메뉴 건너뛰기




Volumn 63, Issue 1, 2013, Pages 165-183

The molecular mystique of tetrodotoxin

Author keywords

Saxitoxin; Sodium channel; Tetrodotoxin

Indexed keywords

11 DEOXYEPITETRODOTOXIN; 4 EPITETRODOTOXIN; 4,9 ANHYDROTETRODOTOXIN; 6 EPITETRODOTOXIN; ACONITINE; AMANTADINE; BATRACHOTOXIN; BREVETOXIN; CHIRIQUITOXIN; CIGUATOXIN; COCAINE; CONOTOXIN; CURARE; DIGITOXIN; GRAYANOTOXIN; GUANIDINIUM TOXIN; LIDOCAINE; MORPHINE; NEUROTOXIN; PROCAINE; SAXITOXIN; SCORPION VENOM; SEA ANEMONE TOXIN; SODIUM CHANNEL NAV1.4; TARANTULA PEPTIDE TOXIN; TETRODOTOXIN; TOXIN; TRITIUM; UNCLASSIFIED DRUG; UNINDEXED DRUG; VERATRIDINE;

EID: 84872419608     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2012.11.026     Document Type: Review
Times cited : (103)

References (183)
  • 1
    • 0031464230 scopus 로고    scopus 로고
    • Tetrodotoxin-blockable calcium currents in rat ventricular myocytes; a third type of cardiac cell sodium current
    • Aggarwal R., Shorofsky S.R., Goldman L., Balke C.W. Tetrodotoxin-blockable calcium currents in rat ventricular myocytes; a third type of cardiac cell sodium current. J. Physiol. (London) 1997, 505(2):353-369.
    • (1997) J. Physiol. (London) , vol.505 , Issue.2 , pp. 353-369
    • Aggarwal, R.1    Shorofsky, S.R.2    Goldman, L.3    Balke, C.W.4
  • 2
    • 0009345298 scopus 로고
    • Purification of the tetrodotoxin-binding component associated with the voltage-sensitive channel from Electrophorus electricus
    • Agnew W.S., Levinson S.R., Brabson J.S., Raftery M.A. Purification of the tetrodotoxin-binding component associated with the voltage-sensitive channel from Electrophorus electricus. 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
  • 3
    • 77949497356 scopus 로고    scopus 로고
    • Total synthesis of (-)-tetrodotoxin from D-glucose: a new route to multi-functionalized cyclitol employing the Ferrier(II) reaction toward (-)-tetrodotoxin
    • Akai S., Seki H., Sugita N., Kogure T., Nishizawa N., Suzuki K., Nakamura Y., Kajhara Y., Yoshimura J., Sato K. Total synthesis of (-)-tetrodotoxin from D-glucose: a new route to multi-functionalized cyclitol employing the Ferrier(II) reaction toward (-)-tetrodotoxin. Bull. Chem. Soc. Jpn. 2010, 83:279-287.
    • (2010) Bull. Chem. Soc. Jpn. , vol.83 , pp. 279-287
    • Akai, S.1    Seki, H.2    Sugita, N.3    Kogure, T.4    Nishizawa, N.5    Suzuki, K.6    Nakamura, Y.7    Kajhara, Y.8    Yoshimura, J.9    Sato, K.10
  • 4
    • 0030041548 scopus 로고    scopus 로고
    • A tetrodotoxin-resistant voltage-gated sodium channel expressed by sensory neurons
    • Akopian A.N., Sivilotti L., Wood J.N. A tetrodotoxin-resistant voltage-gated sodium channel expressed by sensory neurons. Nature 1996, 379:257-262.
    • (1996) Nature , vol.379 , pp. 257-262
    • Akopian, A.N.1    Sivilotti, L.2    Wood, J.N.3
  • 5
    • 0015210117 scopus 로고
    • Batrachotoxin: chemistry and pharmacology
    • Albuquerque E.X., Daly J.W., Witkop B. Batrachotoxin: chemistry and pharmacology. Science 1971, 172:995-1002.
    • (1971) Science , vol.172 , pp. 995-1002
    • Albuquerque, E.X.1    Daly, J.W.2    Witkop, B.3
  • 6
    • 0016735801 scopus 로고
    • Tetrodotoxin-binding to normal and depolarized frog muscle and the conductance of a single sodium channel
    • Almers W., Levinson S.R. Tetrodotoxin-binding to normal and depolarized frog muscle and the conductance of a single sodium channel. J. Physiol. (London) 1975, 247:483-509.
    • (1975) J. Physiol. (London) , vol.247 , pp. 483-509
    • Almers, W.1    Levinson, S.R.2
  • 7
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium derivatives with the potassium channels of giant axons
    • Armstrong C.M. Interaction of tetraethylammonium derivatives with the potassium channels of giant axons. J. Gen. Physiol. 1971, 58:413-437.
    • (1971) J. Gen. Physiol. , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 8
    • 0017144669 scopus 로고
    • Voltage-dependent action of tetrodotoxin in mammalian cardiac muscle
    • Baer M., Best P.M., Reuter H. Voltage-dependent action of tetrodotoxin in mammalian cardiac muscle. Nature 1976, 263:344-345.
    • (1976) Nature , vol.263 , pp. 344-345
    • Baer, M.1    Best, P.M.2    Reuter, H.3
  • 9
    • 0019186072 scopus 로고
    • Purification from rat sarcolemma of the saxitoxin-binding component of the excitable membrane sodium channel
    • Barchi R.L., Cohen S.A., Murphy L.E. Purification from rat sarcolemma of the saxitoxin-binding component of the excitable membrane sodium channel. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:1306-1310.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 1306-1310
    • Barchi, R.L.1    Cohen, S.A.2    Murphy, L.E.3
  • 10
    • 0018652843 scopus 로고
    • Characteristics of saxitoxin binding to the sodium channel of sarcolemma isolated from rat skeletal muscle
    • Barchi R.L., Weigele J.B. Characteristics of saxitoxin binding to the sodium channel of sarcolemma isolated from rat skeletal muscle. J. Physiol. (London) 1979, 295:383-396.
    • (1979) J. Physiol. (London) , vol.295 , pp. 383-396
    • Barchi, R.L.1    Weigele, J.B.2
  • 11
    • 0015457789 scopus 로고
    • Partial characterization of a tetrodotoxin-binding component from nerve membrane
    • Benzer T.I., Raftery M.A. Partial characterization of a tetrodotoxin-binding component from nerve membrane. Proc. Natl. Acad. Sci. U. S. A. 1972, 69:3634-3637.
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 3634-3637
    • Benzer, T.I.1    Raftery, M.A.2
  • 13
    • 0024287403 scopus 로고
    • Voodoo science
    • Booth W. Voodoo science. Science 1988, 240:274-277.
    • (1988) Science , vol.240 , pp. 274-277
    • Booth, W.1
  • 14
    • 0025595532 scopus 로고
    • Tetrodotoxin resistance in garter snakes: an evolutionary response of predators to dangerous prey
    • Brodie E.D., Brodie E.D. Tetrodotoxin resistance in garter snakes: an evolutionary response of predators to dangerous prey. Evolution 1990, 44:651-659.
    • (1990) Evolution , vol.44 , pp. 651-659
    • Brodie, E.D.1    Brodie, E.D.2
  • 16
    • 0014214679 scopus 로고
    • Potency difference between the zwitterion form and the cation forms of tetrodotoxin
    • Camougis G., Takman B.H., Tasse J.R.P. Potency difference between the zwitterion form and the cation forms of tetrodotoxin. Science 1967, 167:1625-1627.
    • (1967) Science , vol.167 , pp. 1625-1627
    • Camougis, G.1    Takman, B.H.2    Tasse, J.R.P.3
  • 18
    • 0023574096 scopus 로고
    • Common modes of drug action on Na+ channels: local anesthetics, antiarrhythmics, and anticonvulsants
    • Catterall W.A. Common modes of drug action on Na+ channels: local anesthetics, antiarrhythmics, and anticonvulsants. Trends Pharmacol. Sci. 1987, 8:57-65.
    • (1987) Trends Pharmacol. Sci. , vol.8 , pp. 57-65
    • Catterall, W.A.1
  • 19
    • 84861716984 scopus 로고    scopus 로고
    • Voltage-gated sodium channels at 60: structure, function, and pathophysiology
    • Catterall W.A. Voltage-gated sodium channels at 60: structure, function, and pathophysiology. J. Physiol. (London) 2012, 590(11):2577-2589.
    • (2012) J. Physiol. (London) , vol.590 , Issue.11 , pp. 2577-2589
    • Catterall, W.A.1
  • 20
    • 80054957679 scopus 로고    scopus 로고
    • The chemical synthesis of tetrodotoxin: an ongoing quest
    • Chau J., Ciufolini M.A. The chemical synthesis of tetrodotoxin: an ongoing quest. Mar. Drugs 2011, 9:2046-2074.
    • (2011) Mar. Drugs , vol.9 , pp. 2046-2074
    • Chau, J.1    Ciufolini, M.A.2
  • 21
    • 79955369100 scopus 로고    scopus 로고
    • On the origins and biosynthesis of tetrodotoxin
    • Chau R., Kalaitzis J.A., Neilan B.A. On the origins and biosynthesis of tetrodotoxin. Aquat. Toxicol. 2011, 104:61-72.
    • (2011) Aquat. Toxicol. , vol.104 , pp. 61-72
    • Chau, R.1    Kalaitzis, J.A.2    Neilan, B.A.3
  • 22
    • 0018987868 scopus 로고
    • Synthesis of new, highly radioactive tetrodotoxin derivatives and their binding properties to the sodium channel
    • Chicheportiche R., Balerna M., Lombet A., Romey G., Lazdunski M. Synthesis of new, highly radioactive tetrodotoxin derivatives and their binding properties to the sodium channel. Eur. J. Biochem. 1980, 104:617-625.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 617-625
    • Chicheportiche, R.1    Balerna, M.2    Lombet, A.3    Romey, G.4    Lazdunski, M.5
  • 23
    • 0019520819 scopus 로고
    • Tetrodotoxin block of sodium channels in rabbit Purkinje fibers: interactions between toxin binding and channel gating
    • Cohen C.J., Bean B.P., Colatsky T.J., Tsien R.W. Tetrodotoxin block of sodium channels in rabbit Purkinje fibers: interactions between toxin binding and channel gating. J. Gen. Physiol. 1981, 78:383-411.
    • (1981) J. Gen. Physiol. , vol.78 , pp. 383-411
    • Cohen, C.J.1    Bean, B.P.2    Colatsky, T.J.3    Tsien, R.W.4
  • 24
    • 0029741451 scopus 로고
    • Use dependence of tetrodotoxin block of sodium channels: a revival of the trapped ion mechanism
    • Conti F., Gheri A., Pusch M., Moran O. Use dependence of tetrodotoxin block of sodium channels: a revival of the trapped ion mechanism. Biophys. J. 1986, 71:1295-1312.
    • (1986) Biophys. J. , vol.71 , pp. 1295-1312
    • Conti, F.1    Gheri, A.2    Pusch, M.3    Moran, O.4
  • 25
    • 4344714713 scopus 로고    scopus 로고
    • Marine toxins and nonmarine toxins: convergence or symbiotic organisms?
    • Daly J.W. Marine toxins and nonmarine toxins: convergence or symbiotic organisms?. J. Nat. Prod. 2004, 67:1211-1215.
    • (2004) J. Nat. Prod. , vol.67 , pp. 1211-1215
    • Daly, J.W.1
  • 27
    • 67849088716 scopus 로고    scopus 로고
    • Frequent occurrence of the tetrodotoxin-bearing horseshoe crab Carcinoscorpius rotundicauda in Vietnam
    • Dao H., Takata Y., Sato S., Fukuyo Y., Kodama M. Frequent occurrence of the tetrodotoxin-bearing horseshoe crab Carcinoscorpius rotundicauda in Vietnam. Fish. Sci. 2009, 75:435-438.
    • (2009) Fish. Sci. , vol.75 , pp. 435-438
    • Dao, H.1    Takata, Y.2    Sato, S.3    Fukuyo, Y.4    Kodama, M.5
  • 28
    • 0010834692 scopus 로고
    • Rapid and reversible block of electrical activity by powerful marine biotoxins
    • Dettbarn W.D., Higman H., Rosenberg P., Nachmansohn D. Rapid and reversible block of electrical activity by powerful marine biotoxins. Science 1960, 132:300-301.
    • (1960) Science , vol.132 , pp. 300-301
    • Dettbarn, W.D.1    Higman, H.2    Rosenberg, P.3    Nachmansohn, D.4
  • 29
    • 0032555278 scopus 로고    scopus 로고
    • NaN, a novel voltage-gated Na channel, is expressed preferentially in peripheral sensory neurons and down-regulated after axotomy
    • Dib-Hajj S.D., Tyrrell L., Black J.A., Waxman S.G. NaN, a novel voltage-gated Na channel, is expressed preferentially in peripheral sensory neurons and down-regulated after axotomy. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:8963-8968.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 8963-8968
    • Dib-Hajj, S.D.1    Tyrrell, L.2    Black, J.A.3    Waxman, S.G.4
  • 31
    • 0025209816 scopus 로고
    • Identification of deep-sea sediment bacteria which produce tetrodotoxin
    • Do H., Kogure K., Simidu U. Identification of deep-sea sediment bacteria which produce tetrodotoxin. Appl. Environ. Microbiol. 1990, 56:1162-1163.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1162-1163
    • Do, H.1    Kogure, K.2    Simidu, U.3
  • 33
    • 0027471751 scopus 로고
    • Divalent cation competition with [3H]saxitoxin binding to tetrodotoxin-resistant and -sensitive sodium channels: a two-site structural model of ion/toxin interaction
    • Doyle D.D., Guo Y., Lustig S.L., Satin J., Rogart R.B., Fozzard H.A. Divalent cation competition with [3H]saxitoxin binding to tetrodotoxin-resistant and -sensitive sodium channels: a two-site structural model of ion/toxin interaction. J. Gen. Physiol. 1993, 101:153-182.
    • (1993) J. Gen. Physiol. , vol.101 , pp. 153-182
    • Doyle, D.D.1    Guo, Y.2    Lustig, S.L.3    Satin, J.4    Rogart, R.B.5    Fozzard, H.A.6
  • 34
    • 34547912273 scopus 로고
    • Paralytic effects of " paralytic shellfish poison" on frog nerve and muscle
    • Evans M.H. Paralytic effects of " paralytic shellfish poison" on frog nerve and muscle. Br. J. Pharmacol. 1964, 22:478-485.
    • (1964) Br. J. Pharmacol. , vol.22 , pp. 478-485
    • Evans, M.H.1
  • 35
    • 0029103341 scopus 로고
    • Specificity for block by saxitoxin and divalent cations at a residue which determines sensitivity of sodium channel subtypes to guanidinium toxins
    • Favre I., Moczydlowski E., Schild L. Specificity for block by saxitoxin and divalent cations at a residue which determines sensitivity of sodium channel subtypes to guanidinium toxins. J. Gen. Physiol. 1995, 106:203-229.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 203-229
    • Favre, I.1    Moczydlowski, E.2    Schild, L.3
  • 36
    • 0029754658 scopus 로고    scopus 로고
    • On the structural basis for ionic selectivity among Na+, K+, and Ca2+ in the voltage-gated sodium channel
    • Favre I., Moczydlowski E., Schild L. On the structural basis for ionic selectivity among Na+, K+, and Ca2+ in the voltage-gated sodium channel. Biophys. J. 1996, 71:3110-3125.
    • (1996) Biophys. J. , vol.71 , pp. 3110-3125
    • Favre, I.1    Moczydlowski, E.2    Schild, L.3
  • 37
    • 0031729725 scopus 로고    scopus 로고
    • Reconstitution of native and cloned channels into planar bilayers
    • Favre I., Sun Y.M., Moczydlowski E. Reconstitution of native and cloned channels into planar bilayers. Meth. Enzymol. 1999, 294:287-305.
    • (1999) Meth. Enzymol. , vol.294 , pp. 287-305
    • Favre, I.1    Sun, Y.M.2    Moczydlowski, E.3
  • 39
    • 77649213717 scopus 로고    scopus 로고
    • The tetrodotoxin binding site is within the outer vestibule of the sodium channel
    • Fozzard H.A., Lipkind G.M. The tetrodotoxin binding site is within the outer vestibule of the sodium channel. Mar. Drugs 2010, 8:219-234.
    • (2010) Mar. Drugs , vol.8 , pp. 219-234
    • Fozzard, H.A.1    Lipkind, G.M.2
  • 40
    • 9144242506 scopus 로고    scopus 로고
    • Sodium channel toxins - receptor targeting ad therapeutic potential
    • French R.J., Terlau H. Sodium channel toxins - receptor targeting ad therapeutic potential. Curr. Med. Chem. 2004, 11:3053-3064.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 3053-3064
    • French, R.J.1    Terlau, H.2
  • 41
    • 77955300752 scopus 로고    scopus 로고
    • The tetrodotoxin receptor of voltage-gated sodium channels - perspectives from interactions with m-conotoxins
    • French R.J., Yoshikami D., Sheets M.F., Olivera B.M. The tetrodotoxin receptor of voltage-gated sodium channels - perspectives from interactions with m-conotoxins. Mar. Drugs 2010, 8:2153-2161.
    • (2010) Mar. Drugs , vol.8 , pp. 2153-2161
    • French, R.J.1    Yoshikami, D.2    Sheets, M.F.3    Olivera, B.M.4
  • 42
    • 0022930564 scopus 로고
    • Tetrodotoxin, tarichatoxin, and chiriquitoxin: historical perspectives
    • Fuhrman F.A. Tetrodotoxin, tarichatoxin, and chiriquitoxin: historical perspectives. Ann. N. Y. Acad. Sci. 1986, 479:1-14.
    • (1986) Ann. N. Y. Acad. Sci. , vol.479 , pp. 1-14
    • Fuhrman, F.A.1
  • 43
    • 0017100930 scopus 로고
    • An octopus toxin, maculotoxin, selectively blocks sodium current in squid axon
    • Gage P.W., Moore J.W., Westerfield M. An octopus toxin, maculotoxin, selectively blocks sodium current in squid axon. J. Physiol. (London) 1976, 259:427-443.
    • (1976) J. Physiol. (London) , vol.259 , pp. 427-443
    • Gage, P.W.1    Moore, J.W.2    Westerfield, M.3
  • 44
    • 17144385848 scopus 로고    scopus 로고
    • Evolutionary diversification of TTX-resistant sodium channels in a predator-prey interaction
    • Geffeney S.L., Fujimoto E., Brodie E.D., Brodie E.D., Ruben P.C. Evolutionary diversification of TTX-resistant sodium channels in a predator-prey interaction. Nature 2005, 434:759-763.
    • (2005) Nature , vol.434 , pp. 759-763
    • Geffeney, S.L.1    Fujimoto, E.2    Brodie, E.D.3    Brodie, E.D.4    Ruben, P.C.5
  • 45
    • 0018842787 scopus 로고
    • Saxitoxin binding to sodium channels in head extracts from wild-type and tetrodotoxin-sensitive strains of Drosophila melanogaster
    • Gitschier J., Strichartz G., Hall L.M. Saxitoxin binding to sodium channels in head extracts from wild-type and tetrodotoxin-sensitive strains of Drosophila melanogaster. Biochim. Biophys. Acta 1980, 595:291-303.
    • (1980) Biochim. Biophys. Acta , vol.595 , pp. 291-303
    • Gitschier, J.1    Strichartz, G.2    Hall, L.M.3
  • 47
    • 0022930575 scopus 로고
    • Surface charges near the guanidinium neurotoxin binding site
    • Green W.N., Andersen O.S. Surface charges near the guanidinium neurotoxin binding site. Ann. N. Y. Acad. Sci. 1986, 479:306-312.
    • (1986) Ann. N. Y. Acad. Sci. , vol.479 , pp. 306-312
    • Green, W.N.1    Andersen, O.S.2
  • 48
    • 0023269150 scopus 로고
    • Batrachotoxin-modified sodium channels in planar lipid bilayers: characterization of saxitoxin- and tetrodotoxin-induced closures
    • Green W.N., Weiss L.B., Andersen O.S. Batrachotoxin-modified sodium channels in planar lipid bilayers: characterization of saxitoxin- and tetrodotoxin-induced closures. J. Gen. Physiol. 1987, 89:873-903.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 873-903
    • Green, W.N.1    Weiss, L.B.2    Andersen, O.S.3
  • 49
    • 0019514340 scopus 로고
    • Chemically tritiated tetrodotoxin: physiological activity and binding to Na-channels
    • Grunhagen H.H., Rack M., Stampfli R., Fasold H., Reiter P. Chemically tritiated tetrodotoxin: physiological activity and binding to Na-channels. Arch. Biochem. Biophys. 1981, 206:198-204.
    • (1981) Arch. Biochem. Biophys. , vol.206 , pp. 198-204
    • Grunhagen, H.H.1    Rack, M.2    Stampfli, R.3    Fasold, H.4    Reiter, P.5
  • 50
    • 0023502221 scopus 로고
    • Kinetic basis for insensitivity to tetrodotoxin and saxitoxin in sodium channels of canine heart and denervated rat skeletal muscle
    • Guo X., Uehara A., Ravindran A., Bryant S.H., Hall S., Moczydlowski E. Kinetic basis for insensitivity to tetrodotoxin and saxitoxin in sodium channels of canine heart and denervated rat skeletal muscle. Biochemistry 1987, 26:7546-7556.
    • (1987) Biochemistry , vol.26 , pp. 7546-7556
    • Guo, X.1    Uehara, A.2    Ravindran, A.3    Bryant, S.H.4    Hall, S.5    Moczydlowski, E.6
  • 51
    • 77952520268 scopus 로고    scopus 로고
    • The chemical ecology and evolutionary ecology of tetrodotoxin (TTX) toxicity in terrestrial vertebrates
    • Hanifin C.T. The chemical ecology and evolutionary ecology of tetrodotoxin (TTX) toxicity in terrestrial vertebrates. Mar. Drugs 2010, 8:577-593.
    • (2010) Mar. Drugs , vol.8 , pp. 577-593
    • Hanifin, C.T.1
  • 52
    • 0035993548 scopus 로고    scopus 로고
    • Tetrodotoxin levels of the rough-skinned newt, Taricha granulosa, increase in long-term captivity
    • Hanifin C.T., Brodie E.D., Brodie E.D. Tetrodotoxin levels of the rough-skinned newt, Taricha granulosa, increase in long-term captivity. Toxicon: Off. J. Int. Soc. Toxinol. 2002, 40:1149-1153.
    • (2002) Toxicon: Off. J. Int. Soc. Toxinol. , vol.40 , pp. 1149-1153
    • Hanifin, C.T.1    Brodie, E.D.2    Brodie, E.D.3
  • 53
    • 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.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78
    • Hartshorne, R.P.1    Catterall, W.A.2
  • 55
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • Heinemann S.H., Terlau H., Stuhmer 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    Stuhmer, W.3    Imoto, K.4    Numa, S.5
  • 56
    • 0015166645 scopus 로고
    • The permeability of the sodium channel to organic cations in myelinated nerve
    • Hille B. The permeability of the sodium channel to organic cations in myelinated nerve. J. Gen. Physiol. 1971, 58:599-619.
    • (1971) J. Gen. Physiol. , vol.58 , pp. 599-619
    • Hille, B.1
  • 57
    • 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
  • 58
    • 0016612808 scopus 로고
    • An essential ionized acid group in sodium channels
    • Hille B. An essential ionized acid group in sodium channels. Fed. Proc. 1975, 34:1318-1321.
    • (1975) Fed. Proc. , vol.34 , pp. 1318-1321
    • Hille, B.1
  • 59
    • 0016782794 scopus 로고
    • The receptor for tetrodotoxin and saxitoxin: a structural hypothesis
    • Hille B. The receptor for tetrodotoxin and saxitoxin: a structural hypothesis. Biophys. J. 1975, 15:615-619.
    • (1975) Biophys. J. , vol.15 , pp. 615-619
    • Hille, B.1
  • 61
    • 0141534438 scopus 로고    scopus 로고
    • A stereoselective synthesis of (-)-tetrodotoxin
    • Hinman A., Du Bois J.A. A stereoselective synthesis of (-)-tetrodotoxin. J. Am. Chem. Soc. 2003, 125:11510-11511.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11510-11511
    • Hinman, A.1    Du Bois, J.A.2
  • 62
    • 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. (London) 1952, 117:500-544.
    • (1952) J. Physiol. (London) , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 63
    • 84870785539 scopus 로고    scopus 로고
    • Use-dependent block of the voltage-gated Na+ channel by tetrodotoxin and saxitoxin: effect of pore mutations that change ionic selectivity
    • Huang C.-J., Schild L., Moczydlowski E. Use-dependent block of the voltage-gated Na+ channel by tetrodotoxin and saxitoxin: effect of pore mutations that change ionic selectivity. J. Gen. Physiol. 2012, 140:435-454.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 435-454
    • Huang, C.-J.1    Schild, L.2    Moczydlowski, E.3
  • 64
    • 0020065556 scopus 로고
    • Batrachotoxin modifies the gating kinetics of sodium channels in internally perfused neuroblastoma cells
    • Huang L.-Y.M., Moran N., Ehrenstein G. Batrachotoxin modifies the gating kinetics of sodium channels in internally perfused neuroblastoma cells. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:2082-2085.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 2082-2085
    • Huang, L.-Y.M.1    Moran, N.2    Ehrenstein, G.3
  • 67
    • 33746512054 scopus 로고    scopus 로고
    • Accumulation of tetrodotoxin (TTX) in Pseudocaligus fugu, a parasitic copepod from panther puffer Takifugu pardalis, but without vertical transmission - using an immunoenzymatic technique
    • Ikeda K., Maran B.A.V., Honda S., Ohtsuka S., Arakawa O., Takatani T., Asakawa M., Boxshall G.A. Accumulation of tetrodotoxin (TTX) in Pseudocaligus fugu, a parasitic copepod from panther puffer Takifugu pardalis, but without vertical transmission - using an immunoenzymatic technique. Toxicon: Off. J. Int. Soc. Toxinol. 2006, 48:116-122.
    • (2006) Toxicon: Off. J. Int. Soc. Toxinol. , vol.48 , pp. 116-122
    • Ikeda, K.1    Maran, B.A.V.2    Honda, S.3    Ohtsuka, S.4    Arakawa, O.5    Takatani, T.6    Asakawa, M.7    Boxshall, G.A.8
  • 68
    • 33749598361 scopus 로고    scopus 로고
    • Detection of tetrodotoxin (TTX) from two copepods infecting the grass puffer Takifugu niphobles: TTX attracting the parasites?
    • Ito K., Okabe S., Asakawa M., Bessho K., Taniyama S., Shida Y., Ohtsuka S. Detection of tetrodotoxin (TTX) from two copepods infecting the grass puffer Takifugu niphobles: TTX attracting the parasites?. Toxicon: Off. J. Int. Soc. Toxinol. 2006, 48:620-626.
    • (2006) Toxicon: Off. J. Int. Soc. Toxinol. , vol.48 , pp. 620-626
    • Ito, K.1    Okabe, S.2    Asakawa, M.3    Bessho, K.4    Taniyama, S.5    Shida, Y.6    Ohtsuka, S.7
  • 70
    • 44649109665 scopus 로고    scopus 로고
    • Toxin-resistant sodium channels: parallel adaptive evolution across a complete gene family
    • Jost M.C., Hillis D.M., Lu Y., Kyle J.W., Fozzard H.A., Zakon H.H. Toxin-resistant sodium channels: parallel adaptive evolution across a complete gene family. Mol. Biol. Evol. 2008, 25:1016-1024.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1016-1024
    • Jost, M.C.1    Hillis, D.M.2    Lu, Y.3    Kyle, J.W.4    Fozzard, H.A.5    Zakon, H.H.6
  • 73
    • 0013921003 scopus 로고
    • Tetrodotoxin, saxitoxin and their significance in the study of excitation phenomena
    • Kao C.Y. Tetrodotoxin, saxitoxin and their significance in the study of excitation phenomena. Pharmacol. Rev. 1966, 18:997-1049.
    • (1966) Pharmacol. Rev. , vol.18 , pp. 997-1049
    • Kao, C.Y.1
  • 74
    • 0022930560 scopus 로고
    • Structure-activity relations of tetrodotoxin, saxitoxin, and analogues
    • Kao C.Y. Structure-activity relations of tetrodotoxin, saxitoxin, and analogues. Ann. N. Y. Acad. Sci. 1986, 479:52-67.
    • (1986) Ann. N. Y. Acad. Sci. , vol.479 , pp. 52-67
    • Kao, C.Y.1
  • 75
    • 0002961886 scopus 로고
    • Pharmacological studies on tarichatoxin, a potent neurotoxin
    • Kao C.Y., Fuhrman F.A. Pharmacological studies on tarichatoxin, a potent neurotoxin. J. Pharmacol. Exp. Ther. 1963, 140:31-40.
    • (1963) J. Pharmacol. Exp. Ther. , vol.140 , pp. 31-40
    • Kao, C.Y.1    Fuhrman, F.A.2
  • 76
    • 0013797237 scopus 로고
    • Actions of saxitoxin on peripheral neuromuscular systems
    • Kao C.Y., Nishiyama A. Actions of saxitoxin on peripheral neuromuscular systems. J. Physiol. (London) 1965, 180:50-66.
    • (1965) J. Physiol. (London) , vol.180 , pp. 50-66
    • Kao, C.Y.1    Nishiyama, A.2
  • 77
    • 0022195372 scopus 로고
    • Actions of 4-epitetrodotoxin and anhydrotetrodotoxin on the squid axon
    • Kao C.Y., Yasumoto T. Actions of 4-epitetrodotoxin and anhydrotetrodotoxin on the squid axon. Toxicon: Off. J. Int. Soc. Toxinol. 1985, 23:725-729.
    • (1985) Toxicon: Off. J. Int. Soc. Toxinol. , vol.23 , pp. 725-729
    • Kao, C.Y.1    Yasumoto, T.2
  • 79
    • 0030273231 scopus 로고    scopus 로고
    • Occurrence of tetrodotoxin in Alexandrium tamarense, a causative dinoflagellate of paralytic shellfish poisoning
    • Kodama M., Sato S., Sakamoto S., Ogata T. Occurrence of tetrodotoxin in Alexandrium tamarense, a causative dinoflagellate of paralytic shellfish poisoning. Toxicon: Off. J. Int. Soc. Toxinol. 1996, 34:1101-1105.
    • (1996) Toxicon: Off. J. Int. Soc. Toxinol. , vol.34 , pp. 1101-1105
    • Kodama, M.1    Sato, S.2    Sakamoto, S.3    Ogata, T.4
  • 80
    • 0020640470 scopus 로고
    • Single sodium channels from rat brain incorporated into planar lipid bilayers
    • Krueger B.K., Worley J.F., French R.J. Single sodium channels from rat brain incorporated into planar lipid bilayers. Nature 1983, 303:172-175.
    • (1983) Nature , vol.303 , pp. 172-175
    • Krueger, B.K.1    Worley, J.F.2    French, R.J.3
  • 81
    • 0022989915 scopus 로고
    • Block of sodium channels in planar lipid bilayers by guanidinium toxins and calcium: are the mechanisms of voltage-dependence the same?
    • Krueger B.K., Worley J.F., French R.J. Block of sodium channels in planar lipid bilayers by guanidinium toxins and calcium: are the mechanisms of voltage-dependence the same?. Ann. N. Y. Acad. Sci. 1986, 479:257-268.
    • (1986) Ann. N. Y. Acad. Sci. , vol.479 , pp. 257-268
    • Krueger, B.K.1    Worley, J.F.2    French, R.J.3
  • 82
    • 78650792933 scopus 로고    scopus 로고
    • Biophysical costs associated with tetrodotoxin resistance in the sodium channel pore of the garter snake, Thamnophis sirtalis
    • Lee C.H., Jones D.K., Ahern C.A., Sarhan M.F., Ruben P.C. Biophysical costs associated with tetrodotoxin resistance in the sodium channel pore of the garter snake, Thamnophis sirtalis. J. Comp. Physiol. A 2011, 197:33-43.
    • (2011) J. Comp. Physiol. A , vol.197 , pp. 33-43
    • Lee, C.H.1    Jones, D.K.2    Ahern, C.A.3    Sarhan, M.F.4    Ruben, P.C.5
  • 83
    • 64149102359 scopus 로고    scopus 로고
    • Interaction between voltage-gated sodium channels and the neurotoxin, tetrodotoxin
    • Lee H.L., Ruben P.C. Interaction between voltage-gated sodium channels and the neurotoxin, tetrodotoxin. Channels 2008, 2:407-412.
    • (2008) Channels , vol.2 , pp. 407-412
    • Lee, H.L.1    Ruben, P.C.2
  • 84
    • 4043147877 scopus 로고    scopus 로고
    • No evidence for an endosymbiotic bacterial origin of tetrodotoxin in the newt Taricha granulosa
    • Lehman E.M., Brodie E.D., Brodie E.D. No evidence for an endosymbiotic bacterial origin of tetrodotoxin in the newt Taricha granulosa. Toxicon: Off. J. Int. Soc. Toxinol. 2004, 44:243-249.
    • (2004) Toxicon: Off. J. Int. Soc. Toxinol. , vol.44 , pp. 243-249
    • Lehman, E.M.1    Brodie, E.D.2    Brodie, E.D.3
  • 85
    • 77951883450 scopus 로고    scopus 로고
    • The physiological significance of the cardiotonic steroid/ouabain-binding site of the Na, K-ATPase
    • Lingrel J.B. The physiological significance of the cardiotonic steroid/ouabain-binding site of the Na, K-ATPase. Annu. Rev. Physiol. 2010, 72:395-412.
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 395-412
    • Lingrel, J.B.1
  • 86
    • 0028055161 scopus 로고
    • A structural model of the tetrodotoxin and saxitoxin binding site of the Na+ channel
    • Lipkind G.M., Fozzard H.A. A structural model of the tetrodotoxin and saxitoxin binding site of the Na+ channel. Biophys. J. 1994, 66:1-13.
    • (1994) Biophys. J. , vol.66 , pp. 1-13
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 87
    • 0034682616 scopus 로고    scopus 로고
    • KcsA crystal structure as framework for a molecular model of the Na+ channel pore
    • Lipkind G.M., Fozzard H.A. KcsA crystal structure as framework for a molecular model of the Na+ channel pore. Biochemistry 2000, 39:8161-8170.
    • (2000) Biochemistry , vol.39 , pp. 8161-8170
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 88
    • 0030845479 scopus 로고    scopus 로고
    • Phylogenetic survey of soluble saxitoxin-binding activity in pursuit of the function and evolution of saxiphilin, a relative of transferrin
    • Llewellyn L.E., Bell P.M., Moczydlowski E.G. Phylogenetic survey of soluble saxitoxin-binding activity in pursuit of the function and evolution of saxiphilin, a relative of transferrin. Proc. R. Soc. Lond. B 1997, 264:891-902.
    • (1997) Proc. R. Soc. Lond. B , vol.264 , pp. 891-902
    • Llewellyn, L.E.1    Bell, P.M.2    Moczydlowski, E.G.3
  • 89
    • 0023265064 scopus 로고
    • Identification in mammalian brain of an endogenous substance with Na+ channel blocking activities similar to those of tetrodotoxin
    • Lombet A., Fosset M., Romey G., Jacomet Y., Lazdunski M. Identification in mammalian brain of an endogenous substance with Na+ channel blocking activities similar to those of tetrodotoxin. Brain Res. 1987, 417:327-334.
    • (1987) Brain Res. , vol.417 , pp. 327-334
    • Lombet, A.1    Fosset, M.2    Romey, G.3    Jacomet, Y.4    Lazdunski, M.5
  • 90
    • 23244441222 scopus 로고    scopus 로고
    • Voltage-sensor of Kv1.2: structural basis of electromechanical coupling
    • Long S.B., Campbell E.B., MacKinnon R. Voltage-sensor of Kv1.2: structural basis of electromechanical coupling. Science 2005, 309:903-908.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 91
    • 0021741804 scopus 로고
    • Occurrence of tetrodotoxin in the starfish Astropecten latespinosus
    • 1395-1395
    • Maruyama J., Noguchi T., Jeon J., Hashimoto K. Occurrence of tetrodotoxin in the starfish Astropecten latespinosus. Cell Mol. Life Sci. 1984, 40. 1395-1395.
    • (1984) Cell Mol. Life Sci. , vol.40
    • Maruyama, J.1    Noguchi, T.2    Jeon, J.3    Hashimoto, K.4
  • 93
    • 0029638871 scopus 로고
    • Tetrodotoxin as a pheromone
    • Matsumura K. Tetrodotoxin as a pheromone. Nature 1995, 378:563-564.
    • (1995) Nature , vol.378 , pp. 563-564
    • Matsumura, K.1
  • 94
    • 0020665772 scopus 로고
    • Principal glycopeptide of the tetrodotoxin/saxitoxin binding protein from Electrophorus electricus: isolation and partial chemical and physical characterization
    • Miller J.A., Agnew W.S., Levinson S.R. Principal glycopeptide of the tetrodotoxin/saxitoxin binding protein from Electrophorus electricus: isolation and partial chemical and physical characterization. Biochemistry 1983, 22:462-470.
    • (1983) Biochemistry , vol.22 , pp. 462-470
    • Miller, J.A.1    Agnew, W.S.2    Levinson, S.R.3
  • 95
    • 0023618885 scopus 로고
    • Distribution of tetrodotoxin in various organs of the starfish Astopecten polyacanthus
    • Miyazawa K., Higashiyama M., Hori K., Noguchi T., Ito K., Hashimoto K. Distribution of tetrodotoxin in various organs of the starfish Astopecten polyacanthus. Mar. Biol. 1987, 96:385-390.
    • (1987) Mar. Biol. , vol.96 , pp. 385-390
    • Miyazawa, K.1    Higashiyama, M.2    Hori, K.3    Noguchi, T.4    Ito, K.5    Hashimoto, K.6
  • 96
    • 0021675856 scopus 로고
    • Batrachotoxin-activated Na+ channels in planar lipid bilayers: competition of tetrodotoxin block by Na+
    • Moczydlowski E., Garber S.S., Miller C. Batrachotoxin-activated Na+ channels in planar lipid bilayers: competition of tetrodotoxin block by Na+. J. Gen. Physiol. 1984, 84:665-686.
    • (1984) J. Gen. Physiol. , vol.84 , pp. 665-686
    • Moczydlowski, E.1    Garber, S.S.2    Miller, C.3
  • 97
    • 0021736390 scopus 로고
    • Voltage-dependent blockade of muscle Na+ channels by guanidinium toxins: effect of toxin charge
    • Moczydlowski E., Hall S.H., Garber S.S., Strichartz G., Miller C. Voltage-dependent blockade of muscle Na+ channels by guanidinium toxins: effect of toxin charge. J. Gen. Physiol. 1984, 84:687-707.
    • (1984) J. Gen. Physiol. , vol.84 , pp. 687-707
    • Moczydlowski, E.1    Hall, S.H.2    Garber, S.S.3    Strichartz, G.4    Miller, C.5
  • 98
    • 0022930556 scopus 로고
    • The chemistry of tetrodotoxin
    • Mosher H.S. The chemistry of tetrodotoxin. Ann. N. Y. Acad. Sci. 1986, 479:32-43.
    • (1986) Ann. N. Y. Acad. Sci. , vol.479 , pp. 32-43
    • Mosher, H.S.1
  • 100
    • 79951831891 scopus 로고    scopus 로고
    • Extraordinary conservation, gene loss, and positive selection in the evolution of an ancient neurotoxin
    • Murray S.A., Mihali T.K., Neilan B.A. Extraordinary conservation, gene loss, and positive selection in the evolution of an ancient neurotoxin. Mol. Biol. Evol. 2011, 28:1173-1182.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 1173-1182
    • Murray, S.A.1    Mihali, T.K.2    Neilan, B.A.3
  • 103
  • 105
    • 0000433667 scopus 로고
    • Stabilization and rectification of muscle fiber membrane by tetrodotoxin
    • Narahashi T., Deguchi T., Urakawa N., Ohkubu Y. Stabilization and rectification of muscle fiber membrane by tetrodotoxin. Am. J. Physiol. 1960, 198:934-938.
    • (1960) Am. J. Physiol. , vol.198 , pp. 934-938
    • Narahashi, T.1    Deguchi, T.2    Urakawa, N.3    Ohkubu, Y.4
  • 106
    • 0014214211 scopus 로고
    • Saxitoxin and tetrodotoxin: comparison of nerve blocking mechanism
    • Narahashi T., Haas H.G., Therrien E.F. Saxitoxin and tetrodotoxin: comparison of nerve blocking mechanism. Science 1967, 157:1441-1442.
    • (1967) Science , vol.157 , pp. 1441-1442
    • Narahashi, T.1    Haas, H.G.2    Therrien, E.F.3
  • 107
    • 0000752763 scopus 로고
    • Tetrodotoxin blockage of sodium conductance increase in lobster giant axons
    • Narahashi T., Moore J.W., Scott W.R. Tetrodotoxin blockage of sodium conductance increase in lobster giant axons. J. Gen. Physiol. 1964, 47:965-974.
    • (1964) J. Gen. Physiol. , vol.47 , pp. 965-974
    • Narahashi, T.1    Moore, J.W.2    Scott, W.R.3
  • 112
    • 0024811092 scopus 로고
    • A single point mutation confers tetrodotoxin and saxitoxin sensitivity on the sodium channel II
    • Noda M., Suzuki H., Numa S., Stuhmer W. A single point mutation confers tetrodotoxin and saxitoxin sensitivity 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    Stuhmer, W.4
  • 113
    • 33644507696 scopus 로고    scopus 로고
    • Toxicity of pufferfish Takifugu rubripes cultured in netcages at sea or aquaria on land
    • Noguchi T., Arakawa O., Takatani T. Toxicity of pufferfish Takifugu rubripes cultured in netcages at sea or aquaria on land. Comp. Biochem. Physiol. Part D 2006, 1:153-157.
    • (2006) Comp. Biochem. Physiol. Part D , vol.1 , pp. 153-157
    • Noguchi, T.1    Arakawa, O.2    Takatani, T.3
  • 116
    • 0022658561 scopus 로고
    • Occurrence of tetrodotoxin and anhydrotetrodotoxin in Vibrio sp. isolated from the intestines of a xanthid crab, Atergatis floridus
    • Noguchi T., Jeon J., Arakawa O., Sugita H., Deguchi Y., Shida Y., Hashimoto K. Occurrence of tetrodotoxin and anhydrotetrodotoxin in Vibrio sp. isolated from the intestines of a xanthid crab, Atergatis floridus. J. Biochem. 1986, 99:311-314.
    • (1986) J. Biochem. , vol.99 , pp. 311-314
    • Noguchi, T.1    Jeon, J.2    Arakawa, O.3    Sugita, H.4    Deguchi, Y.5    Shida, Y.6    Hashimoto, K.7
  • 117
    • 0017087818 scopus 로고
    • A fluorimetric method to determine tetrodotoxin
    • Nunez M.T., Fischer S., Jaimovich E. A fluorimetric method to determine tetrodotoxin. Anal. Biochem. 1976, 74:320-325.
    • (1976) Anal. Biochem. , vol.74 , pp. 320-325
    • Nunez, M.T.1    Fischer, S.2    Jaimovich, E.3
  • 118
    • 0038637028 scopus 로고    scopus 로고
    • First asymmetric total synthesis of tetrodotoxin
    • Ohyabu N., Nishikawa T., Isobe M. First asymmetric total synthesis of tetrodotoxin. J. Amer. Chem. Soc. 2003, 125:8798-8805.
    • (2003) J. Amer. Chem. Soc. , vol.125 , pp. 8798-8805
    • Ohyabu, N.1    Nishikawa, T.2    Isobe, M.3
  • 119
    • 0026055174 scopus 로고
    • A voltage-dependent gating transition induces use-dependence block by tetrodotoxin of rat IIA sodium channels expressed in Xenopus oocytes
    • Patton D.E., Goldin A.L. A voltage-dependent gating transition induces use-dependence block by tetrodotoxin of rat IIA sodium channels expressed in Xenopus oocytes. Neuron 1991, 7:637-647.
    • (1991) Neuron , vol.7 , pp. 637-647
    • Patton, D.E.1    Goldin, A.L.2
  • 120
    • 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, 475:353-358.
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 121
    • 0031768855 scopus 로고    scopus 로고
    • Differences in saxitoxin and tetrodotoxin binding revealed by mutagenesis of the Na+ channel outer vestibule
    • Penzotti J.L., Fozzard H.A., Lipkind G.M., Dudley S.C. Differences in saxitoxin and tetrodotoxin binding revealed by mutagenesis of the Na+ channel outer vestibule. Biophys. J. 1998, 75:2647-2657.
    • (1998) Biophys. J. , vol.75 , pp. 2647-2657
    • Penzotti, J.L.1    Fozzard, H.A.2    Lipkind, G.M.3    Dudley, S.C.4
  • 122
    • 0024503421 scopus 로고
    • Influence of negative surface charge on toxin binding to canine heart Na channels in planar bilayers
    • Ravindran A., Moczydlowski E. Influence of negative surface charge on toxin binding to canine heart Na channels in planar bilayers. Biophys. J. 1989, 55:359-365.
    • (1989) Biophys. J. , vol.55 , pp. 359-365
    • Ravindran, A.1    Moczydlowski, E.2
  • 123
    • 0025959151 scopus 로고
    • Divalent cation selectivity for external block of voltage-dependent Na+ channels prolonged by batrachotoxin: Zn2+ induces discrete substates in cardiac Na+ channels
    • Ravindran A., Schild L., Moczydlowski E. Divalent cation selectivity for external block of voltage-dependent Na+ channels prolonged by batrachotoxin: Zn2+ induces discrete substates in cardiac Na+ channels. J. Gen. Physiol. 1991, 97:89-115.
    • (1991) J. Gen. Physiol. , vol.97 , pp. 89-115
    • Ravindran, A.1    Schild, L.2    Moczydlowski, E.3
  • 124
    • 0017327105 scopus 로고
    • The binding of tetrodotoxin and saxitoxin to excitable tissue
    • Ritchie J.M., Rogart R.B. The binding of tetrodotoxin and saxitoxin to excitable tissue. Rev. Physiol. Biochem. Pharmacol. 1977, 79:1-50.
    • (1977) Rev. Physiol. Biochem. Pharmacol. , vol.79 , pp. 1-50
    • Ritchie, J.M.1    Rogart, R.B.2
  • 125
    • 0017108130 scopus 로고
    • Binding to nerve and muscle of saxitoxin labelled by a new method of tritium exchange
    • Ritchie J.M., Rogart R.B., Strichartz G. Binding to nerve and muscle of saxitoxin labelled by a new method of tritium exchange. J. Physiol. (London) 1976, 261:477-494.
    • (1976) J. Physiol. (London) , vol.261 , pp. 477-494
    • Ritchie, J.M.1    Rogart, R.B.2    Strichartz, G.3
  • 128
    • 0022930559 scopus 로고
    • Use- and voltage-dependent block of the sodium channel by saxitoxin
    • Salgado V.L., Yeh J.Z., Narahashi T. Use- and voltage-dependent block of the sodium channel by saxitoxin. Ann. N. Y. Acad. Sci. 1986, 479:84-95.
    • (1986) Ann. N. Y. Acad. Sci. , vol.479 , pp. 84-95
    • Salgado, V.L.1    Yeh, J.Z.2    Narahashi, T.3
  • 129
    • 34247267099 scopus 로고    scopus 로고
    • A cation-p interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block
    • Santarelli V.P., Eastwood A.L., Dougherty D.A., Horn R., Ahern C.A. A cation-p interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block. J. Biol. Chem. 2007, 282:8044-8055.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8044-8055
    • Santarelli, V.P.1    Eastwood, A.L.2    Dougherty, D.A.3    Horn, R.4    Ahern, C.A.5
  • 130
    • 0026637366 scopus 로고
    • A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties
    • Satin J., Kyle J.W., Chen M., Bell P., Cribs L.L., Fozzard H.A., Rogart R.B. A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties. Science 1992, 256:1202-1205.
    • (1992) Science , vol.256 , pp. 1202-1205
    • Satin, J.1    Kyle, J.W.2    Chen, M.3    Bell, P.4    Cribs, L.L.5    Fozzard, H.A.6    Rogart, R.B.7
  • 131
    • 0028108255 scopus 로고
    • The saxitoxin-tetrodotoxin binding site on cloned rat brain IIa Na channels is in the transmembrane electric field
    • Satin J., Limberis J.T., Kyle J.W., Rogart R.B., Fozzard H.A. The saxitoxin-tetrodotoxin binding site on cloned rat brain IIa Na channels is in the transmembrane electric field. Biophys. J. 1994, 67:1007-1014.
    • (1994) Biophys. J. , vol.67 , pp. 1007-1014
    • Satin, J.1    Limberis, J.T.2    Kyle, J.W.3    Rogart, R.B.4    Fozzard, H.A.5
  • 134
    • 0026031454 scopus 로고
    • Competitive binding interaction between Zn2+ and saxitoxin in cardiac Na+ channels: evidence for a sulfhydryl group in the Zn2+/saxitoxin binding site
    • Schild L., Moczydlowski E. Competitive binding interaction between Zn2+ and saxitoxin in cardiac Na+ channels: evidence for a sulfhydryl group in the Zn2+/saxitoxin binding site. Biophys. J. 1991, 59:523-637.
    • (1991) Biophys. J. , vol.59 , pp. 523-637
    • Schild, L.1    Moczydlowski, E.2
  • 135
    • 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. J. Biophys. 1996, 25:75-91.
    • (1996) Eur. J. Biophys. , vol.25 , pp. 75-91
    • Schlief, T.1    Schonherr, R.2    Imoto, K.3    Heinemann, S.H.4
  • 136
    • 0026907261 scopus 로고
    • Mechanisms of extracellular divalent and trivalent cation block of the sodium current in canine cardiac Purkinje cells
    • Sheets M.F., Hanck D.A. Mechanisms of extracellular divalent and trivalent cation block of the sodium current in canine cardiac Purkinje cells. J. Physiol. (London) 1992, 454:299-320.
    • (1992) J. Physiol. (London) , vol.454 , pp. 299-320
    • Sheets, M.F.1    Hanck, D.A.2
  • 137
    • 0017870726 scopus 로고
    • Maculotoxin: a neurotoxin from the venom glands of the octopus Hapalochlaena maculosa identified as tetrodotoxin
    • Sheumack D.D., Howden M.E.H., Spence I., Quinn R.J. Maculotoxin: a neurotoxin from the venom glands of the octopus Hapalochlaena maculosa identified as tetrodotoxin. Science 1978, 199:188-189.
    • (1978) Science , vol.199 , pp. 188-189
    • Sheumack, D.D.1    Howden, M.E.H.2    Spence, I.3    Quinn, R.J.4
  • 138
    • 0021040806 scopus 로고
    • Apparent lack of tetrodotoxin biosynthesis in captured Taricha torosa and Taricha granulosa
    • Shimizu Y., Kobayashi M. Apparent lack of tetrodotoxin biosynthesis in captured Taricha torosa and Taricha granulosa. Chem. Pharm. Bull. 1983, 31:3625-3631.
    • (1983) Chem. Pharm. Bull. , vol.31 , pp. 3625-3631
    • Shimizu, Y.1    Kobayashi, M.2
  • 139
    • 80054042382 scopus 로고    scopus 로고
    • Synthesis of skeletal analogues of saxitoxin derivatives and evaluation of their inhibitory activity on sodium ion channels Na(V)1.4 and Na(V)1.5
    • Shinohara R., Akimoto T., Iwamoto O., Hirokawa T., Yotsu-Yamashita M., Yamaoka K., Nagasawa K. Synthesis of skeletal analogues of saxitoxin derivatives and evaluation of their inhibitory activity on sodium ion channels Na(V)1.4 and Na(V)1.5. Chem. Eur. J. 2011, 17:12144-12152.
    • (2011) Chem. Eur. J. , vol.17 , pp. 12144-12152
    • Shinohara, R.1    Akimoto, T.2    Iwamoto, O.3    Hirokawa, T.4    Yotsu-Yamashita, M.5    Yamaoka, K.6    Nagasawa, K.7
  • 140
    • 0018910573 scopus 로고
    • Properties of toxin-resistant sodium channels produced by chemical modification in frog skeletal muscle
    • Spalding B.C. Properties of toxin-resistant sodium channels produced by chemical modification in frog skeletal muscle. J. Physiol. (London) 1980, 305:485-500.
    • (1980) J. Physiol. (London) , vol.305 , pp. 485-500
    • Spalding, B.C.1
  • 142
    • 0019825209 scopus 로고
    • Saxitoxin binding in nerves from walking legs of the lobster Homarus americanus
    • Strichartz G., Hansen Bay C.M. Saxitoxin binding in nerves from walking legs of the lobster Homarus americanus. J. Gen. Physiol. 1981, 77:205-221.
    • (1981) J. Gen. Physiol. , vol.77 , pp. 205-221
    • Strichartz, G.1    Hansen Bay, C.M.2
  • 143
    • 79956218158 scopus 로고    scopus 로고
    • Discovery of nuclear-encoded genes for the neurotoxin saxitoxin in dinoflagellates
    • e20096
    • Stüken A., Orr R.J.S., Kellmann R., Murray S.A., Neilan B.A., Jakobsen K.S. Discovery of nuclear-encoded genes for the neurotoxin saxitoxin in dinoflagellates. PLoS ONE 2011, 6(e20096):1-12.
    • (2011) PLoS ONE , vol.6 , pp. 1-12
    • Stüken, A.1    Orr, R.J.S.2    Kellmann, R.3    Murray, S.A.4    Neilan, B.A.5    Jakobsen, K.S.6
  • 146
    • 0030777655 scopus 로고    scopus 로고
    • On the structural basis for size-selective permeation of organic cations through the voltage-gated sodium channel: effect of alanine mutations at the DEKA locus on selectivity, inhibition by Ca2+ and H+, and molecular sieving
    • Sun Y.-M., Favre I., Schild L., Moczydlowski E. On the structural basis for size-selective permeation of organic cations through the voltage-gated sodium channel: effect of alanine mutations at the DEKA locus on selectivity, inhibition by Ca2+ and H+, and molecular sieving. J. Gen. Physiol. 1997, 110:693-715.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 693-715
    • Sun, Y.-M.1    Favre, I.2    Schild, L.3    Moczydlowski, E.4
  • 147
    • 0008894364 scopus 로고
    • Uber das tetrodongift
    • Tahara Y. Uber das tetrodongift. Biochem. Zeitsch. 1910, 10:255-275.
    • (1910) Biochem. Zeitsch. , vol.10 , pp. 255-275
    • Tahara, Y.1
  • 148
    • 0002800142 scopus 로고
    • A bacterial source of tetrodotoxins and saxitoxins
    • American Chemical Society, Washington, DC, S. Hall, G. Strichartz (Eds.)
    • Tamplin M.L. A bacterial source of tetrodotoxins and saxitoxins. Marine Toxins: Origin, Structure, and Molecular Pharmacology 1990, 78-86. American Chemical Society, Washington, DC. S. Hall, G. Strichartz (Eds.).
    • (1990) Marine Toxins: Origin, Structure, and Molecular Pharmacology , pp. 78-86
    • Tamplin, M.L.1
  • 150
    • 11244296111 scopus 로고    scopus 로고
    • Modeling P-loops domain of sodium channel: homology with potassium channels and interaction with ligands
    • Tikhonov D.B., Zhorov B.S. Modeling P-loops domain of sodium channel: homology with potassium channels and interaction with ligands. Biophys. J. 2005, 88:184-197.
    • (2005) Biophys. J. , vol.88 , pp. 184-197
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 151
    • 84862561580 scopus 로고    scopus 로고
    • Architecture and the pore block of eukaryotic voltage-gated sodium channels in view of the NavAb bacterial sodium channel structure
    • Tikhonov D.B., Zhorov B.S. Architecture and the pore block of eukaryotic voltage-gated sodium channels in view of the NavAb bacterial sodium channel structure. Mol. Pharmacol. 2012, 82:97-104.
    • (2012) Mol. Pharmacol. , vol.82 , pp. 97-104
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 155
    • 0343563436 scopus 로고
    • The constituents of the ovaries of globefish. VII. Purification of tetrodotoxin by chromatography
    • Tsuda K., Kauamura M. The constituents of the ovaries of globefish. VII. Purification of tetrodotoxin by chromatography. J. Pharm. Soc. Jpn. 1952, 72:771-772.
    • (1952) J. Pharm. Soc. Jpn. , vol.72 , pp. 771-772
    • Tsuda, K.1    Kauamura, M.2
  • 156
    • 0040766536 scopus 로고
    • Motor inhibition in Amblystoma produced by Triturus transplants
    • Twitty V.C., Johnson H.H. Motor inhibition in Amblystoma produced by Triturus transplants. Science 1934, 80:78-79.
    • (1934) Science , vol.80 , pp. 78-79
    • Twitty, V.C.1    Johnson, H.H.2
  • 157
    • 0037290637 scopus 로고    scopus 로고
    • Voltage-gated sodium channels as primary targets of diverse lipid-soluble neurotoxins
    • Wang S.Y., Wang G.K. Voltage-gated sodium channels as primary targets of diverse lipid-soluble neurotoxins. Cell. Signal. 2003, 15:151-159.
    • (2003) Cell. Signal. , vol.15 , pp. 151-159
    • Wang, S.Y.1    Wang, G.K.2
  • 158
    • 0018123088 scopus 로고
    • Saxitoxin binding to the mammalian sodium channel: competition by monovalent and divalent cations
    • Weigele J.B., Barchi R.L. Saxitoxin binding to the mammalian sodium channel: competition by monovalent and divalent cations. FEBS Lett. 1978, 95:49-53.
    • (1978) FEBS Lett. , vol.95 , pp. 49-53
    • Weigele, J.B.1    Barchi, R.L.2
  • 159
    • 0019918257 scopus 로고
    • Functional reconstitution of the purified sodium channel protein from rat sarcolemma
    • Weigele J.B., Barchi R.L. Functional reconstitution of the purified sodium channel protein from rat sarcolemma. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:3651-3655.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3651-3655
    • Weigele, J.B.1    Barchi, R.L.2
  • 160
    • 78650498923 scopus 로고    scopus 로고
    • Differential evolution of voltage-gated sodium channels in tetrapods and teleost fishes
    • Widmark J., Sundstrom G., Daza D.O., Larhammar D. Differential evolution of voltage-gated sodium channels in tetrapods and teleost fishes. Mol. Biol. Evol. 2010, 28:859-871.
    • (2010) Mol. Biol. Evol. , vol.28 , pp. 859-871
    • Widmark, J.1    Sundstrom, G.2    Daza, D.O.3    Larhammar, D.4
  • 161
    • 77952490850 scopus 로고    scopus 로고
    • Behavioral and chemical ecology of marine organisms with respect to tetrodotoxin
    • Williams B.L. Behavioral and chemical ecology of marine organisms with respect to tetrodotoxin. Mar. Drugs 2010, 8:381-398.
    • (2010) Mar. Drugs , vol.8 , pp. 381-398
    • Williams, B.L.1
  • 162
    • 84931650591 scopus 로고
    • The structure of tetrodotoxin
    • Woodward R.B. The structure of tetrodotoxin. Pure Appl. Chem. 1964, 9:49-74.
    • (1964) Pure Appl. Chem. , vol.9 , pp. 49-74
    • Woodward, R.B.1
  • 163
    • 0022599511 scopus 로고
    • Trimethyloxonium modification of single batrachotoxin-activated sodium channels in planar bilayers: changes in unit conductance and in block by saxitoxin and calcium
    • Worley J.F., French R.J., Krueger B.K. Trimethyloxonium modification of single batrachotoxin-activated sodium channels in planar bilayers: changes in unit conductance and in block by saxitoxin and calcium. J. Gen. Physiol. 1986, 87:327-349.
    • (1986) J. Gen. Physiol. , vol.87 , pp. 327-349
    • Worley, J.F.1    French, R.J.2    Krueger, B.K.3
  • 164
    • 24044505083 scopus 로고    scopus 로고
    • Toxicity and distribution of tetrodotoxin-producing bacteria in puffer fish Fugu rubripes collected from the Bohai Sea of China
    • Wu Z., Yang Y., Xie L., Xia G., Hu J., Wang S.Y., Zhang R. Toxicity and distribution of tetrodotoxin-producing bacteria in puffer fish Fugu rubripes collected from the Bohai Sea of China. Toxicon: Off. J. Int. Soc. Toxinol. 2005, 46:471-476.
    • (2005) Toxicon: Off. J. Int. Soc. Toxinol. , vol.46 , pp. 471-476
    • Wu, Z.1    Yang, Y.2    Xie, L.3    Xia, G.4    Hu, J.5    Wang, S.Y.6    Zhang, R.7
  • 165
    • 55249117019 scopus 로고    scopus 로고
    • Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain II voltage sensor in the closed configuration
    • Xiao Y., Bingham J.P., Zhu W., Moczydlowski E., Liang S., Cummins T.R. Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain II voltage sensor in the closed configuration. J. Biol. Chem. 2008, 283:27300-27313.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27300-27313
    • Xiao, Y.1    Bingham, J.P.2    Zhu, W.3    Moczydlowski, E.4    Liang, S.5    Cummins, T.R.6
  • 166
    • 0026731650 scopus 로고
    • Actions of chiriquitoxin on frog skeletal muscle fibers and implications for the tetrodotoxin/saxitoxin receptor
    • Yang L., Kao C.Y. Actions of chiriquitoxin on frog skeletal muscle fibers and implications for the tetrodotoxin/saxitoxin receptor. J. Gen. Physiol. 1992, 100:609-622.
    • (1992) J. Gen. Physiol. , vol.100 , pp. 609-622
    • Yang, L.1    Kao, C.Y.2
  • 167
    • 0026623216 scopus 로고
    • Actions of 6-epitetrodotoxin and 11-deoxytetrodotoxin on the frog skeletal muscle fiber
    • Yang L., Kao C.Y., Yasumoto T. Actions of 6-epitetrodotoxin and 11-deoxytetrodotoxin on the frog skeletal muscle fiber. Toxicon: Off. J. Int. Soc. Toxinol. 1992, 30:635-643.
    • (1992) Toxicon: Off. J. Int. Soc. Toxinol. , vol.30 , pp. 635-643
    • Yang, L.1    Kao, C.Y.2    Yasumoto, T.3
  • 169
    • 0022406152 scopus 로고
    • Fluorometric determination of tetrodotoxin by high performance liquid chromatography
    • Yasumoto T., Michishita T. Fluorometric determination of tetrodotoxin by high performance liquid chromatography. Agric. Biol. Chem. 1985, 49:3077-3080.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 3077-3080
    • Yasumoto, T.1    Michishita, T.2
  • 171
    • 33845280591 scopus 로고
    • New tetrodotoxin analogues from the newt Cynops ensicauda
    • Yasumoto T., Yotsu M., Murata M. New tetrodotoxin analogues from the newt Cynops ensicauda. J. Amer. Chem. Soc. 1988, 110:2344-2345.
    • (1988) J. Amer. Chem. Soc. , vol.110 , pp. 2344-2345
    • Yasumoto, T.1    Yotsu, M.2    Murata, M.3
  • 172
    • 84961340389 scopus 로고
    • Chemical studies on globefish poison. III. Separation of spheroodin
    • Yokoo A. Chemical studies on globefish poison. III. Separation of spheroodin. J. Chem. Soc. Jpn. 1950, 71:590-592.
    • (1950) J. Chem. Soc. Jpn. , vol.71 , pp. 590-592
    • Yokoo, A.1
  • 175
    • 0033061210 scopus 로고    scopus 로고
    • Effects of specific modifications of several hydroxyls of tetrodotoxin on its affinity to rat brain membrane
    • Yotsu-Yamashita M., Sugimoto A., Takai T., Yasumoto T. Effects of specific modifications of several hydroxyls of tetrodotoxin on its affinity to rat brain membrane. J. Pharm. Exp. Ther. 1999, 289:1688-1696.
    • (1999) J. Pharm. Exp. Ther. , vol.289 , pp. 1688-1696
    • Yotsu-Yamashita, M.1    Sugimoto, A.2    Takai, T.3    Yasumoto, T.4
  • 176
    • 0035166904 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA cloning of a novel soluble saxitoxin and tetrodotoxin binding protein from the plasma of the puffer fish, Fugu pardalis
    • Yotsu-Yamashita M., Sugimoto A., Terakawa T., Shoji Y., Miyazawa T., Yasumoto T. Purification, characterization, and cDNA cloning of a novel soluble saxitoxin and tetrodotoxin binding protein from the plasma of the puffer fish, Fugu pardalis. Eur. J. Biochem. 2001, 268:5937-5946.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5937-5946
    • Yotsu-Yamashita, M.1    Sugimoto, A.2    Terakawa, T.3    Shoji, Y.4    Miyazawa, T.5    Yasumoto, T.6
  • 177
    • 70649101317 scopus 로고    scopus 로고
    • First report on toxins in the Panamanian toads Atelopus limosus, A. glyphys, and A. certus
    • Yotsu-Yamashita M., Tateki E. First report on toxins in the Panamanian toads Atelopus limosus, A. glyphys, and A. certus. Toxicon: Off. J. Int. Soc. Toxinol. 2010, 55:153-156.
    • (2010) Toxicon: Off. J. Int. Soc. Toxinol. , vol.55 , pp. 153-156
    • Yotsu-Yamashita, M.1    Tateki, E.2
  • 178
    • 0025317364 scopus 로고
    • The distribution of tetrodotoxin, 6-epitetrodotoxin, and 11-deoxytetrodotoxin in newts
    • Yotsu M., Iorizzi M., Yasumoto T. The distribution of tetrodotoxin, 6-epitetrodotoxin, and 11-deoxytetrodotoxin in newts. Toxicon: Off. J. Int. Soc. Toxinol. 1990, 28:238-241.
    • (1990) Toxicon: Off. J. Int. Soc. Toxinol. , vol.28 , pp. 238-241
    • Yotsu, M.1    Iorizzi, M.2    Yasumoto, T.3
  • 179
    • 0025368753 scopus 로고
    • The structure of chiriquitoxin from the Costa Rican frog Atelopus chriquiensis
    • Yotsu M., Yasumoto T., Kim Y.H., Naoki H., Kao C.Y. The structure of chiriquitoxin from the Costa Rican frog Atelopus chriquiensis. Tetrahedron Lett. 1990, 31:3187-3190.
    • (1990) Tetrahedron Lett. , vol.31 , pp. 3187-3190
    • Yotsu, M.1    Yasumoto, T.2    Kim, Y.H.3    Naoki, H.4    Kao, C.Y.5
  • 180
    • 15244344363 scopus 로고    scopus 로고
    • The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis
    • re15
    • Yu F.W., Catterall W.A. The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis. Sci. STKE 2004, re15:1-17.
    • (2004) Sci. STKE , pp. 1-17
    • Yu, F.W.1    Catterall, W.A.2
  • 181
    • 82655168258 scopus 로고    scopus 로고
    • Isolation and identification of a new tetrodotoxin-producing bacterial species, Raoultella terrigena, from Hong Kong marine puffer fish Takifugu niphobles
    • Yu V.C.-H., Yu P.H.-F., Ho K.-C., Lee F.W.-F. Isolation and identification of a new tetrodotoxin-producing bacterial species, Raoultella terrigena, from Hong Kong marine puffer fish Takifugu niphobles. Mar. Drugs 2011, 9:2384-2396.
    • (2011) Mar. Drugs , vol.9 , pp. 2384-2396
    • Yu, V.C.-H.1    Yu, P.H.-F.2    Ho, K.-C.3    Lee, F.W.-F.4
  • 182
    • 79952849568 scopus 로고    scopus 로고
    • Expansion of voltage-dependent Na+ channel gene family in early tetrapods coincided with the emergence of terrestriality and increased brain complexity
    • Zakon H.H., Jost M.C., Lu Y. Expansion of voltage-dependent Na+ channel gene family in early tetrapods coincided with the emergence of terrestriality and increased brain complexity. Mol. Biol. Evol. 2011, 28:1415-1424.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 1415-1424
    • Zakon, H.H.1    Jost, M.C.2    Lu, Y.3
  • 183
    • 37549010308 scopus 로고    scopus 로고
    • Neuroecology, chemical defense, and the keystone species concept
    • Zimmer R.K., Ferrer R.P. Neuroecology, chemical defense, and the keystone species concept. Biol. Bull. 2007, 213:208-225.
    • (2007) Biol. Bull. , vol.213 , pp. 208-225
    • Zimmer, R.K.1    Ferrer, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.