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Volumn 4, Issue 3, 2006, Pages 157-192

Marine toxins that target voltage-gated sodium channels

Author keywords

Marine neurotoxins; Sodium channel receptor sites; Voltage gated sodium channel

Indexed keywords

ACONITINE; ANTICONVULSIVE AGENT; ANTIDEPRESSANT AGENT; ANTILLATOXIN; BATRACHOTOXIN; BREVETOXIN; CHLORPHENOTANE; CIGUATOXIN; CONOTOXIN; GRAYANOTOXIN; JAMAICAMIDE; KALKITOXIN; LIPOPEPTIDE; LOCAL ANESTHETIC AGENT; MARINE TOXIN; PYRETHROID; SAXITOXIN; SCORPION VENOM; SEA ANEMONE TOXIN; TETRODOTOXIN; UNCLASSIFIED DRUG; VERATRIDINE; VOLTAGE GATED SODIUM CHANNEL;

EID: 33646764233     PISSN: 16603397     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md403157     Document Type: Review
Times cited : (62)

References (171)
  • 1
    • 0642377359 scopus 로고    scopus 로고
    • Drugs from the sea: Conotoxins as drug leads for neuropathic pain and other neurological conditions
    • 37 refs
    • Alonso, D.; Khalil, Z.; Satkunanthan, N.; Livett, B.G. Drugs from the sea: conotoxins as drug leads for neuropathic pain and other neurological conditions. [Review] [37 refs]. Mini-Rev. in Med. Chem. 2003, 3, 785-787.
    • (2003) Mini-Rev. in Med. Chem. , vol.3 , pp. 785-787
    • Alonso, D.1    Khalil, Z.2    Satkunanthan, N.3    Livett, B.G.4
  • 2
    • 0024544737 scopus 로고
    • Brevetoxins: Unique polyether dinoflagellate toxins
    • 56 refs
    • Baden, D.G. Brevetoxins: unique polyether dinoflagellate toxins. [Review] [56 refs]. FASEB J. 1989, 3, 1807-1817.
    • (1989) FASEB J. , vol.3 , pp. 1807-1817
    • Baden, D.G.1
  • 3
    • 19044370182 scopus 로고    scopus 로고
    • Natural and derivative brevetoxins: Historical background, multiplicity, and effects
    • 42 refs
    • Baden, D.G.; Bourdelais, A.J.; Jacocks, H.; Michelliza, S.; Naar, J. Natural and derivative brevetoxins: historical background, multiplicity, and effects. [Review] [42 refs]. Environ. Health Persp. 2005, 113, 621-625.
    • (2005) Environ. Health Persp. , vol.113 , pp. 621-625
    • Baden, D.G.1    Bourdelais, A.J.2    Jacocks, H.3    Michelliza, S.4    Naar, J.5
  • 4
    • 0020025693 scopus 로고
    • Toxicity of two toxins from the Florida red tide marine dinoflagellate, Ptychodiscus brevis
    • Baden, D.G. and Mende, T.J. Toxicity of two toxins from the Florida red tide marine dinoflagellate, Ptychodiscus brevis. Toxicon 1982, 20, 457-461.
    • (1982) Toxicon , vol.20 , pp. 457-461
    • Baden, D.G.1    Mende, T.J.2
  • 6
    • 0031584274 scopus 로고    scopus 로고
    • Structure of neurotoxin B-IV from the marine worm Cerebratulus lacteus: A helical hairpin cross-linked by disulphide bonding
    • Barnham, K.J.; Dyke, T.R.; Kem, W.R.; Norton, R.S. Structure of neurotoxin B-IV from the marine worm Cerebratulus lacteus: a helical hairpin cross-linked by disulphide bonding. J. Mol. Biol. 1997, 268, 886-902.
    • (1997) J. Mol. Biol. , vol.268 , pp. 886-902
    • Barnham, K.J.1    Dyke, T.R.2    Kem, W.R.3    Norton, R.S.4
  • 7
    • 0022655450 scopus 로고
    • Effects of ciguatoxin on current and voltage clamped frog myelinated nerve fibre
    • Benoit, E.; Legrand, A.M.; Dubois, J.M. Effects of ciguatoxin on current and voltage clamped frog myelinated nerve fibre. Toxicon 1986, 24, 357-364.
    • (1986) Toxicon , vol.24 , pp. 357-364
    • Benoit, E.1    Legrand, A.M.2    Dubois, J.M.3
  • 9
    • 0033231630 scopus 로고    scopus 로고
    • Antillatoxin and kalkitoxin, ichthyotoxins from the tropical cyanobacterium Lyngbya majuscula, induce distinct temporal patterns 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 patterns of NMDA receptor-mediated neurotoxicity. Toxicon 1999, 37, 1645-1648.
    • (1999) Toxicon , vol.37 , pp. 1645-1648
    • Berman, F.W.1    Gerwick, W.H.2    Murray, T.F.3
  • 11
    • 3042681285 scopus 로고    scopus 로고
    • Brominated pyrrole alkaloids from marine Agelas sponges reduce depolarization-induced cellular calcium elevation
    • Bickmeyer, U.; Drechsler, C.; Kock, M.; Assmann, M. Brominated pyrrole alkaloids from marine Agelas sponges reduce depolarization-induced cellular calcium elevation. Toxicon 2004, 44, 45-51.
    • (2004) Toxicon , vol.44 , pp. 45-51
    • Bickmeyer, U.1    Drechsler, C.2    Kock, M.3    Assmann, M.4
  • 13
    • 0019776937 scopus 로고
    • Structure and action of heteronemertine polypeptide toxins. Amino acid sequence of Cerebratulus lacteus toxin B-II and revised structure of toxin B-IV
    • Blumenthal, K.M.; Keim, P.S.; Heinrikson, R.L.; Kem, W.R. Structure and action of heteronemertine polypeptide toxins. Amino acid sequence of Cerebratulus lacteus toxin B-II and revised structure of toxin B-IV. J. Biol. Chem. 1981, 256, 9063-9067.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9063-9067
    • Blumenthal, K.M.1    Keim, P.S.2    Heinrikson, R.L.3    Kem, W.R.4
  • 14
    • 0017163091 scopus 로고
    • Structure and action of heteronemertine polypeptide toxins. Primary structure of Cerebratulus lacteus toxin B-IV
    • Blumenthal, K.M. and Kem, W.R. Structure and action of heteronemertine polypeptide toxins. Primary structure of Cerebratulus lacteus toxin B-IV. J. Biol. Chem. 1976, 251, 6025-6029.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6025-6029
    • Blumenthal, K.M.1    Kem, W.R.2
  • 16
    • 0038358133 scopus 로고    scopus 로고
    • Type B brevetoxins show tissue selectivity for voltage-gated sodium channels: Comparison of brain, skeletal muscle and cardiac sodium channels
    • Bottein Dechraoui, M.Y. and Ramsdell, J.S. Type B brevetoxins show tissue selectivity for voltage-gated sodium channels: comparison of brain, skeletal muscle and cardiac sodium channels. Toxicon 2003, 41, 919-927.
    • (2003) Toxicon , vol.41 , pp. 919-927
    • Bottein Dechraoui, M.Y.1    Ramsdell, J.S.2
  • 21
    • 0018747959 scopus 로고
    • Seaweed dermatitis: Structure of lyngbyatoxin A
    • Cardellina, J.H.; Marner, F.J.; Moore, R.E. Seaweed dermatitis: structure of lyngbyatoxin A. Science 1979, 204, 193-195.
    • (1979) Science , vol.204 , pp. 193-195
    • Cardellina, J.H.1    Marner, F.J.2    Moore, R.E.3
  • 22
    • 0024280869 scopus 로고
    • Structure and function of voltage-sensitive ion channels
    • Catterall, W.A. Structure and function of voltage-sensitive ion channels. Science 1988, 242, 50-61.
    • (1988) Science , vol.242 , pp. 50-61
    • Catterall, W.A.1
  • 23
    • 0027930590 scopus 로고
    • Molecular properties of a superfamily of plasma-membrane cation channels
    • Catterall, W.A. Molecular properties of a superfamily of plasma-membrane cation channels. Curr. Opin. Cell Biol. 1994, 6, 607-615.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 607-615
    • Catterall, W.A.1
  • 24
    • 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
  • 25
    • 0036134038 scopus 로고    scopus 로고
    • Molecular mechanisms of gating and drug block of sodium channels
    • Catterall, W.A. Molecular mechanisms of gating and drug block of sodium channels. Novartis Found. Symp. 2002, 241, 206-218.
    • (2002) Novartis Found. Symp. , vol.241 , pp. 206-218
    • Catterall, W.A.1
  • 26
    • 0021824172 scopus 로고
    • Interaction of brevetoxin A with a new receptor site on the sodium channel
    • Catterall, W.A. and Gainer, M. Interaction of brevetoxin A with a new receptor site on the sodium channel. Toxicon 1985, 23, 497-504.
    • (1985) Toxicon , vol.23 , pp. 497-504
    • Catterall, W.A.1    Gainer, M.2
  • 27
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • 111 refs
    • Cestele, S. and Catterall, W.A. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. [Review] [111 refs]. Biochimie 2000, 82, 883-892.
    • (2000) Biochimie , vol.82 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 28
    • 0031808799 scopus 로고    scopus 로고
    • Extrapore residues of the S5-S6 loop of domain 2 of the voltage-gated skeletal muscle sodium channel (rSkM1) contribute to the μ-conotoxin GIIIA binding site
    • Chahine, M.; Sirois, J.; Marcotte, P.; Chen, L.-Q.; Kallen, R.G. Extrapore residues of the S5-S6 loop of domain 2 of the voltage-gated skeletal muscle sodium channel (rSkM1) contribute to the μ-conotoxin GIIIA binding site. Biophys. J. 1998, 75, 236-246.
    • (1998) Biophys. J. , vol.75 , pp. 236-246
    • Chahine, M.1    Sirois, J.2    Marcotte, P.3    Chen, L.-Q.4    Kallen, R.G.5
  • 29
    • 0035997028 scopus 로고    scopus 로고
    • Energetic localization of saxitoxin in its channel binding site
    • Choudhary, G.; Shang, L.; Li, X.; Dudley, S.C., Jr. Energetic localization of saxitoxin in its channel binding site. Biophys. J. 2002, 83, 912-919.
    • (2002) Biophys. J. , vol.83 , pp. 912-919
    • Choudhary, G.1    Shang, L.2    Li, X.3    Dudley Jr., S.C.4
  • 30
    • 12244288289 scopus 로고    scopus 로고
    • Interactions of the C-11 hydroxyl of tetrodotoxin with the sodium channel outer vestibule
    • Choudhary, G.; Yotsu-Yamashita, M.; Shang, L.; Yasumoto, T.; Dudley, S.C., Jr. Interactions of the C-11 hydroxyl of tetrodotoxin with the sodium channel outer vestibule. Biophys. J. 2003, 84, 287-294.
    • (2003) Biophys. J. , vol.84 , pp. 287-294
    • Choudhary, G.1    Yotsu-Yamashita, M.2    Shang, L.3    Yasumoto, T.4    Dudley Jr., S.C.5
  • 31
    • 1242321357 scopus 로고    scopus 로고
    • Bloom inside the bloom: Intracellular bacteria multiplication within toxic dinoflagellates
    • Córdova, J.L.; Escudero, C.; Bustamante, J. Bloom inside the bloom: intracellular bacteria multiplication within toxic dinoflagellates. Revista de Biologia Marina y Oceanografia 2003, 38, 57-67.
    • (2003) Revista de Biologia Marina Y Oceanografia , vol.38 , pp. 57-67
    • Córdova, J.L.1    Escudero, C.2    Bustamante, J.3
  • 34
    • 2942554865 scopus 로고    scopus 로고
    • Structures of muO-conotoxins from Conus marmoreus. Inhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons
    • Daly, N.L.; Ekberg, J.A.; Thomas, L.; Adams, D.J.; Lewis, R.J.; Craik, D.J. Structures of muO-conotoxins from Conus marmoreus. Inhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons. J. Biol. Chem. 2004, 279, 25774-25782.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25774-25782
    • Daly, N.L.1    Ekberg, J.A.2    Thomas, L.3    Adams, D.J.4    Lewis, R.J.5    Craik, D.J.6
  • 35
    • 0033661482 scopus 로고    scopus 로고
    • Structure, function and pharmacology of voltage-gated sodium channels
    • 288 refs
    • Denac, H.; Mevissen, M.; Scholtysik, G. Structure, function and pharmacology of voltage-gated sodium channels. [Review] [288 refs]. Naunyn-Schmiedebergs Arch. Pharmacol. 2000, 362, 453-479.
    • (2000) Naunyn-Schmiedebergs Arch. Pharmacol. , vol.362 , pp. 453-479
    • Denac, H.1    Mevissen, M.2    Scholtysik, G.3
  • 36
    • 11144285533 scopus 로고    scopus 로고
    • Brevetoxin augments NMDA receptor signaling in murine neocortical neurons
    • Dravid, S.M.; Baden, D.G.; Murray, T.F. Brevetoxin augments NMDA receptor signaling in murine neocortical neurons. Brain Res. 2005, 1031, 30-38.
    • (2005) Brain Res. , vol.1031 , pp. 30-38
    • Dravid, S.M.1    Baden, D.G.2    Murray, T.F.3
  • 38
    • 3042551455 scopus 로고    scopus 로고
    • Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula
    • Edwards, D.J.; Marquez, B.L.; Nogle, L.M.; McPhail, K.; Goeger, D.E.; Roberts, M.A.; Gerwick, W.H. Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula.[see comment]. Chem. & Biol. 2004, 11, 817-833.
    • (2004) Chem. & Biol. , vol.11 , pp. 817-833
    • Edwards, D.J.1    Marquez, B.L.2    Nogle, L.M.3    McPhail, K.4    Goeger, D.E.5    Roberts, M.A.6    Gerwick, W.H.7
  • 39
    • 0021783184 scopus 로고
    • Introduction to symposium - Brevetoxins: Chemistry and pharmacology of 'red tide' toxins from Ptychodiscus brevis (formerly Gymnodinium breve)
    • Ellis, S. Introduction to symposium - brevetoxins: chemistry and pharmacology of 'red tide' toxins from Ptychodiscus brevis (formerly Gymnodinium breve). Toxicon 1985, 23, 469-472.
    • (1985) Toxicon , vol.23 , pp. 469-472
    • Ellis, S.1
  • 40
    • 0017644703 scopus 로고
    • The pharmacological actions on guinea-pig ileum of crude venoms from the marine gastropods Conus striatus and Conus magus
    • Endean, R.; Gyr, P.; Surridge, J. The pharmacological actions on guinea-pig ileum of crude venoms from the marine gastropods Conus striatus and Conus magus. Toxicon 1977, 15, 327-337.
    • (1977) Toxicon , vol.15 , pp. 327-337
    • Endean, R.1    Gyr, P.2    Surridge, J.3
  • 41
    • 0018338606 scopus 로고
    • The effects of crude venoms of Conus magus and Conus striatus on the contractile response and electrical activity of guinea-pig cardiac musculature
    • Endean, R.; Gyr, P.; Surridge, J. The effects of crude venoms of Conus magus and Conus striatus on the contractile response and electrical activity of guinea-pig cardiac musculature. Toxicon 1979, 17, 381-395.
    • (1979) Toxicon , vol.17 , pp. 381-395
    • Endean, R.1    Gyr, P.2    Surridge, J.3
  • 42
    • 0017682296 scopus 로고
    • Some effects of crude venom from the cones Conus striatus and Conus magus on isolated guinea-pig atria
    • Endean, R.; Surridge, J.; Gyr, P. Some effects of crude venom from the cones Conus striatus and Conus magus on isolated guinea-pig atria. Toxicon 1977, 15, 369-374.
    • (1977) Toxicon , vol.15 , pp. 369-374
    • Endean, R.1    Surridge, J.2    Gyr, P.3
  • 43
    • 0017113846 scopus 로고
    • Some effects on muscle and nerve of crude venom from the gastropod Conus striatus
    • Endean, R.; Williams, H.; Gyr, P.; Surridge, J. Some effects on muscle and nerve of crude venom from the gastropod Conus striatus. Toxicon 1976, 14, 267-274.
    • (1976) Toxicon , vol.14 , pp. 267-274
    • Endean, R.1    Williams, H.2    Gyr, P.3    Surridge, J.4
  • 46
    • 0028049479 scopus 로고
    • A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in molluscs and acts as an antagonist in rat brain
    • Fainzilber, M.; Kofman, O.; Zlotkin, E.; Gordon, D. A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in molluscs and acts as an antagonist in rat brain. J. Biol. Chem. 1994, 269, 2574-2580.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2574-2580
    • Fainzilber, M.1    Kofman, O.2    Zlotkin, E.3    Gordon, D.4
  • 48
    • 0029051186 scopus 로고
    • New sodium channel-blocking conotoxins also affect calcium currents in Lymnaea neurons
    • Fainzilber, M.; van der, S.R.; Lodder, J.C.; Li, K.W.; Geraerts, W.P.; Kits, K.S. New sodium channel-blocking conotoxins also affect calcium currents in Lymnaea neurons. Biochemistry 1995, 34, 5364-5371.
    • (1995) Biochemistry , vol.34 , pp. 5364-5371
    • Fainzilber, M.1    Van Der, S.R.2    Lodder, J.C.3    Li, K.W.4    Geraerts, W.P.5    Kits, K.S.6
  • 49
    • 0033118848 scopus 로고    scopus 로고
    • Marine natural products
    • Faulkner, D.J. Marine natural products. Nat. Prod. Rep. 1999, 16, 155-198.
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 155-198
    • Faulkner, D.J.1
  • 50
    • 0036007872 scopus 로고    scopus 로고
    • Marine natural products
    • Faulkner, D.J. Marine natural products. Nat. Prod. Rep. 2002, 19, 1-48.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 1-48
    • Faulkner, D.J.1
  • 52
    • 9144242506 scopus 로고    scopus 로고
    • Sodium channel toxins - Receptor targeting and therapeutic potential
    • 85 refs
    • French, R.J. and Terlau, H. Sodium channel toxins - receptor targeting and therapeutic potential. [Review] [85 refs]. Curr. Med. Chem. 2004, 11, 3053-3064.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 3053-3064
    • French, R.J.1    Terlau, H.2
  • 53
    • 0035206447 scopus 로고    scopus 로고
    • Effect of sea anemone toxin anthopleurin-Q on sodium current in guinea pig ventricular myocytes
    • Fu, L.Y.; Li, Y.; Cheng, L.; Zhou, H.Y.; Yao, W.X.; Xia, G.J.; Jiang, M.X. Effect of sea anemone toxin anthopleurin-Q on sodium current in guinea pig ventricular myocytes. Acta Pharmacol. Sinica 2001, 22, 1107-1112.
    • (2001) Acta Pharmacol. Sinica , vol.22 , pp. 1107-1112
    • Fu, L.Y.1    Li, Y.2    Cheng, L.3    Zhou, H.Y.4    Yao, W.X.5    Xia, G.J.6    Jiang, M.X.7
  • 54
    • 0018291936 scopus 로고
    • Effects of Goniopora toxin, a polypeptide isolated from coral, on electromechanical properties of rabbit myocardium
    • Fujiwara, M.; Muramatsu, I.; Hidaka, H.; Ikushima, S.; Ashida, K. Effects of Goniopora toxin, a polypeptide isolated from coral, on electromechanical properties of rabbit myocardium. J. Pharmacol. Exp. Ther. 1979, 210, 153-157.
    • (1979) J. Pharmacol. Exp. Ther. , vol.210 , pp. 153-157
    • Fujiwara, M.1    Muramatsu, I.2    Hidaka, H.3    Ikushima, S.4    Ashida, K.5
  • 55
    • 0031032755 scopus 로고    scopus 로고
    • Evidence for production of paralytic shellfish toxins by bacteria associated with Alexandrium spp. (Dinophyta) in culture
    • Gallacher, S.; Flynn, K.J.; Franco, J.M.; Brueggemann, E.E.; Hines, H.B. Evidence for production of paralytic shellfish toxins by bacteria associated with Alexandrium spp. (Dinophyta) in culture. Appl. Env. Microbiol. 1997, 63, 239-245.
    • (1997) Appl. Env. Microbiol. , vol.63 , pp. 239-245
    • Gallacher, S.1    Flynn, K.J.2    Franco, J.M.3    Brueggemann, E.E.4    Hines, H.B.5
  • 56
    • 0001685110 scopus 로고
    • Chemical variation in the tropical seaweed Stypopodium zonale (dictyotaceae)
    • Gerwick, W.H.; Fenical, W.; Norris, J.N. Chemical variation in the tropical seaweed Stypopodium zonale (dictyotaceae). Phytochemistry 1985, 24, 1279-1283.
    • (1985) Phytochemistry , vol.24 , pp. 1279-1283
    • Gerwick, W.H.1    Fenical, W.2    Norris, J.N.3
  • 57
    • 0022470918 scopus 로고
    • Mechanism of action of a polypeptide neurotoxin from the coral Goniopora on sodium channels in mouse neuroblastoma cells
    • Gonoi, T.; Ashida, K.; Feller, D.; Schmidt, J.; Fujiwara, M.; Catterall, W.A. Mechanism of action of a polypeptide neurotoxin from the coral Goniopora on sodium channels in mouse neuroblastoma cells. Mol. Pharmacol. 1986, 29, 347-354.
    • (1986) Mol. Pharmacol. , vol.29 , pp. 347-354
    • Gonoi, T.1    Ashida, K.2    Feller, D.3    Schmidt, J.4    Fujiwara, M.5    Catterall, W.A.6
  • 58
    • 0023101235 scopus 로고
    • Gating of Na channels. Inactivation modifiers discriminate among models
    • Gonoi, T. and Hille, B. Gating of Na channels. Inactivation modifiers discriminate among models. J. Gen. Physiol. 1987, 89, 253-274.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 253-274
    • Gonoi, T.1    Hille, B.2
  • 59
    • 0023499474 scopus 로고
    • Actions of a polypeptide toxin from the marine snail Conus striatus on voltage-sensitive sodium channels
    • Gonoi, T.; Ohizumi, Y.; Kobayashi, J.; Nakamura, H.; Catterall, W.A. Actions of a polypeptide toxin from the marine snail Conus striatus on voltage-sensitive sodium channels. Molecular Pharmacology 1987, 32, 691-698.
    • (1987) Molecular Pharmacology , vol.32 , pp. 691-698
    • Gonoi, T.1    Ohizumi, Y.2    Kobayashi, J.3    Nakamura, H.4    Catterall, W.A.5
  • 60
    • 0008941662 scopus 로고
    • Screening of toxic corals and isolation of a toxic polypeptide from Goniopora spp.
    • Hashimoto, Y. and Ashida, K. Screening of toxic corals and isolation of a toxic polypeptide from Goniopora spp. Pub. the Seto Marine Biol. Lab. 1973, 20, 703-711.
    • (1973) Pub. the Seto Marine Biol. Lab. , vol.20 , pp. 703-711
    • Hashimoto, Y.1    Ashida, K.2
  • 61
    • 0028922707 scopus 로고
    • Alterations of voltage-activated sodium current by a novel conotoxin from the venom of Conus gloriamaris
    • Hasson, A.; Shon, K.J.; Olivera, B.M.; Spira, M.E. Alterations of voltage-activated sodium current by a novel conotoxin from the venom of Conus gloriamaris. J. Neurophysiol. 1995, 73, 1295-1301.
    • (1995) J. Neurophysiol. , vol.73 , pp. 1295-1301
    • Hasson, A.1    Shon, K.J.2    Olivera, B.M.3    Spira, M.E.4
  • 62
    • 0033863552 scopus 로고    scopus 로고
    • Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure
    • Hill, J.M.; Alewood, P.F.; Craik, D.J. Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure. Eur. J. Biochem. 2000, 267, 4649-4657.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4649-4657
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 63
    • 0015357133 scopus 로고
    • The permeability of the sodium channel to metal cations in myelinated nerve
    • Hille, B. The permeability of the sodium channel to metal cations in myelinated nerve. J. Gen. Physiol. 1972, 59, 637-658.
    • (1972) J. Gen. Physiol. , vol.59 , pp. 637-658
    • Hille, B.1
  • 66
    • 0037401410 scopus 로고    scopus 로고
    • Occurrence of type 3 sodium channel peptide toxins in two species of sea anemones (Dofleinia armata and Entacmaea ramsayi)
    • Honma, T.; Iso, T.; Ishida, M.; Nagashima, Y.; Shiomi, K. Occurrence of type 3 sodium channel peptide toxins in two species of sea anemones (Dofleinia armata and Entacmaea ramsayi). Toxicon 2003, 41, 637-639.
    • (2003) Toxicon , vol.41 , pp. 637-639
    • Honma, T.1    Iso, T.2    Ishida, M.3    Nagashima, Y.4    Shiomi, K.5
  • 67
    • 0025734190 scopus 로고
    • Mutagenesis of Cerebratulus lacteus neurotoxin B-IV identifies NH2-terminal sequences important for biological activity
    • Howell, M.L. and Blumenthal, K.M. Mutagenesis of Cerebratulus lacteus neurotoxin B-IV identifies NH2-terminal sequences important for biological activity. J. Biol. Chem. 1991, 266, 12884-12888.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12884-12888
    • Howell, M.L.1    Blumenthal, K.M.2
  • 70
    • 0035139342 scopus 로고    scopus 로고
    • Sodium channel β subunits: Anything but auxiliary
    • Isom, L.L. Sodium channel β subunits: anything but auxiliary. Neuroscientist 2001, 7(1), 42-54.
    • (2001) Neuroscientist , vol.7 , Issue.1 , pp. 42-54
    • Isom, L.L.1
  • 71
    • 0028263694 scopus 로고
    • Auxiliary subunits of voltage-gated ion channels
    • Isom, L.L.; De Jongh, K.S.; Catterall, W.A. Auxiliary subunits of voltage-gated ion channels. Neuron 1994, 12, 1183-1194.
    • (1994) Neuron , vol.12 , pp. 1183-1194
    • Isom, L.L.1    De Jongh, K.S.2    Catterall, W.A.3
  • 72
    • 0031909499 scopus 로고    scopus 로고
    • Brevetoxin-3 (PbTx-3) and its derivatives modulate single tetrodotoxin-sensitive sodium channels in rat sensory neurons
    • Jeglitsch, G.; Rein, K.; Baden, D.G.; Adams, D.J. Brevetoxin-3 (PbTx-3) and its derivatives modulate single tetrodotoxin-sensitive sodium channels in rat sensory neurons. J. Pharmacol. Exp. Ther. 1998, 284, 516-525.
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 516-525
    • Jeglitsch, G.1    Rein, K.2    Baden, D.G.3    Adams, D.J.4
  • 74
    • 0017115933 scopus 로고
    • Purification and characterization of a new family of polypeptide neurotoxins from the heteronemertine Cerebratulus lacteus (Leidy)
    • Kem, W.R. Purification and characterization of a new family of polypeptide neurotoxins from the heteronemertine Cerebratulus lacteus (Leidy). J. Biol. Chem. 1976, 251, 4184-4192.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4184-4192
    • Kem, W.R.1
  • 75
    • 0024973385 scopus 로고
    • Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus
    • Kem, W.R.; Parten, B.; Pennington, M.W.; Price, D.A.; Dunn, B.M. Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus. Biochemistry 1989, 28, 3483-3489.
    • (1989) Biochemistry , vol.28 , pp. 3483-3489
    • Kem, W.R.1    Parten, B.2    Pennington, M.W.3    Price, D.A.4    Dunn, B.M.5
  • 76
    • 0020418529 scopus 로고
    • Isolation of a cardiotonic glycoprotein, striatoxin, from the venom of the marine snail Conus Striatus
    • Kobayashi, J.; Nakamura, H.; Hirata, Y.; Ohizumi, Y. Isolation of a cardiotonic glycoprotein, striatoxin, from the venom of the marine snail Conus Striatus. Biochem. Biophys. Res. Commun. 1982, 105, 1389-1395.
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 1389-1395
    • Kobayashi, J.1    Nakamura, H.2    Hirata, Y.3    Ohizumi, Y.4
  • 77
    • 0037184042 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the sodium channel agonist/antagonist delta-conotoxin TxVIA
    • Kohno, T.; Sasaki, T.; Kobayashi, K.; Fainzilber, M.; Sato, K. Three-dimensional solution structure of the sodium channel agonist/antagonist delta-conotoxin TxVIA. J. Biol. Chem. 2002, 277, 36387-36391.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36387-36391
    • Kohno, T.1    Sasaki, T.2    Kobayashi, K.3    Fainzilber, M.4    Sato, K.5
  • 78
    • 14244264690 scopus 로고    scopus 로고
    • Pharmacological effects of the marine toxins, brevetoxin and saxitoxin, on murine frontal cortex neuronal networks
    • Kulagina, N.V.; O'shaughnessy, T.J.; Ma, W.; Ramsdell, J.S.; Pancrazio, J.J. Pharmacological effects of the marine toxins, brevetoxin and saxitoxin, on murine frontal cortex neuronal networks. Toxicon 2004, 44, 669-676.
    • (2004) Toxicon , vol.44 , pp. 669-676
    • Kulagina, N.V.1    O'shaughnessy, T.J.2    Ma, W.3    Ramsdell, J.S.4    Pancrazio, J.J.5
  • 79
    • 0034332886 scopus 로고    scopus 로고
    • Ciguatera: Recent advances but the risk remains
    • Lehane, L. and Lewis, R.J. Ciguatera: recent advances but the risk remains. Int. J. Food Microbiol. 2000, 61, 91-125.
    • (2000) Int. J. Food Microbiol. , vol.61 , pp. 91-125
    • Lehane, L.1    Lewis, R.J.2
  • 80
    • 21844466444 scopus 로고    scopus 로고
    • Molecular interaction of delta-conotoxins with voltage-gated sodium channels
    • Leipold, E.; Hansel, A.; Olivera, B.M.; Terlau, H.; Heinemann, S.H. Molecular interaction of delta-conotoxins with voltage-gated sodium channels. FEBS Lett. 2005, 579, 3881-3884.
    • (2005) FEBS Lett. , vol.579 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 81
    • 22544467754 scopus 로고    scopus 로고
    • The neurotoxic lipopeptide kalkitoxin interacts with voltage-sensitive sodium channels in cerebellar granule neurons
    • LePage, K.T.; Goeger, D.; Yokokawa, F.; Asano, T.; Shioiri, T.; Gerwick, W.H.; Murray, T.F. The neurotoxic lipopeptide kalkitoxin interacts with voltage-sensitive sodium channels in cerebellar granule neurons. Toxicol. Lett. 2005, 158, 133-139.
    • (2005) Toxicol. Lett. , vol.158 , pp. 133-139
    • LePage, K.T.1    Goeger, D.2    Yokokawa, F.3    Asano, T.4    Shioiri, T.5    Gerwick, W.H.6    Murray, T.F.7
  • 82
    • 0026533770 scopus 로고
    • Ciguatoxins are potent ichthyotoxins
    • Lewis, R.J. Ciguatoxins are potent ichthyotoxins. Toxicon 1992, 30, 207-211.
    • (1992) Toxicon , vol.30 , pp. 207-211
    • Lewis, R.J.1
  • 83
    • 0035239230 scopus 로고    scopus 로고
    • The changing face of ciguatera
    • [Review] [64 refs]
    • Lewis, R.J. The changing face of ciguatera. [Review] [64 refs]. Toxicon 2001, 39, 97-106.
    • (2001) Toxicon , vol.39 , pp. 97-106
    • Lewis, R.J.1
  • 84
    • 0035815713 scopus 로고    scopus 로고
    • Clockwise domain arrangement of the sodium channel revealed by μ-conotoxin (GIIIA) docking orientation
    • Li, R.A.; Ennis, I.L.; French, R.J.; Dudley, S.C., Jr.; Tomaselli, G.F.; Marbán, E. Clockwise domain arrangement of the sodium channel revealed by μ-conotoxin (GIIIA) docking orientation. J. Biol. Chem. 2001, 276(14), 11072-11077.
    • (2001) J. Biol. Chem. , vol.276 , Issue.14 , pp. 11072-11077
    • Li, R.A.1    Ennis, I.L.2    French, R.J.3    Dudley Jr., S.C.4    Tomaselli, G.F.5    Marbán, E.6
  • 87
    • 0033917903 scopus 로고    scopus 로고
    • Structure-activity relationship of inhibition of fish feeding by sponge-derived and synthetic pyrrole-imidazole alkaloids
    • Lindel, T.; Hoffman, H.; Hochgurtel, M.; Pawlik, J.R. Structure-activity relationship of inhibition of fish feeding by sponge-derived and synthetic pyrrole-imidazole alkaloids. J. Chem. Ecol. 2000, 26.
    • (2000) J. Chem. Ecol. , pp. 26
    • Lindel, T.1    Hoffman, H.2    Hochgurtel, M.3    Pawlik, J.R.4
  • 88
    • 1242337382 scopus 로고    scopus 로고
    • High affinity for the rat brain sodium channel of newly discovered hydroxybenzoate saxitoxin analogues from the dinoflagellate Gymnodinium catenatum
    • Llewellyn, L.; Negri, A.; Quilliam, M. High affinity for the rat brain sodium channel of newly discovered hydroxybenzoate saxitoxin analogues from the dinoflagellate Gymnodinium catenatum. Toxicon 2004, 43, 101-104.
    • (2004) Toxicon , vol.43 , pp. 101-104
    • Llewellyn, L.1    Negri, A.2    Quilliam, M.3
  • 89
    • 0023666436 scopus 로고
    • Ciguatoxin and brevetoxins share a common receptor site on the neuronal voltage-dependent Na+ channel
    • Lombet, A.; Bidard, J.N.; Lazdunski, M. Ciguatoxin and brevetoxins share a common receptor site on the neuronal voltage-dependent Na+ channel. FEBS Lett. 1987, 219, 355-359.
    • (1987) FEBS Lett. , vol.219 , pp. 355-359
    • Lombet, A.1    Bidard, J.N.2    Lazdunski, M.3
  • 92
    • 0141481133 scopus 로고    scopus 로고
    • Reevaluation of production of paralytic shellfish toxin by bacteria associated with dinoflagellates of the Portuguese coast
    • Martins, C.A.; Alvito, P.; Tavares, M.J.; Pereira, P.; Doucette, G.; Franca, S. Reevaluation of production of paralytic shellfish toxin by bacteria associated with dinoflagellates of the Portuguese coast. Appl. Environ. Microbiol. 2003, 69, 5693-5698.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5693-5698
    • Martins, C.A.1    Alvito, P.2    Tavares, M.J.3    Pereira, P.4    Doucette, G.5    Franca, S.6
  • 93
    • 0033558371 scopus 로고    scopus 로고
    • Neurotoxins targetting receptor site 5 of voltage-dependent sodium channels increase the nodal volume of myelinated axons
    • Mattei, C.; Dechraoui, M.Y.; Molgo, J.; Meunier, F.A.; Legrand, A.M.; Benoit, E. Neurotoxins targetting receptor site 5 of voltage-dependent sodium channels increase the nodal volume of myelinated axons. J. Neurosci. Res. 1999, 55, 666-673.
    • (1999) J. Neurosci. Res. , vol.55 , pp. 666-673
    • Mattei, C.1    Dechraoui, M.Y.2    Molgo, J.3    Meunier, F.A.4    Legrand, A.M.5    Benoit, E.6
  • 94
    • 0013816719 scopus 로고
    • The occurrence of a ciguatera-like poison in oysters, clams, and Gymnodinium breve cultures
    • McFarren, E.F.; Silva, F.J.; Tanabe, H.; Wilson, W.B.; Campbell, J.E.; Lewis, K.H. The occurrence of a ciguatera-like poison in oysters, clams, and Gymnodinium breve cultures. Toxicon 1965, 3, 111-123.
    • (1965) Toxicon , vol.3 , pp. 111-123
    • McFarren, E.F.1    Silva, F.J.2    Tanabe, H.3    Wilson, W.B.4    Campbell, J.E.5    Lewis, K.H.6
  • 96
    • 0026043006 scopus 로고
    • The structure of clathrodin, a novel alkaloid isolated from the Caribbean Sea sponge Agelas clathrodes
    • Morales, J.J. and Rodriguez, A.D. The structure of clathrodin, a novel alkaloid isolated from the Caribbean Sea sponge Agelas clathrodes. J. Nat. Prod. 1991, 54, 629-631.
    • (1991) J. Nat. Prod. , vol.54 , pp. 629-631
    • Morales, J.J.1    Rodriguez, A.D.2
  • 97
    • 0017624098 scopus 로고
    • Antileukemia activity in the Osillatoriaceae: Isolation of Debromoaplysiatoxin from Lyngbya
    • Mynderse, J.S.; Moore, R.E.; Kashiwagi, M.; Norton, T.R. Antileukemia activity in the Osillatoriaceae: isolation of Debromoaplysiatoxin from Lyngbya. Science 1977, 196, 538-540.
    • (1977) Science , vol.196 , pp. 538-540
    • Mynderse, J.S.1    Moore, R.E.2    Kashiwagi, M.3    Norton, T.R.4
  • 99
    • 0022098713 scopus 로고
    • Amino acid sequence of a sea anemone toxin from Parasicyonis actinostoloides
    • Nishida, S.; Fujita, S.; Warashina, A.; Satake, M.; Tamiya, N. Amino acid sequence of a sea anemone toxin from Parasicyonis actinostoloides. Eur. J. Biochem. 1985, 150, 171-173.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 171-173
    • Nishida, S.1    Fujita, S.2    Warashina, A.3    Satake, M.4    Tamiya, N.5
  • 100
    • 0024811092 scopus 로고
    • A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II
    • Noda, M.; Suzuki, H.; Numa, S.; Stühmer, W. A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II. FEBS Lett. 1989, 259, 213-216.
    • (1989) FEBS Lett. , vol.259 , pp. 213-216
    • Noda, M.1    Suzuki, H.2    Numa, S.3    Stühmer, W.4
  • 101
    • 0034909167 scopus 로고    scopus 로고
    • Antillatoxin B, a neurotoxic lipopeptide from the marine cyanobacterium Lyngbya majuscula
    • Nogle, L.M.; Okino, T.; Gerwick, W.H. Antillatoxin B, a neurotoxic lipopeptide from the marine cyanobacterium Lyngbya majuscula. J. Nat. Prod. 2001, 64, 983-985.
    • (2001) J. Nat. Prod. , vol.64 , pp. 983-985
    • Nogle, L.M.1    Okino, T.2    Gerwick, W.H.3
  • 102
    • 0025915724 scopus 로고
    • Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel
    • [Review] [127 refs]
    • Norton, R.S. Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel. [Review] [127 refs]. Toxicon 1991, 29, 1051-1084.
    • (1991) Toxicon , vol.29 , pp. 1051-1084
    • Norton, R.S.1
  • 103
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton, R.S. and Pallaghy, P.K. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon 1998, 36, 1573-1583.
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 105
    • 0030729069 scopus 로고    scopus 로고
    • Just Lecture, 1996. Conus venom peptides, receptor and ion channel targets, and drug design: 50 Million years of neuropharmacology
    • Olivera, B.M. E.E. Just Lecture, 1996. Conus venom peptides, receptor and ion channel targets, and drug design: 50 million years of neuropharmacology. Mol. Biol. Cell 1997, 8, 2101-2109.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2101-2109
    • Olivera, B.M.1
  • 106
    • 0036930324 scopus 로고    scopus 로고
    • Conus venom peptides: Reflections from the biology of clades and species
    • Olivera, B.M. Conus venom peptides: reflections from the biology of clades and species. Annu. Rev. Ecol. Syst. 2002, 33, 25-47.
    • (2002) Annu. Rev. Ecol. Syst. , vol.33 , pp. 25-47
    • Olivera, B.M.1
  • 107
    • 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
  • 108
    • 15244350922 scopus 로고    scopus 로고
    • Bacterial Na channels: Progenitors, progeny, or parallel evolution?
    • edited by Kubalski A and Martinac B. American Society for Microbiology
    • Pavlov E, Bladen C, Diao C and French RJ. Bacterial Na channels: progenitors, progeny, or parallel evolution? In: Bacterial ion channels and eukaryotic homologues, edited by Kubalski A and Martinac B. American Society for Microbiology, 2005, p. 191-207.
    • (2005) Bacterial Ion Channels and Eukaryotic Homologues , pp. 191-207
    • Pavlov, E.1    Bladen, C.2    Diao, C.3    French, R.J.4
  • 112
    • 0022969230 scopus 로고
    • Red tide (Ptychodiscus brevis) toxin aerosols: A review
    • Pierce, R.H. Red tide (Ptychodiscus brevis) toxin aerosols: a review. Toxicon 1986, 24, 955-965.
    • (1986) Toxicon , vol.24 , pp. 955-965
    • Pierce, R.H.1
  • 113
    • 0022901519 scopus 로고
    • Brevetoxins, unique activators of voltage-sensitive sodium channels, bind to specific sites in rat brain synaptosomes
    • Poli, M.A.; Mende, T.J.; Baden, D.G. Brevetoxins, unique activators of voltage-sensitive sodium channels, bind to specific sites in rat brain synaptosomes. Mol. Pharmacol. 1986, 30, 129-135.
    • (1986) Mol. Pharmacol. , vol.30 , pp. 129-135
    • Poli, M.A.1    Mende, T.J.2    Baden, D.G.3
  • 115
    • 0022345864 scopus 로고
    • Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B
    • Reimer, N.S.; Yasunobu, C.L.; Yasunobu, K.T.; Norton, T.R. Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B. J. Biol. Chem. 1985, 260, 8690-8693.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8690-8693
    • Reimer, N.S.1    Yasunobu, C.L.2    Yasunobu, K.T.3    Norton, T.R.4
  • 116
    • 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
  • 117
    • 0000796013 scopus 로고
    • Brevetoxin B: Chemical modifications, synaptosome binding, toxicity, and an unexpected conformational effect
    • Rein, K.S.; Lynn, B.; Gawley, R.E.; Baden, D.G. Brevetoxin B: chemical modifications, synaptosome binding, toxicity, and an unexpected conformational effect. J. Org. Chem. 1994, 59, 2107-2113.
    • (1994) J. Org. Chem. , vol.59 , pp. 2107-2113
    • Rein, K.S.1    Lynn, B.2    Gawley, R.E.3    Baden, D.G.4
  • 118
  • 119
    • 0029041114 scopus 로고
    • Effect of alkaloid toxins from tropical marine sponges on membrane sodium currents
    • Rentas, A.L.; Rosa, R.; Rodriguez, A.D.; De Motta, G.E. Effect of alkaloid toxins from tropical marine sponges on membrane sodium currents. Toxicon 1995, 33, 491-497.
    • (1995) Toxicon , vol.33 , pp. 491-497
    • Rentas, A.L.1    Rosa, R.2    Rodriguez, A.D.3    De Motta, G.E.4
  • 126
    • 0030472463 scopus 로고    scopus 로고
    • Pore properties of rat brain II sodium channels mutated in the selectivity filter domain
    • Schlief, T.; Schonherr, R.; Imoto, K.; Heinemann, S.H. Pore properties of rat brain II sodium channels mutated in the selectivity filter domain. Eur. Biophys. J. 1996, 25, 75-91.
    • (1996) Eur. Biophys. J. , vol.25 , pp. 75-91
    • Schlief, T.1    Schonherr, R.2    Imoto, K.3    Heinemann, S.H.4
  • 127
    • 0346850582 scopus 로고    scopus 로고
    • Arg-14 loop of site 3 anemone toxins: Effects of glycine replacement on toxin affinity
    • Seibert, A.L.; Liu, J.; Hanck, D.A.; Blumenthal, K.M. Arg-14 loop of site 3 anemone toxins: effects of glycine replacement on toxin affinity. Biochemistry 2003, 42, 14515-14521.
    • (2003) Biochemistry , vol.42 , pp. 14515-14521
    • Seibert, A.L.1    Liu, J.2    Hanck, D.A.3    Blumenthal, K.M.4
  • 129
    • 0023117471 scopus 로고
    • Allosteric modulation of neurotoxin binding to voltage-sensitive sodium channels by Ptychodiscus brevis toxin 2
    • Sharkey, R.G.; Jover, E.; Couraud, F.; Baden, D.G.; Catterall, W.A. Allosteric modulation of neurotoxin binding to voltage-sensitive sodium channels by Ptychodiscus brevis toxin 2. Mol. Pharmacol. 1987, 31, 273-278.
    • (1987) Mol. Pharmacol. , vol.31 , pp. 273-278
    • Sharkey, R.G.1    Jover, E.2    Couraud, F.3    Baden, D.G.4    Catterall, W.A.5
  • 130
    • 0029826273 scopus 로고    scopus 로고
    • Interactions of delta-conotoxins with alkaloid neurotoxins reveal differences between the silent and effective binding sites on voltage-sensitive sodium channels
    • Shichor, I.; Fainzilber, M.; Pelhate, M.; Malecot, C.O.; Zlotkin, E.; Gordon, D. Interactions of delta-conotoxins with alkaloid neurotoxins reveal differences between the silent and effective binding sites on voltage-sensitive sodium channels. J. Neurochem. 1996, 67, 2451-2460.
    • (1996) J. Neurochem. , vol.67 , pp. 2451-2460
    • Shichor, I.1    Fainzilber, M.2    Pelhate, M.3    Malecot, C.O.4    Zlotkin, E.5    Gordon, D.6
  • 131
    • 0001377493 scopus 로고
    • Microalgal metabolites
    • Shimizu, Y. Microalgal metabolites. Chem. Rev. 1993, 93, 1685-1698.
    • (1993) Chem. Rev. , vol.93 , pp. 1685-1698
    • Shimizu, Y.1
  • 133
    • 0028173320 scopus 로고
    • Delta-conotoxin GmVIA, a novel peptide from the venom of Conus gloriamaris
    • Shon, K.J.; Hasson, A.; Spira, M.E.; Cruz, L.J.; Gray, W.R.; Olivera, B.M. Delta-conotoxin GmVIA, a novel peptide from the venom of Conus gloriamaris. Biochemistry 1994, 33, 11420-11425.
    • (1994) Biochemistry , vol.33 , pp. 11420-11425
    • Shon, K.J.1    Hasson, A.2    Spira, M.E.3    Cruz, L.J.4    Gray, W.R.5    Olivera, B.M.6
  • 135
    • 0035344095 scopus 로고    scopus 로고
    • Biotransformations of paralytic shellfish toxins by bacteria isolated from bivalve molluscs
    • Smith, E.A.; Grant, F.; Ferguson, C.M.; Gallacher, S. Biotransformations of paralytic shellfish toxins by bacteria isolated from bivalve molluscs. Appl. Env. Microbiol. 2001, 67, 2345-2353.
    • (2001) Appl. Env. Microbiol. , vol.67 , pp. 2345-2353
    • Smith, E.A.1    Grant, F.2    Ferguson, C.M.3    Gallacher, S.4
  • 137
    • 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.M.; Potts, J.F.; Agnew, W.S. The μI skeletal muscle sodium channel: mutation E403Q eliminates sensitivity to tetrodotoxin but not to μ-conotoxins GIIIA and GIIIB. J. Membrane Biol. 1994, 137, 1-8.
    • (1994) J. Membrane Biol. , vol.137 , pp. 1-8
    • Stephan, M.M.1    Potts, J.F.2    Agnew, W.S.3
  • 138
    • 0032940658 scopus 로고    scopus 로고
    • Differential actions of pacific ciguatoxin-1 on sodium channel subtypes in mammalian sensory neurons
    • Strachan, L.C.; Lewis, R.J.; Nicholson, G.M. Differential actions of pacific ciguatoxin-1 on sodium channel subtypes in mammalian sensory neurons. J Pharmacol. Exp. Ther. 1999, 288, 379-388.
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 379-388
    • Strachan, L.C.1    Lewis, R.J.2    Nicholson, G.M.3
  • 141
    • 0023153991 scopus 로고
    • Amino acid sequence of two sea anemone toxins from Anthopleura fuscoviridis
    • Sunahara, S.; Muramoto, K.; Tenma, K.; Kamiya, H. Amino acid sequence of two sea anemone toxins from Anthopleura fuscoviridis. Toxicon 1987, 25, 211-219.
    • (1987) Toxicon , vol.25 , pp. 211-219
    • Sunahara, S.1    Muramoto, K.2    Tenma, K.3    Kamiya, H.4
  • 142
    • 0017617014 scopus 로고
    • Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin A
    • Tanaka, M.; Hainu, M.; Yasunobu, K.T.; Norton, T.R. Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin A. Biochemistry 1977, 16, 204-208.
    • (1977) Biochemistry , vol.16 , pp. 204-208
    • Tanaka, M.1    Hainu, M.2    Yasunobu, K.T.3    Norton, T.R.4
  • 144
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • [Review] [196 refs]
    • Terlau, H. and Olivera, B.M. Conus venoms: a rich source of novel ion channel-targeted peptides. [Review] [196 refs]. Physiol. Rev. 2004, 84, 41-68.
    • (2004) Physiol. Rev. , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 145
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • Terlau, H.; Shon, K.J.; Grilley, M.; Stocker, M.; Stuhmer, W.; Olivera, B.M. Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature 1996, 381, 148-151.
    • (1996) Nature , vol.381 , pp. 148-151
    • Terlau, H.1    Shon, K.J.2    Grilley, M.3    Stocker, M.4    Stuhmer, W.5    Olivera, B.M.6
  • 146
    • 0029658417 scopus 로고    scopus 로고
    • μO-conotoxin MrVIA inhibits mammalian sodium channels, but not through site I
    • Terlau, H.; Stocker, M.; Shon, K.-J.; McIntosh, J.M.; Olivera, B.M. μO-conotoxin MrVIA inhibits mammalian sodium channels, but not through site I. J. Neurophysiol. 1996, 76(3), 1423-1429.
    • (1996) J. Neurophysiol. , vol.76 , Issue.3 , pp. 1423-1429
    • Terlau, H.1    Stocker, M.2    Shon, K.-J.3    McIntosh, J.M.4    Olivera, B.M.5
  • 148
    • 0036337692 scopus 로고    scopus 로고
    • Limited selection of sodium channel blocking toxin-producing bacteria from paralytic shellfish toxin-contaminated mussels (Aulacomya ater)
    • Vasquez, M.; Gruttner, C.; Moeller, B.; Moore, E.R. Limited selection of sodium channel blocking toxin-producing bacteria from paralytic shellfish toxin-contaminated mussels (Aulacomya ater). Res. Microbiol. 2002, 153, 333-338.
    • (2002) Res. Microbiol. , vol.153 , pp. 333-338
    • Vasquez, M.1    Gruttner, C.2    Moeller, B.3    Moore, E.R.4
  • 149
    • 0035754168 scopus 로고    scopus 로고
    • Slow inactivation in voltage-gated sodium channels: Molecular substrates and contributions to channelopathies
    • Vilin, Y.Y. and Ruben, P.C. Slow inactivation in voltage-gated sodium channels: molecular substrates and contributions to channelopathies. Cell Biochem. Biophys. 2001, 35, 171-190.
    • (2001) Cell Biochem. Biophys. , vol.35 , pp. 171-190
    • Vilin, Y.Y.1    Ruben, P.C.2
  • 150
    • 2442684336 scopus 로고    scopus 로고
    • NMR solution structures of delta-conotoxin EVIA from Conus ermineus that selectively acts on vertebrate neuronal Na+ channels
    • Volpon, L.; Lamthanh, H.; Barbier, J.; Gilles, N.; Molgo, J.; Menez, A.; Lancelin, J.M. NMR solution structures of delta-conotoxin EVIA from Conus ermineus that selectively acts on vertebrate neuronal Na+ channels. J. Biol. Chem. 2004, 279, 21356-21366.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21356-21366
    • Volpon, L.1    Lamthanh, H.2    Barbier, J.3    Gilles, N.4    Molgo, J.5    Menez, A.6    Lancelin, J.M.7
  • 151
    • 0037290637 scopus 로고    scopus 로고
    • Voltage-gated sodium channels as primary targets of diverse lipid-soluble neurotoxins
    • [Review] [68 refs]
    • Wang, S.Y. and Wang, G.K. Voltage-gated sodium channels as primary targets of diverse lipid-soluble neurotoxins. [Review] [68 refs]. Cell. Signal. 2003, 15, 151-159.
    • (2003) Cell. Signal. , vol.15 , pp. 151-159
    • Wang, S.Y.1    Wang, G.K.2
  • 153
    • 0029982147 scopus 로고    scopus 로고
    • Role of electrostatic interactions in defining the potency of neurotoxin B-IV from Cerebratulus lacteus
    • Wen, P.H. and Blumenthal, K.M. Role of electrostatic interactions in defining the potency of neurotoxin B-IV from Cerebratulus lacteus. J. Biol. Chem. 1996, 271, 29752-29758.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29752-29758
    • Wen, P.H.1    Blumenthal, K.M.2
  • 154
    • 0030786191 scopus 로고    scopus 로고
    • Structure and function of Cerebratulus lacteus neurotoxin B-IV: Tryptophan-30 is critical for function while lysines-18, -19, -29, and -33 are not required
    • Wen, P.H. and Blumenthal, K.M. Structure and function of Cerebratulus lacteus neurotoxin B-IV: tryptophan-30 is critical for function while lysines-18, -19, -29, and -33 are not required. Biochemistry 1997, 36, 13435-13440.
    • (1997) Biochemistry , vol.36 , pp. 13435-13440
    • Wen, P.H.1    Blumenthal, K.M.2
  • 155
    • 0345642813 scopus 로고    scopus 로고
    • A new tyrosine kinase inhibitor from the marine brown alga Stypopodium zonale
    • Wessels, M.; Konig, G.M.; Wright, A.D. A new tyrosine kinase inhibitor from the marine brown alga Stypopodium zonale. J. Nat. Prod. 1999, 62, 927-930.
    • (1999) J. Nat. Prod. , vol.62 , pp. 927-930
    • Wessels, M.1    Konig, G.M.2    Wright, A.D.3
  • 156
    • 0037168454 scopus 로고    scopus 로고
    • Mu-conotoxin SmIIIA, a potent inhibitor of tetrodotoxin-resistant sodium channels in amphibian sympathetic and sensory neurons
    • West, P.J.; Bulaj, G.; Garrett, J.E.; Olivera, B.M.; Yoshikami, D. Mu-conotoxin SmIIIA, a potent inhibitor of tetrodotoxin-resistant sodium channels in amphibian sympathetic and sensory neurons. Biochemistry 2002, 41, 15388-15393.
    • (2002) Biochemistry , vol.41 , pp. 15388-15393
    • West, P.J.1    Bulaj, G.2    Garrett, J.E.3    Olivera, B.M.4    Yoshikami, D.5
  • 157
    • 28044453479 scopus 로고    scopus 로고
    • Effects of delta-conotoxins PVIA and SVIE on sodium channels in the amphibian sympathetic nervous system
    • West, P.J.; Bulaj, G.; Yoshikami, D. Effects of delta-conotoxins PVIA and SVIE on sodium channels in the amphibian sympathetic nervous system. J. Neurophysiol. 2005, 94, 3916-3924.
    • (2005) J. Neurophysiol. , vol.94 , pp. 3916-3924
    • West, P.J.1    Bulaj, G.2    Yoshikami, D.3
  • 158
    • 0024790415 scopus 로고
    • Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy
    • Widmer, H.; Billeter, M.; Wuthrich, K. Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy. Proteins 1989, 6, 357-371.
    • (1989) Proteins , vol.6 , pp. 357-371
    • Widmer, H.1    Billeter, M.2    Wuthrich, K.3
  • 159
    • 0034008867 scopus 로고    scopus 로고
    • The chemical defense ecology of marine unicellular plankton: Constraints, mechanisms, and impacts
    • [Review] [270 refs]
    • Wolfe, G.V. The chemical defense ecology of marine unicellular plankton: constraints, mechanisms, and impacts. [Review] [270 refs]. Biol. Bull. 2000, 198, 225-244.
    • (2000) Biol. Bull. , vol.198 , pp. 225-244
    • Wolfe, G.V.1
  • 161
    • 0018101137 scopus 로고
    • Amino-acid sequence of toxin I from Anemonia sulcata
    • Wunderer, G. and Eulitz, M. Amino-acid sequence of toxin I from Anemonia sulcata. Eur. J. Biochem. 1978, 89, 11-17.
    • (1978) Eur. J. Biochem. , vol.89 , pp. 11-17
    • Wunderer, G.1    Eulitz, M.2
  • 162
    • 0017103673 scopus 로고
    • Amino-acid sequence of a coelenterate toxin: Toxin II from Anemonia sulcata
    • Wunderer, G.; Fritz, H.; Wachter, E.; Machleidt, W. Amino-acid sequence of a coelenterate toxin: toxin II from Anemonia sulcata. Eur. J. Biochem. 1976, 68, 193-198.
    • (1976) Eur. J. Biochem. , vol.68 , pp. 193-198
    • Wunderer, G.1    Fritz, H.2    Wachter, E.3    Machleidt, W.4
  • 163
    • 0023711980 scopus 로고
    • A novel sodium channel inhibitor from Conus geographus: Purification, structure, and pharmacological properties
    • Yanagawa, Y.; Abe, T.; Satake, M.; Odani, S.; Suzuki, J.; Ishikawa, K. A novel sodium channel inhibitor from Conus geographus: purification, structure, and pharmacological properties. Biochemistry 1988, 27, 6256-6262.
    • (1988) Biochemistry , vol.27 , pp. 6256-6262
    • Yanagawa, Y.1    Abe, T.2    Satake, M.3    Odani, S.4    Suzuki, J.5    Ishikawa, K.6
  • 164
    • 1542502091 scopus 로고
    • Marine toxins
    • Yasumoto, T. and murata, M. Marine toxins. Chem. Rev. 1993, 93, 1897-1909.
    • (1993) Chem. Rev. , vol.93 , pp. 1897-1909
    • Yasumoto, T.1    Murata, M.2
  • 165
    • 1842481343 scopus 로고    scopus 로고
    • The structure of zetekitoxin AB, a saxitoxin analog from the Panamanian golden frog Atelopus zeteki: A potent sodium-channel blocker
    • Yotsu-Yamashita, M.; Kim, Y.H.; Dudley, S.C., Jr.; Choudhary, G.; Pfahnl, A.; Oshima, Y.; Daly, J.W. The structure of zetekitoxin AB, a saxitoxin analog from the Panamanian golden frog Atelopus 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 Jr., S.C.3    Choudhary, G.4    Pfahnl, A.5    Oshima, Y.6    Daly, J.W.7
  • 166
    • 0033805192 scopus 로고    scopus 로고
    • The diversity of harmful algal blooms: A challenge for science and management
    • Zingone, A. and Enevoldsen, H.O. The diversity of harmful algal blooms: a challenge for science and management. Ocean & Coastal Management 2000, 43, 725-748.
    • (2000) Ocean & Coastal Management , vol.43 , pp. 725-748
    • Zingone, A.1    Enevoldsen, H.O.2
  • 167
    • 0033017102 scopus 로고    scopus 로고
    • The insect voltage-gated sodium channel as target of insecticides
    • [Review] [73 refs]
    • Zlotkin, E. The insect voltage-gated sodium channel as target of insecticides. [Review] [73 refs]. Ann. Rev. Entomol. 1999, 44, 429-455.
    • (1999) Ann. Rev. Entomol. , vol.44 , pp. 429-455
    • Zlotkin, E.1
  • 168
    • 0024745741 scopus 로고
    • Amino acid sequence of a neurotoxin from the anemone Radianthus macrodactylus
    • Zykova, T.A. and Kozlovskaia, E.P. [Amino acid sequence of a neurotoxin from the anemone Radianthus macrodactylus]. Bioorg. Khim. 1989, 15, 1301-1306.
    • (1989) Bioorg. Khim. , vol.15 , pp. 1301-1306
    • Zykova, T.A.1    Kozlovskaia, E.P.2
  • 169
    • 0024696558 scopus 로고
    • Disulfide bonds in neurotoxin-III from the sea anenome Radianthus macrodactylus
    • Zykova, T.A. and Kozlovskaia, E.P. [Disulfide bonds in neurotoxin-III from the sea anenome Radianthus macrodactylus]. Bioorg. Khim. 1989, 15, 904-907.
    • (1989) Bioorg. Khim. , vol.15 , pp. 904-907
    • Zykova, T.A.1    Kozlovskaia, E.P.2
  • 170
    • 0023820861 scopus 로고
    • Amino acid sequence of neurotoxin II from the sea anemone Radianthus macrodactylus
    • Zykova, T.A.; Kozlovskaia, E.P.; Eliakov, G.B. [Amino acid sequence of neurotoxin II from the sea anemone Radianthus macrodactylus]. Bioorg. Khim. 1988, 14, 878-882.
    • (1988) Bioorg. Khim. , vol.14 , pp. 878-882
    • Zykova, T.A.1    Kozlovskaia, E.P.2    Eliakov, G.B.3
  • 171
    • 0024119895 scopus 로고
    • Amino acid sequence of neurotoxins IV and V from the sea anemone Radianthus macrodactylus
    • Zykova, T.A.; Kozlovskaia, E.P.; Eliakov, G.B. [Amino acid sequence of neurotoxins IV and V from the sea anemone Radianthus macrodactylus]. Bioorg. Khim. 1988, 14, 1489-1494.
    • (1988) Bioorg. Khim. , vol.14 , pp. 1489-1494
    • Zykova, T.A.1    Kozlovskaia, E.P.2    Eliakov, G.B.3


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