    • Berman, F.W.1    Gerwick, W.H.2    Murray, T.F.3
  • 138
    • 84894096248 scopus 로고    scopus 로고
    • Chemical construction and structural permutation of neurotoxic natural product, antillatoxin: Importance of the three-dimensional structure of the bulky side chain
    • Inoue, M. Chemical construction and structural permutation of neurotoxic natural product, antillatoxin: importance of the three-dimensional structure of the bulky side chain Proc. Jpn. Acad. (Ser. B) 2014, 90, 56-65
    • (2014) Proc. Jpn. Acad. (Ser. B) , vol.90 , pp. 56-65
    • Inoue, M.1
  • 143
    • 84924353392 scopus 로고    scopus 로고
    • Roles of individual disulfide bridges in the conformation and activity of μ-conotoxin GIIIA, a peptide blocker of muscle sodium channels
    • Sato, K.; Yamaguchi, Y.; Ishida, Y. Roles of individual disulfide bridges in the conformation and activity of μ-conotoxin GIIIA, a peptide blocker of muscle sodium channels Int. J. Pept. Res. Ther. 2014, 20, 253-258
    • (2014) Int. J. Pept. Res. Ther. , vol.20 , pp. 253-258
    • Sato, K.1    Yamaguchi, Y.2    Ishida, Y.3
  • 148
    • 84878009040 scopus 로고    scopus 로고
    • Expanding chemical diversity of conotoxins: Peptoid-peptide chimeras of the sodium channel blocker μ-KIIIA and its selenopeptide analogues
    • Walewska, A.; Han, T. S.; Zhang, M.-M.; Yoshikami, D.; Bulaj, G.; Rolka, K. Expanding chemical diversity of conotoxins: peptoid-peptide chimeras of the sodium channel blocker μ-KIIIA and its selenopeptide analogues Eur. J. Med. Chem. 2013, 65, 144-150
    • (2013) Eur. J. Med. Chem. , vol.65 , pp. 144-150
    • Walewska, A.1    Han, T.S.2    Zhang, M.-M.3    Yoshikami, D.4    Bulaj, G.5    Rolka, K.6
  • 149
    • 29944442294 scopus 로고    scopus 로고
    • A novel conotoxin from Conus striatus, μ-SIIIA, selectively blocking rat tetrodotoxin-resistant sodium channels
    • Wang, C.-Z.; Zhang, H.; Jiang, H.; Lu, W.; Zhao, Z.-Q.; Chi, C.-W. A novel conotoxin from Conus striatus, μ-SIIIA, selectively blocking rat tetrodotoxin-resistant sodium channels Toxicon 2006, 47 (1) 122-132
    • (2006) Toxicon , vol.47 , Issue.1 , pp. 122-132
    • Wang, C.-Z.1    Zhang, H.2    Jiang, H.3    Lu, W.4    Zhao, Z.-Q.5    Chi, C.-W.6
  • 150
    • 84897735499 scopus 로고    scopus 로고
    • Re-engineering the μ-conotoxin SIIIA scaffold
    • Akondi, K. B.; Lewis, R. J.; Alewood, P. F. Re-engineering the μ-conotoxin SIIIA scaffold Biopolymers 2013, 101, 347-354
    • (2013) Biopolymers , vol.101 , pp. 347-354
    • Akondi, K.B.1    Lewis, R.J.2    Alewood, P.F.3
  • 153
    • 84875158614 scopus 로고    scopus 로고
    • Pharmacological fractionation of tetrodotoxin-sensitive sodium currents in rat dorsal root ganglion neurons by μ-conotoxins
    • Zhang, M.-M.; Wilson, M. J.; Gajewjak, J.; Rivier, J. E.; Bulaj, G.; Olivera, B. M.; Yoshikami, D. Pharmacological fractionation of tetrodotoxin-sensitive sodium currents in rat dorsal root ganglion neurons by μ-conotoxins Br. J. Pharmacol. 2013, 169, 102-114
    • (2013) Br. J. Pharmacol. , vol.169 , pp. 102-114
    • Zhang, M.-M.1    Wilson, M.J.2    Gajewjak, J.3    Rivier, J.E.4    Bulaj, G.5    Olivera, B.M.6    Yoshikami, D.7
  • 161
    • 80053013648 scopus 로고    scopus 로고
    • Structure-function map of the receptor site for β-scorpion toxins in domain II of voltage-gated sodium channels
    • Zhang, J. Z.; Yarov-Yarovoy, V.; Scheuer, T.; Karbat, I.; Cohen, L.; Gordon, D.; Gurevitz, M.; Catterall, W. A. Structure-function map of the receptor site for β-scorpion toxins in domain II of voltage-gated sodium channels J. Biol. Chem. 2011, 286 (38) 33641-33651
    • (2011) J. Biol. Chem. , vol.286 , Issue.38 , pp. 33641-33651
    • Zhang, J.Z.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Karbat, I.4    Cohen, L.5    Gordon, D.6    Gurevitz, M.7    Catterall, W.A.8
  • 162
    • 84879761724 scopus 로고    scopus 로고
    • Chemical engineering and structural and pharmacological characterization of the α-scorpion toxin OD1
    • Durek, T.; Vetter, I.; Wang, C.-I.; Motin, L.; Knapp, O.; Adams, D. J.; Lewis, R. J.; Alewood, P. F. Chemical engineering and structural and pharmacological characterization of the α-scorpion toxin OD1 ACS Chem. Biol. 2013, 8, 1215-1222
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1215-1222
    • Durek, T.1    Vetter, I.2    Wang, C.-I.3    Motin, L.4    Knapp, O.5    Adams, D.J.6    Lewis, R.J.7    Alewood, P.F.8
  • 163
    • 33745249950 scopus 로고    scopus 로고
    • Potent modulation of the voltage-gated sodium channel by OD1, a toxin from the scorpion Odonthobuthus doriae
    • Maertens, C.; Cuypers, E.; Amininasab, M.; Jalali, A.; Vatanpour, H.; Tytgat, J. Potent modulation of the voltage-gated sodium channel by OD1, a toxin from the scorpion Odonthobuthus doriae Mol. Pharmacol. 2006, 70 (1) 405-414
    • (2006) Mol. Pharmacol. , vol.70 , Issue.1 , pp. 405-414
    • Maertens, C.1    Cuypers, E.2    Amininasab, M.3    Jalali, A.4    Vatanpour, H.5    Tytgat, J.6
  • 165
    • 84894630909 scopus 로고    scopus 로고
    • Characterization of a novel BmαTX47 toxin modulating sodium channels: The crucial role of expression vectors in toxin pharmacological activity
    • Li, T.; Xu, L.; Liu, H.; He, Y.; Liang, S.; Li, W.; Wu, Y. Characterization of a novel BmαTX47 toxin modulating sodium channels: the crucial role of expression vectors in toxin pharmacological activity Toxins 2014, 6, 816-829
    • (2014) Toxins , vol.6 , pp. 816-829
    • Li, T.1    Xu, L.2    Liu, H.3    He, Y.4    Liang, S.5    Li, W.6    Wu, Y.7
  • 166
    • 84863777217 scopus 로고    scopus 로고
    • Spider-venom peptides that target voltage-gated sodium channels: Pharmacological tools and potential therapeutic leads
    • Klint, J. K.; Senff, S.; Rupasinghe, D. B.; Er, S. Y.; Herzig, V.; Nicholson, G. M.; King, G. F. Spider-venom peptides that target voltage-gated sodium channels: pharmacological tools and potential therapeutic leads Toxicon 2012, 60, 478-491
    • (2012) Toxicon , vol.60 , pp. 478-491
    • Klint, J.K.1    Senff, S.2    Rupasinghe, D.B.3    Er, S.Y.4    Herzig, V.5    Nicholson, G.M.6    King, G.F.7
  • 167
    • 0035239222 scopus 로고    scopus 로고
    • The cysteine knot motif in toxins and implications for drug design
    • Craik, D. J.; Daly, N. L.; Waine, C. The cysteine knot motif in toxins and implications for drug design Toxicon 2001, 39, 43-60
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 168
    • 0033040926 scopus 로고    scopus 로고
    • Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena
    • Shu, Q.; Liang, S. P. Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena J. Pept. Res. 1999, 53 (5) 486-491
    • (1999) J. Pept. Res. , vol.53 , Issue.5 , pp. 486-491
    • Shu, Q.1    Liang, S.P.2
  • 169
    • 84893318577 scopus 로고    scopus 로고
    • Analgesic effects of Huwentoxin-IV on animal models of inflammatory and neuropathic pain
    • Liu, Y.; Wu, Z.; Tang, D.; Xun, X.; Liu, L.; Li, X.; Nie, D.; Xiang, Y.; Yi, J.; Yi, J. Analgesic effects of Huwentoxin-IV on animal models of inflammatory and neuropathic pain Protein Pept. Lett. 2014, 21, 153-158
    • (2014) Protein Pept. Lett. , vol.21 , pp. 153-158
    • Liu, Y.1    Wu, Z.2    Tang, D.3    Xun, X.4    Liu, L.5    Li, X.6    Nie, D.7    Xiang, Y.8    Yi, J.9    Yi, J.10
  • 170
    • 84879525993 scopus 로고    scopus 로고
    • Synthesis and biological characterization of synthetic analogs of huwentoxin-IV, a neuronal tetrodotoxin-sensitive sodium channel inhibitor
    • Deng, M.; Luo, X.; Jiang, L.; Chen, H.; Wang, J.; He, H.; Liang, S. Synthesis and biological characterization of synthetic analogs of huwentoxin-IV, a neuronal tetrodotoxin-sensitive sodium channel inhibitor Toxicon 2013, 71, 57-65
    • (2013) Toxicon , vol.71 , pp. 57-65
    • Deng, M.1    Luo, X.2    Jiang, L.3    Chen, H.4    Wang, J.5    He, H.6    Liang, S.7
  • 171
    • 84906075173 scopus 로고    scopus 로고
    • Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage-gated sodium channels
    • Park, J. H.; Carlin, K. P.; Wu, G.; Ilyin, V. I.; Musza, L. L.; Blake, P. R.; Kyle, D. J. Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage-gated sodium channels J. Med. Chem. 2014, 57 (15) 6623-6631
    • (2014) J. Med. Chem. , vol.57 , Issue.15 , pp. 6623-6631
    • Park, J.H.1    Carlin, K.P.2    Wu, G.3    Ilyin, V.I.4    Musza, L.L.5    Blake, P.R.6    Kyle, D.J.7
  • 172
    • 15744403398 scopus 로고    scopus 로고
    • Differential phospholipid binding by site 3 and site 4 toxins
    • Smith, J. J.; Alphy, S.; Seibert, A. L.; Blumenthal, K. M. Differential phospholipid binding by site 3 and site 4 toxins J. Biol. Chem. 2005, 280 (12) 11127-11133
    • (2005) J. Biol. Chem. , vol.280 , Issue.12 , pp. 11127-11133
    • Smith, J.J.1    Alphy, S.2    Seibert, A.L.3    Blumenthal, K.M.4
  • 173
    • 0038010666 scopus 로고    scopus 로고
    • Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana
    • Liu, Z.; Dai, J.; Chen, Z.; Hu, W.; Xiao, Y.; Liang, S. Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana Cell. Mol. Life Sci. 2003, 60, 972-978
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 972-978
    • Liu, Z.1    Dai, J.2    Chen, Z.3    Hu, W.4    Xiao, Y.5    Liang, S.6
  • 174
    • 84930969777 scopus 로고    scopus 로고
    • Mapping the interaction site for the tarantula toxin hainantoxin-IV (β-TRTX-Hn2a) in the voltage sensor module of domain II of voltage-gated sodium channels
    • September 10
    • Cai, T.; Luo, J.; Meng, E.; Ding, J.; Liang, S.; Wang, S.; Liu, Z. Mapping the interaction site for the tarantula toxin hainantoxin-IV (β-TRTX-Hn2a) in the voltage sensor module of domain II of voltage-gated sodium channels. Peptides 2014, September 10.
    • (2014) Peptides
    • Cai, T.1    Luo, J.2    Meng, E.3    Ding, J.4    Liang, S.5    Wang, S.6    Liu, Z.7
  • 175
    • 84874395348 scopus 로고    scopus 로고
    • The venom of the fishing spider Dolomedes sulfurous contains various neurotoxins acting on voltage-activated ion channels in rat dorsal root ganglion neurons
    • Wang, H.; Zhang, F.; Li, D.; Xu, S.; He, J.; Yu, H.; Li, J.; Liu, Z.; Liang, S. The venom of the fishing spider Dolomedes sulfurous contains various neurotoxins acting on voltage-activated ion channels in rat dorsal root ganglion neurons Toxicon 2013, 65, 68-75
    • (2013) Toxicon , vol.65 , pp. 68-75
    • Wang, H.1    Zhang, F.2    Li, D.3    Xu, S.4    He, J.5    Yu, H.6    Li, J.7    Liu, Z.8    Liang, S.9
  • 176
    • 0018900234 scopus 로고
    • The potent excitatory effect of a novel polypeptide, anthopleurin-B, isolated from a sea anemone (Anthopleura xanthogrammica) on the frog spinal cord
    • Kudo, Y.; Shibata, S. The potent excitatory effect of a novel polypeptide, anthopleurin-B, isolated from a sea anemone (Anthopleura xanthogrammica) on the frog spinal cord J. Pharmacol. Exp. Ther. 1980, 214 (2) 443-448
    • (1980) J. Pharmacol. Exp. Ther. , vol.214 , Issue.2 , pp. 443-448
    • Kudo, Y.1    Shibata, S.2
  • 177
    • 70350374052 scopus 로고    scopus 로고
    • Sea anemone toxins affecting voltage-gated sodium channels-molecular and evolutionary features
    • Moran, Y.; Gordon, D.; Gurevitz, M. Sea anemone toxins affecting voltage-gated sodium channels-molecular and evolutionary features Toxicon 2009, 54 (8) 1089-1101
    • (2009) Toxicon , vol.54 , Issue.8 , pp. 1089-1101
    • Moran, Y.1    Gordon, D.2    Gurevitz, M.3
  • 179
    • 80053645532 scopus 로고    scopus 로고
    • Venoms as a platform for human drugs: Translating toxins into therapeutics
    • King, G. F. Venoms as a platform for human drugs: translating toxins into therapeutics Exp. Opin. Biol. Ther. 2011, 11 (11) 1469-1484
    • (2011) Exp. Opin. Biol. Ther. , vol.11 , Issue.11 , pp. 1469-1484
    • King, G.F.1
  • 180
  • 183
    • 84942281216 scopus 로고    scopus 로고
    • A Clinical Trial to Evaluate PF-05089771 on Its Own and as an Add-on Therapy to Pregabalin (Lyrica) for the Treatment of Pain Due to Diabetic Peripheral Neuropathy (DPN)
    • U.S. National Institutes of Health: Bethesda, MD, August 11, (accessed Mar 5, 2015)
    • A Clinical Trial To Evaluate PF-05089771 on Its Own and as an Add-on Therapy to Pregabalin (Lyrica) for the Treatment of Pain Due to Diabetic Peripheral Neuropathy (DPN). ClinicalTrials.gov; U.S. National Institutes of Health: Bethesda, MD, August 11, 2014; http://clinicaltrials.gov/ct2/show/NCT02215252?term=PF-05089771&rank=8 (accessed Mar 5, 2015).
    • (2014) ClinicalTrials.gov
  • 191
    • 84942257852 scopus 로고    scopus 로고
    • Convergence Pharmaceuticals: Cambridge, UK, (accessed Mar 20, 2015)id=16, (accessed Mar 20, 2015)
    • The Pipeline; Convergence Pharmaceuticals: Cambridge, UK, 2015; http://www.convergencepharma.com/?page
    • (2015) The Pipeline
  • 206
    • 84942281222 scopus 로고    scopus 로고
    • Xenon Pharmaceuticals, Inc. Burnaby, BC, Canada, (accessed Mar 5, 2015)
    • Selective Small-Molecule Sodium Channel Modulators for Dravet Syndrome, or DS; Xenon Pharmaceuticals, Inc.: Burnaby, BC, Canada, 2015; http://www.xenon-pharma.com/product-candidates/dravet-syndrome (accessed Mar 5, 2015).
    • (2015) Selective Small-Molecule Sodium Channel Modulators for Dravet Syndrome, or DS
  • 207
    • 84942281223 scopus 로고    scopus 로고
    • EDGAR Online, Inc. New York, (accessed Dec 15, 2015)
    • Prospectus Summary: Xenon Pharmaceuticals Inc.; EDGAR Online, Inc.: New York, 2014; http://sec.edgar-online.com/xenon-pharmaceuticals-inc/s-1-securities-registration-statement/2014/09/10/section5.aspx (accessed Dec 15, 2015).
    • (2014) Prospectus Summary: Xenon Pharmaceuticals Inc.
  • 209
    • 84942246695 scopus 로고    scopus 로고
    • Sumitomo Dainippon Pharma Co. Ltd. Osaka, (accessed Mar 5, 2015).profile.html (accessed Mar 5, 2015)
    • Profile of Major Products under Development (as of January 29, 2015); Sumitomo Dainippon Pharma Co. Ltd.: Osaka, 2015; http://www.ds-pharma.com/rd/clinical/pipeline
    • (2015) Profile of Major Products under Development (As of January 29, 2015)
  • 210
    • 84942249357 scopus 로고    scopus 로고
    • BioMed Central Ltd: London, (accessed Mar 5, 2015)
    • ISRCTN Registry; BioMed Central Ltd: London, 2015; http://www.controlled-trials.com/ISRCTN80154838/DSP2230 (accessed Mar 5, 2015).
    • (2015) ISRCTN Registry
  • 211
    • 84942281224 scopus 로고    scopus 로고
    • Nektar: San Francisco, (accessed Mar 5, 2015)
    • NKTR-171; Nektar: San Francisco, 2015; http://www.nektar.com/product pipeline/cnspainnktr-171.html (accessed Mar 5, 2015).
    • (2015) NKTR-171
  • 213
    • 84942281226 scopus 로고    scopus 로고
    • WEX Pharmaceuticals, Inc. Vancouver, BC, Canada, (accessed Mar 5, 2015.trials.asp?m=5&s=1&p=1 (accessed Mar 5, 2015
    • TTX; WEX Pharmaceuticals, Inc.: Vancouver, BC, Canada, 2015; http://www.wextech.ca/clinical
    • (2015) TTX
  • 214
    • 84942281227 scopus 로고    scopus 로고
    • Determine the Effect of AZD3161,Injected Intradermally, on Quantitative Sensory Testing Variables in Normal and Ultraviolet-C (UVC) Exposed Skin in Healthy Volunteers
    • U.S. National Institutes of Health: Bethesda, MD, Nov 10, (accessed Mar 5, 2015)
    • Determine the Effect of AZD3161,Injected Intradermally, on Quantitative Sensory Testing Variables in Normal and Ultraviolet-C (UVC) Exposed Skin in Healthy Volunteers. ClinicalTrials.gov; U.S. National Institutes of Health: Bethesda, MD, Nov 10, 2010; http://clinicaltrials.gov/show/NCT01240148 (accessed Mar 5, 2015).
    • (2010) ClinicalTrials.gov
  • 216
    • 84942281228 scopus 로고    scopus 로고
    • GSK2339345 Hypertussive Challenge Study
    • U.S. National Institutes of Health: Bethesda, MD, July 11, (accessed Mar 5, 2015)
    • GSK2339345 Hypertussive Challenge Study. ClinicalTrials.gov; U.S. National Institutes of Health: Bethesda, MD, July 11, 2013; https://clinicaltrials.gov/ct2/show/NCT01899768?term=GSK2339345&rank=3 (accessed Mar 5, 2015).
    • (2013) ClinicalTrials.gov
  • 217
    • 84897492866 scopus 로고    scopus 로고
    • Pharmacological Characterization of GSK2339345, A Novel Voltage-Gated Sodium Channel Blocker for the Symptomatic Relief of Cough
    • Kwong, K.; Webb, E. F.; Hunsberger, G. E.; Osborn, R. R.; Ghatta, S.; Ingleby, L.; Carr, M. J.; Kerns, J. K.; Rumsey, W. Pharmacological Characterization Of GSK2339345, A Novel Voltage-Gated Sodium Channel Blocker For The Symptomatic Relief Of Cough Am J. Resp. Crit. Care Med. 2013, 187, A4936 http://www.atsjournals.org/doi/pdf/10.1164/ajrccm-conference.2013.187.1
    • (2013) Am J. Resp. Crit. Care Med. , vol.187 , pp. A4936
    • Kwong, K.1    Webb, E.F.2    Hunsberger, G.E.3    Osborn, R.R.4    Ghatta, S.5    Ingleby, L.6    Carr, M.J.7    Kerns, J.K.8    Rumsey, W.9
  • 218
    • 84942281229 scopus 로고    scopus 로고
    • Safety, Tolerability and Pharmacokinetics of Repeat Doses of GSK1014802
    • U.S. National Institutes of Health: Bethesda, MD, May 7, (accessed on Mar 5, 2015)
    • Safety, Tolerability and Pharmacokinetics of Repeat Doses of GSK1014802. ClinicalTrials.gov; U.S. National Institutes of Health: Bethesda, MD, May 7, 2009; https://clinicaltrials.gov/ct2/show/NCT00908154?term=GSK1014802&rank=1 (accessed on Mar 5, 2015).
    • (2009) ClinicalTrials.gov
  • 220
    • 84886083169 scopus 로고    scopus 로고
    • Gilead: Foster City, CA, (accessed on Mar 5, 2015)
    • HIV/AIDS; Gilead: Foster City, CA, 2013; http://www.gilead.com/research/pipeline (accessed on Mar 5, 2015).
    • (2013) HIV/AIDS
  • 221
    • 84942281230 scopus 로고    scopus 로고
    • GS-6615
    • U.S. National Institutes of Health: Bethesda, MD, (accessed on Mar 5, 2015)
    • GS-6615. ClinicalTrials.gov; U.S. National Institutes of Health: Bethesda, MD, 2015; https://clinicaltrials.gov/ct2/results?term=GS6615&Search=Search; (accessed on Mar 5, 2015).
    • (2015) ClinicalTrials.gov
  • 222
    • 84864445461 scopus 로고    scopus 로고
    • The economic costs of pain in the United States
    • Gaskin, D. J.; Richard, P. The economic costs of pain in the United States J. Pain 2012, 13 (8) 715-724
    • (2012) J. Pain , vol.13 , Issue.8 , pp. 715-724
    • Gaskin, D.J.1    Richard, P.2
  • 223
    • 84925665870 scopus 로고    scopus 로고
    • A systematic review of therapeutic interventions to reduce acute and chronic post-surgical pain after amputation, thoracotomy or mastectomy
    • Humble, S. R.; Dalton, A. J.; Li, L. A systematic review of therapeutic interventions to reduce acute and chronic post-surgical pain after amputation, thoracotomy or mastectomy Eur. J. Pain 2014, 19, 451-465 10.1002/ejp.567
    • (2014) Eur. J. Pain , vol.19 , pp. 451-465
    • Humble, S.R.1    Dalton, A.J.2    Li, L.3
  • 224
    • 67349126560 scopus 로고    scopus 로고
    • Pharmacotherapy of chronic pain: A synthesis of recommendations from systematic reviews
    • Kroenke, K.; Krebs, E. E.; Bair, M. J. Pharmacotherapy of chronic pain: a synthesis of recommendations from systematic reviews Gen. Hosp. Psychiatry 2009, 31, 206-219
    • (2009) Gen. Hosp. Psychiatry , vol.31 , pp. 206-219
    • Kroenke, K.1    Krebs, E.E.2    Bair, M.J.3
  • 225
    • 84907434110 scopus 로고    scopus 로고
    • New strategies in ion channel screening for drug discovery: Are there ways to improve its productivity?
    • Farre, C.; Fertig, N. New strategies in ion channel screening for drug discovery: are there ways to improve its productivity? Expert Opin. Drug Discovery 2014, 9 (10) 1103-1107
    • (2014) Expert Opin. Drug Discovery , vol.9 , Issue.10 , pp. 1103-1107
    • Farre, C.1    Fertig, N.2
  • 226
    • 84898419493 scopus 로고    scopus 로고
    • Development and utilization of a fluorescence-based receptor-binding assay for the site 5 voltgage-sensistive sodium channel ligands brevetoxin and ciguatoxin
    • McCall, J.; M. Jacocks, H. M.; Niven, S. C.; Poli, M. A.; Baden, D. G.; Bourdelais, A. J. Development and utilization of a fluorescence-based receptor-binding assay for the site 5 voltgage-sensistive sodium channel ligands brevetoxin and ciguatoxin J. AOAC Int. 2014, 97 (2) 307-315
    • (2014) J. AOAC Int. , vol.97 , Issue.2 , pp. 307-315
    • McCall, J.1    Jacocks, H.M.M.2    Niven, S.C.3    Poli, M.A.4    Baden, D.G.5    Bourdelais, A.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.