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Volumn 15, Issue 7, 2015, Pages 581-603

Organic toxins as tools to understand ion channel mechanisms and structure

Author keywords

Gating modifiers; Ion channels; Ligand gated channels; Pore blockers; Structure function; Toxin; Voltage gated channel

Indexed keywords

BLOCKING AGENT; CALCIUM CHANNEL BLOCKING AGENT; CHOLINERGIC RECEPTOR; CIGUATOXIN; CONE SNAIL TOXIN; ION CHANNEL; ION TRANSPORT AFFECTING AGENT; KV CHANNEL INTERACTING PROTEIN; LIGAND GATED ION CHANNEL; MECHANO SENSITIVE ION CHANNEL; POTASSIUM CHANNEL; RESINIFERATOXIN; SCORPION VENOM; SEA ANEMONE TOXIN; SNAKE VENOM; SODIUM CHANNEL; SODIUM CHANNEL BLOCKING AGENT; SPIDER VENOM; TETRODOTOXIN; TOXIN; UNCLASSIFIED DRUG; VANILLOID RECEPTOR 1; VANILLOID RECEPTOR ANTAGONIST; VENOM; VOLTAGE GATED ION CHANNEL; LIGAND; PROTEIN SUBUNIT;

EID: 84930982023     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026615666150217110710     Document Type: Article
Times cited : (16)

References (297)
  • 2
    • 33747646924 scopus 로고    scopus 로고
    • An overview of the potassium channel family
    • REVIEWS 0004
    • Miller, C. An overview of the potassium channel family. Genome. Biol, 2000, 1(4), REVIEWS 0004.
    • (2000) Genome. Biol , vol.1 , Issue.4
    • Miller, C.1
  • 3
    • 0037104657 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation
    • Bhave, G.; Zhu, W.; Wang, H.; Brasier, D. J.; Oxford, G. S.; Gereau, R. W.; t. cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation. Neuron, 2002, 35(4), 721-31.
    • (2002) Neuron , vol.35 , Issue.4 , pp. 721-731
    • Bhave, G.1    Zhu, W.2    Wang, H.3    Brasier, D.J.4    Oxford, G.S.5    Gereau, R.W.T.6
  • 5
    • 84931000584 scopus 로고    scopus 로고
    • Redox Regulation of Ion Channels in the Pulmonary Circulation
    • Olschewski, A.; Weir, E. K. Redox Regulation of Ion Channels in the Pulmonary Circulation. Antioxid. Redox. Signal., 2014.
    • (2014) Antioxid. Redox. Signal
    • Olschewski, A.1    Weir, E.K.2
  • 6
    • 84862970522 scopus 로고    scopus 로고
    • An extracellular domain of the accessory beta1 subunit is required for modulating BK channel voltage sensor and gate
    • Gruslova, A.; Semenov, I.; Wang, B. An extracellular domain of the accessory beta1 subunit is required for modulating BK channel voltage sensor and gate. J. Gen. Physiol., 2012, 139(1), 57-67.
    • (2012) J. Gen. Physiol , vol.139 , Issue.1 , pp. 57-67
    • Gruslova, A.1    Semenov, I.2    Wang, B.3
  • 7
    • 84859159873 scopus 로고    scopus 로고
    • Voltage-gated sodium channel-associated proteins and alternative mechanisms of inactivation and block
    • Goldfarb, M. Voltage-gated sodium channel-associated proteins and alternative mechanisms of inactivation and block. Cell. Mol. Life Sci., 2012, 69(7), 1067-76.
    • (2012) Cell. Mol. Life Sci , vol.69 , Issue.7 , pp. 1067-1076
    • Goldfarb, M.1
  • 9
    • 27344442574 scopus 로고    scopus 로고
    • Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane
    • Lee, S. Y.; Lee A.; Chen, J.; MacKinnon, R. Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc. Natl. Acad. Sci. U S A, 2005, 102(43), 15441-6.
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , Issue.43 , pp. 15441-15446
    • Lee, S.Y.1    Lee, A.2    Chen, J.3    McKinnon, R.4
  • 10
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S. B.; Campbell, E. B.; Mackinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science, 2005, 309(5736), 897-903.
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 11
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla, F. The voltage sensor in voltage-dependent ion channels. Physiol. Rev., 2000, 80(2), 555-92.
    • (2000) Physiol. Rev , vol.80 , Issue.2 , pp. 555-592
    • Bezanilla, F.1
  • 14
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2. 0 A resolution
    • Zhou, Y.; Morais-Cabral, J. H.; Kaufman, A.; MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2. 0 A resolution. Nature, 2001, 414(6859), 43-8.
    • (2001) Nature , vol.414 , Issue.6859 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    McKinnon, R.4
  • 15
    • 0035132981 scopus 로고    scopus 로고
    • Mechanisms of permeation and selectivity in calcium channels
    • Corry, B.; Allen, T. W.; Kuyucak, S.; Chung, S. H. Mechanisms of permeation and selectivity in calcium channels. Biophys. J., 2001, 80(1), 195-214.
    • (2001) Biophys. J , vol.80 , Issue.1 , pp. 195-214
    • Corry, B.1    Allen, T.W.2    Kuyucak, S.3    Chung, S.H.4
  • 16
    • 84861119854 scopus 로고    scopus 로고
    • On conduction in a bacterial sodium channel
    • Furini, S.; Domene, C. On conduction in a bacterial sodium channel. PLoS Comput. Biol., 2012, 8(4), e1002476.
    • (2012) PLoS Comput. Biol , vol.8 , Issue.4
    • Furini, S.1    Domene, C.2
  • 17
    • 0026166997 scopus 로고
    • Structure and function of voltage-gated sodium and calcium channels
    • Catterall, W. A. Structure and function of voltage-gated sodium and calcium channels. Curr. Opin. Neurobiol., 1991, 1(1), 5-13.
    • (1991) Curr. Opin. Neurobiol , vol.1 , Issue.1 , pp. 5-13
    • Catterall, W.A.1
  • 18
    • 0029026638 scopus 로고
    • Structure and function of voltage-gated ion channels
    • Catterall, W. A. Structure and function of voltage-gated ion channels. Annu. Rev. Biochem., 1995, 64, 493-531.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 493-531
    • 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, 2012, 590(Pt 11), 2577-89.
    • (2012) J. Physiol , vol.590 , pp. 2577-2589
    • Catterall, W.A.1
  • 20
    • 0023041553 scopus 로고
    • Purified dihydropyridine-binding site from skeletal muscle t-tubules is a functional calcium channel
    • Flockerzi, V.; Oeken, H. J.; Hofmann, F.; Pelzer, D.; Cavalie, A.; Trautwein, W. Purified dihydropyridine-binding site from skeletal muscle t-tubules is a functional calcium channel. Nature, 1986, 323(6083), 66-8.
    • (1986) Nature , vol.323 , Issue.6083 , pp. 66-68
    • Flockerzi, V.1    Oeken, H.J.2    Hofmann, F.3    Pelzer, D.4    Cavalie, A.5    Trautwein, W.6
  • 21
    • 0021280174 scopus 로고
    • Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules
    • Curtis, B. M.; Catterall, W. A. Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules. Biochemistry, 1984, 23(10), 2113-8.
    • (1984) Biochemistry , vol.23 , Issue.10 , pp. 2113-2118
    • Curtis, B.M.1    Catterall, W.A.2
  • 22
    • 0023668412 scopus 로고
    • Photoaffinity labelling and phosphorylation of a 165 kilodalton peptide associated with dihydropyridine and phenylalkylamine-sensitive calcium channels
    • Hosey, M. M.; Barhanin, J.; Schmid, A.; Vandaele, S.; Ptasienski, J.; O'Callahan, C.; Cooper, C.; Lazdunski, M. Photoaffinity labelling and phosphorylation of a 165 kilodalton peptide associated with dihydropyridine and phenylalkylamine-sensitive calcium channels. Biochem. Biophys. Res. Commun., 1987, 147(3), 1137-45.
    • (1987) Biochem. Biophys. Res. Commun , vol.147 , Issue.3 , pp. 1137-1145
    • Hosey, M.M.1    Barhanin, J.2    Schmid, A.3    Vandaele, S.4    Ptasienski, J.5    O'Callahan, C.6    Cooper, C.7    Lazdunski, M.8
  • 23
    • 0023655094 scopus 로고
    • Structural characterization of the 1, 4-dihydropyridine receptor of the voltage-dependent Ca2+ channel from rabbit skeletal muscle. Evidence for two distinct high molecular weight subunits
    • Leung, A. T.; Imagawa, T.; Campbell, K. P. Structural characterization of the 1, 4-dihydropyridine receptor of the voltage-dependent Ca2+ channel from rabbit skeletal muscle. Evidence for two distinct high molecular weight subunits. J. Biol. Chem., 1987, 262(17), 7943-6.
    • (1987) J. Biol. Chem , vol.262 , Issue.17 , pp. 7943-7946
    • Leung, A.T.1    Imagawa, T.2    Campbell, K.P.3
  • 24
    • 0023094034 scopus 로고
    • Photoaffinity labelling of the phenylalkylamine receptor of the skeletal muscle transverse-tubule calcium channel
    • Striessnig, J.; Knaus, H. G.; Grabner, M.; Moosburger, K.; Seitz, W.; Lietz, H.; Glossmann, H. Photoaffinity labelling of the phenylalkylamine receptor of the skeletal muscle transverse-tubule calcium channel. FEBS. Lett., 1987, 212(2), 247-53.
    • (1987) FEBS. Lett , vol.212 , Issue.2 , pp. 247-253
    • Striessnig, J.1    Knaus, H.G.2    Grabner, M.3    Moosburger, K.4    Seitz, W.5    Lietz, H.6    Glossmann, H.7
  • 26
    • 0029933658 scopus 로고    scopus 로고
    • Identification of three subunits of the high affinity omega-conotoxin MVIIC-sensitive Ca2+ channel
    • Liu, H.; De, Waard M.; Scott, V. E.; Gurnett, C. A.; Lennon, V. A.; Campbell, K. P. Identification of three subunits of the high affinity omega-conotoxin MVIIC-sensitive Ca2+ channel. J. Biol. Chem., 1996, 271(23), 13804-10.
    • (1996) J. Biol. Chem , vol.271 , Issue.23 , pp. 13804-13810
    • Liu, H.1    De Waard, M.2    Scott, V.E.3    Gurnett, C.A.4    Lennon, V.A.5    Campbell, K.P.6
  • 27
    • 0029066351 scopus 로고
    • Properties of omega conotoxin MVIIC receptors associated with alpha 1A calcium channel subunits in rat brain
    • Martin-Moutot, N.; Leveque, C.; Sato, K.; Kato, R.; Takahashi, M.; Seagar, M. Properties of omega conotoxin MVIIC receptors associated with alpha 1A calcium channel subunits in rat brain. FEBS. Lett., 1995, 366(1), 21-5.
    • (1995) FEBS. Lett , vol.366 , Issue.1 , pp. 21-25
    • Martin-Moutot, N.1    Leveque, C.2    Sato, K.3    Kato, R.4    Takahashi, M.5    Seagar, M.6
  • 28
    • 0026408918 scopus 로고
    • Evidence for subtypes of the omega-conotoxin GVIA receptor. Identification of the properties intrinsic to the high-affinity receptor
    • McEnery, M. W.; Snowman, A. M.; Snyder, S. H. Evidence for subtypes of the omega-conotoxin GVIA receptor. Identification of the properties intrinsic to the high-affinity receptor. Ann. N. Y. Acad. Sci., 1991, 635, 435-7.
    • (1991) Ann. N.Y. Acad. Sci , vol.635 , pp. 435-437
    • McEnery, M.W.1    Snowman, A.M.2    Snyder, S.H.3
  • 29
    • 0028978246 scopus 로고
    • Association of native Ca2+ channel beta subunits with the alpha 1 subunit interaction domain
    • Witcher, D. R.; De, Waard M.; Liu, H.; Pragnell, M.; Campbell, K. P. Association of native Ca2+ channel beta subunits with the alpha 1 subunit interaction domain. J. Biol. Chem., 1995, 270(30), 18088-93.
    • (1995) J. Biol. Chem , vol.270 , Issue.30 , pp. 18088-18093
    • Witcher, D.R.1    De Waard, M.2    Liu, H.3    Pragnell, M.4    Campbell, K.P.5
  • 30
    • 0034518423 scopus 로고    scopus 로고
    • Structure and regulation of voltage-gated Ca2+ channels
    • Catterall, W. A. Structure and regulation of voltage-gated Ca2+ channels. Annu. Rev. Cell. Dev. Biol., 2000, 16, 521-55.
    • (2000) Annu. Rev. Cell. Dev. Biol , vol.16 , pp. 521-555
    • Catterall, W.A.1
  • 31
    • 0345490949 scopus 로고    scopus 로고
    • International Union of Pharmacology. XL. Compendium of voltagegated ion channels: Calcium channels
    • Catterall, W. A.; Striessnig, J.; Snutch, T. P.; Perez-Reyes, E. International Union of Pharmacology. XL. Compendium of voltagegated ion channels: calcium channels. Pharmacol. Rev., 2003, 55, 579-81.
    • (2003) Pharmacol. Rev , vol.55 , pp. 579-581
    • Catterall, W.A.1    Striessnig, J.2    Snutch, T.P.3    Perez-Reyes, E.4
  • 34
    • 84885615091 scopus 로고    scopus 로고
    • Coarse architecture of the transient receptor potential vanilloid 1 (TRPV1) ion channel determined by fluorescence resonance energy transfer
    • De-la-Rosa, V.; Rangel-Yescas, G. E.; Ladron-de-Guevara, E.; Rosenbaum, T.; Islas, L. D. Coarse architecture of the transient receptor potential vanilloid 1 (TRPV1) ion channel determined by fluorescence resonance energy transfer. J. Biol. Chem., 2013, 288(41), 29506-17.
    • (2013) J. Biol. Chem , vol.288 , Issue.41 , pp. 29506-29517
    • De-la-Rosa, V.1    Rangel-Yescas, G.E.2    Ladron-de-Guevara, E.3    Rosenbaum, T.4    Islas, L.D.5
  • 35
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E.; Liao, M.; Cheng, Y.; Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature, 2013, 504(7478), 113-8.
    • (2013) Nature , vol.504 , Issue.7478 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 36
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M.; Cao, E.; Julius, D.; Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature, 2013, 504(7478), 107-12.
    • (2013) Nature , vol.504 , Issue.7478 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 37
    • 34548362105 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptors: Mutant mice provide new insights for drug development
    • Wess, J.; Eglen, R. M.; Gautam, D. Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development. Nat. Rev. Drug Discov., 2007, 6(9), 721-33.
    • (2007) Nat. Rev. Drug Discov , vol.6 , Issue.9 , pp. 721-733
    • Wess, J.1    Eglen, R.M.2    Gautam, D.3
  • 38
    • 0016167648 scopus 로고
    • The density of acetylcholine receptors and their sensitivity in the postsynaptic membrane of muscle endplates
    • Albuquerque, E. X.; Barnard, E. A.; Porter, C. W.; Warnick, J. E. The density of acetylcholine receptors and their sensitivity in the postsynaptic membrane of muscle endplates. Proc. Natl. Acad. Sci. U S A, 1974, 71(7), 2818-22.
    • (1974) Proc. Natl. Acad. Sci. U S A , vol.71 , Issue.7 , pp. 2818-2822
    • Albuquerque, E.X.1    Barnard, E.A.2    Porter, C.W.3    Warnick, J.E.4
  • 39
    • 0033173332 scopus 로고    scopus 로고
    • Ultrastructural localization of the alpha4-subunit of the neuronal acetylcholine nicotinic receptor in the rat substantia nigra
    • Arroyo-Jim nez, M. M.; Bourgeois, J. P.; Marubio, L. M.; Le, Sourd A. M.; Ottersen, O. P.; Rinvik, E.; Fairen, A.; Changeux, J. P. Ultrastructural localization of the alpha4-subunit of the neuronal acetylcholine nicotinic receptor in the rat substantia nigra. J. Neurosci., 1999, 19(15), 6475-87.
    • (1999) J. Neurosci , vol.19 , Issue.15 , pp. 6475-6487
    • Arroyo-Jim nez, M.M.1    Bourgeois, J.P.2    Marubio, L.M.3    Le Sourd, A.M.4    Ottersen, O.P.5    Rinvik, E.6    Fairen, A.7    Changeux, J.P.8
  • 40
    • 0021909380 scopus 로고
    • Nicotinic binding in rat brain: Autoradiographic comparison of [3H]acetylcholine, [3H]nicotine, and [125I]-alpha-bungarotoxin
    • Clarke, P. B.; Schwartz, R. D.; Paul, S. M.; Pert, C. B.; Pert, A. Nicotinic binding in rat brain: autoradiographic comparison of [3H]acetylcholine, [3H]nicotine, and [125I]-alpha-bungarotoxin. J. Neurosci., 1985, 5(5), 1307-15.
    • (1985) J. Neurosci , vol.5 , Issue.5 , pp. 1307-1315
    • Clarke, P.B.1    Schwartz, R.D.2    Paul, S.M.3    Pert, C.B.4    Pert, A.5
  • 41
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A. Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci., 2002, 3(2), 102-14.
    • (2002) Nat. Rev. Neurosci , vol.3 , Issue.2 , pp. 102-114
    • Karlin, A.1
  • 42
    • 58249113980 scopus 로고    scopus 로고
    • Mammalian nicotinic acetylcholine receptors: From structure to function
    • Albuquerque, E. X.; Pereira, E. F.; Alkondon, M.; Rogers, S. W. Mammalian nicotinic acetylcholine receptors: from structure to function. Physiol. Rev., 2009, 89(1), 73-120.
    • (2009) Physiol. Rev , vol.89 , Issue.1 , pp. 73-120
    • Albuquerque, E.X.1    Pereira, E.F.2    Alkondon, M.3    Rogers, S.W.4
  • 43
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 A resolution
    • Unwin, N. Nicotinic acetylcholine receptor at 9 A resolution. J. Mol. Biol., 1993, 229(4), 1101-24.
    • (1993) J. Mol. Biol , vol.229 , Issue.4 , pp. 1101-1124
    • Unwin, N.1
  • 44
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4. 6 A resolution: Transverse tunnels in the cannel wall
    • Miyazawa, A.; Fujiyoshi, Y.; Stowell, M.; Unwin, N. Nicotinic acetylcholine receptor at 4. 6 A resolution: transverse tunnels in the cannel wall. J. Mol. Biol., 1999, 288(4), 765-86.
    • (1999) J. Mol. Biol , vol.288 , Issue.4 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 45
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A.; Fujiyoshi, Y.; Unwin, N. Structure and gating mechanism of the acetylcholine receptor pore. Nature, 2003, 423(6943), 949-55.
    • (2003) Nature , vol.423 , Issue.6943 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 46
    • 84887007845 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: Insights from Torpedo postsynaptic membranes
    • Unwin, N. Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes. Q. Rev. Biophys., 2013, 46(4), 283-322.
    • (2013) Q. Rev. Biophys , vol.46 , Issue.4 , pp. 283-322
    • Unwin, N.1
  • 47
    • 0031870973 scopus 로고    scopus 로고
    • Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism
    • Auerbach, A.; Akk, G. Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism. J. Gen. Physiol., 1998, 112(2), 181-97.
    • (1998) J. Gen. Physiol , vol.112 , Issue.2 , pp. 181-197
    • Auerbach, A.1    Akk, G.2
  • 48
    • 0029153305 scopus 로고
    • Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: Mutations of alpha-subunit tyrosine 190 affect both binding and gating
    • Chen, J.; Zhang, Y.; Akk, G.; Sine, S.; Auerbach, A. Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of alpha-subunit tyrosine 190 affect both binding and gating. Biophys. J., 1995, 69(3), 849-59.
    • (1995) Biophys. J , vol.69 , Issue.3 , pp. 849-859
    • Chen, J.1    Zhang, Y.2    Akk, G.3    Sine, S.4    Auerbach, A.5
  • 49
    • 0029934560 scopus 로고    scopus 로고
    • Voltage dependence of mouse acetylcholine receptor gating: Different charge movements in di-, mono-and unliganded receptors
    • Auerbach, A.; Sigurdson, W.; Chen, J.; Akk, G. Voltage dependence of mouse acetylcholine receptor gating: different charge movements in di-, mono-and unliganded receptors. J. Physiol., 1996, 494 (Pt 1), 155-70.
    • (1996) J. Physiol , vol.494 , pp. 155-170
    • Auerbach, A.1    Sigurdson, W.2    Chen, J.3    Akk, G.4
  • 51
    • 0035886019 scopus 로고    scopus 로고
    • Ultrastructural distribution of the alpha7 nicotinic acetylcholine receptor subunit in rat hippocampus
    • Fabian-Fine R.; Skehel, P.; Errington, M. L.; Davies, H. A.; Sher, E.; Stewart, M. G.; Fine A. Ultrastructural distribution of the alpha7 nicotinic acetylcholine receptor subunit in rat hippocampus. J. Neurosci., 2001, 21(20), 7993-8003.
    • (2001) J. Neurosci , vol.21 , Issue.20 , pp. 7993-8003
    • Fabian-Fine, R.1    Skehel, P.2    Errington, M.L.3    Davies, H.A.4    Sher, E.5    Stewart, M.G.6    Fine, A.7
  • 52
    • 0030777012 scopus 로고    scopus 로고
    • The capsaicin receptor: A heat-activated ion channel in the pain pathway
    • Caterina, M. J.; Schumacher, M. A.; Tominaga, M.; Rosen, T. A.; Levine, J. D.; Julius, D. The capsaicin receptor: a heat-activated ion channel in the pain pathway. Nature, 1997, 389(6653), 816-24.
    • (1997) Nature , vol.389 , Issue.6653 , pp. 816-824
    • Caterina, M.J.1    Schumacher, M.A.2    Tominaga, M.3    Rosen, T.A.4    Levine, J.D.5    Julius, D.6
  • 56
    • 41549103342 scopus 로고    scopus 로고
    • Influence of TRPV1 on diabetes-induced alterations in thermal pain sensitivity
    • Pabbidi, R. M.; Yu, S. Q.; Peng, S.; Khardori, R.; Pauza, M. E.; Premkumar, L. S. Influence of TRPV1 on diabetes-induced alterations in thermal pain sensitivity. Mol. Pain, 2008, 4, 9.
    • (2008) Mol. Pain , vol.4 , pp. 9
    • Pabbidi, R.M.1    Yu, S.Q.2    Peng, S.3    Khardori, R.4    Pauza, M.E.5    Premkumar, L.S.6
  • 57
    • 34250755449 scopus 로고    scopus 로고
    • Expression of transient receptor potential vanilloid 1 (TRPV1) in synovial fibroblasts from patients with osteoarthritis and rheumatoid arthritis
    • Engler, A.; Aeschlimann, A.; Simmen, B. R.; Michel, B. A.; Gay, R. E.; Gay, S.; Sprott, H. Expression of transient receptor potential vanilloid 1 (TRPV1) in synovial fibroblasts from patients with osteoarthritis and rheumatoid arthritis. Biochem. Biophys. Res. Commun., 2007, 359(4), 884-8.
    • (2007) Biochem. Biophys. Res. Commun , vol.359 , Issue.4 , pp. 884-888
    • Engler, A.1    Aeschlimann, A.2    Simmen, B.R.3    Michel, B.A.4    Gay, R.E.5    Gay, S.6    Sprott, H.7
  • 59
    • 78649500338 scopus 로고    scopus 로고
    • Involvement of lysophosphatidic acid in bone cancer pain by potentiation of TRPV1 via PKCepsilon pathway in dorsal root ganglion neurons
    • Pan, H. L.; Zhang, Y. Q.; Zhao, Z. Q. Involvement of lysophosphatidic acid in bone cancer pain by potentiation of TRPV1 via PKCepsilon pathway in dorsal root ganglion neurons. Mol. Pain, 2010, 6, 85.
    • (2010) Mol. Pain , vol.6 , pp. 85
    • Pan, H.L.1    Zhang, Y.Q.2    Zhao, Z.Q.3
  • 60
    • 84904244404 scopus 로고    scopus 로고
    • Spatiotemporal expression and functional involvement of transient receptor potential vanilloid 1 in diabetic mechanical allodynia in rats
    • Cui, Y. Y.; Xu, H.; Wu, H. H.; Qi, J.; Shi, J.; Li, Y. Q. Spatiotemporal expression and functional involvement of transient receptor potential vanilloid 1 in diabetic mechanical allodynia in rats. PLoS One, 2014, 9(7), e102052.
    • (2014) PLoS One , vol.9 , Issue.7
    • Cui, Y.Y.1    Xu, H.2    Wu, H.H.3    Qi, J.4    Shi, J.5    Li, Y.Q.6
  • 61
    • 33846426807 scopus 로고    scopus 로고
    • Mechanosensitive ion channels and the peptide inhibitor GsMTx-4: History, properties, mechanisms and pharmacology
    • Bowman, C. L.; Gottlieb, P. A.; Suchyna, T. M.; Murphy, Y. K.; Sachs, F. Mechanosensitive ion channels and the peptide inhibitor GsMTx-4: history, properties, mechanisms and pharmacology. Toxicon, 2007, 49(2), 249-70.
    • (2007) Toxicon , vol.49 , Issue.2 , pp. 249-270
    • Bowman, C.L.1    Gottlieb, P.A.2    Suchyna, T.M.3    Murphy, Y.K.4    Sachs, F.5
  • 62
    • 34147177561 scopus 로고    scopus 로고
    • Properties and Mechanism of the Mechanosensitive Ion Channel Inhibitor GsMTx4, a Therapeutic Peptide Derived from Tarantula Venom
    • Gottlieb, P. A.; Suchyna, T. M.; Sachs, F. Properties and Mechanism of the Mechanosensitive Ion Channel Inhibitor GsMTx4, a Therapeutic Peptide Derived from Tarantula Venom. Curr. Top. Membr., 2007, 59, 81-109.
    • (2007) Curr. Top. Membr , vol.59 , pp. 81-109
    • Gottlieb, P.A.1    Suchyna, T.M.2    Sachs, F.3
  • 63
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill, O. P.; Martinac, B. Molecular basis of mechanotransduction in living cells. Physiol. Rev., 2001, 81(2), 685-740.
    • (2001) Physiol. Rev , vol.81 , Issue.2 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 64
    • 0025081008 scopus 로고
    • Swellinginduced changes in electrophysiological properties of cultured astrocytes and oligodendrocytes. II. Whole-cell currents
    • Kimelberg, H. K. O.; Anderson, E.; Kettenmann, H. Swellinginduced changes in electrophysiological properties of cultured astrocytes and oligodendrocytes. II. Whole-cell currents. Brain Res., 1990, 529(1-2), 262-8.
    • (1990) Brain Res , vol.529 , Issue.1-2 , pp. 262-268
    • Kimelberg, H.K.O.1    Anderson, E.2    Kettenmann, H.3
  • 65
    • 0025425558 scopus 로고
    • Swelling-induced release of glutamate, aspartate, and taurine from astrocyte cultures
    • Kimelberg, H. K.; Goderie, S. K.; Higman, S.; Pang, S.; Waniewski, R. A. Swelling-induced release of glutamate, aspartate, and taurine from astrocyte cultures. J. Neurosci., 1990, 10(5), 1583-91.
    • (1990) J. Neurosci , vol.10 , Issue.5 , pp. 1583-1591
    • Kimelberg, H.K.1    Goderie, S.K.2    Higman, S.3    Pang, S.4    Waniewski, R.A.5
  • 66
    • 0025027363 scopus 로고
    • Swelling-induced changes in electrophysiological properties of cultured astrocytes and oligodendrocytes. I. Effects on membrane potentials, input impedance and cell-cell coupling
    • Kimelberg, H. K., Kettenmann, H. Swelling-induced changes in electrophysiological properties of cultured astrocytes and oligodendrocytes. I. Effects on membrane potentials, input impedance and cell-cell coupling. Brain Res., 1990, 529(1-2), 255-61.
    • (1990) Brain Res , vol.529 , Issue.1-2 , pp. 255-261
    • Kimelberg, H.K.1    Kettenmann, H.2
  • 67
    • 3042853029 scopus 로고    scopus 로고
    • Mechanosensitive ion channels: Molecules of mechanotransduction
    • Martinac, B. Mechanosensitive ion channels: molecules of mechanotransduction. J. Cell Sci., 2004, 117(Pt 12), 2449-60.
    • (2004) J. Cell Sci , vol.117 , pp. 2449-2460
    • Martinac, B.1
  • 68
    • 84885596199 scopus 로고    scopus 로고
    • Mechano-gated ion channels in sensory systems
    • Delmas, P.; Coste, B. Mechano-gated ion channels in sensory systems. Cell, 2013, 155(2), 278-84.
    • (2013) Cell , vol.155 , Issue.2 , pp. 278-284
    • Delmas, P.1    Coste, B.2
  • 69
    • 84908208511 scopus 로고    scopus 로고
    • The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct beta Sandwich Fold
    • Kamajaya, A.; Kaiser, J. T.; Lee, J.; Reid, M.; Rees, D. C. The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct beta Sandwich Fold. Structure, 2014, 22(10), 1520-7.
    • (2014) Structure , vol.22 , Issue.10 , pp. 1520-1527
    • Kamajaya, A.1    Kaiser, J.T.2    Lee, J.3    Reid, M.4    Rees, D.C.5
  • 70
    • 0026595617 scopus 로고    scopus 로고
    • P-type calcium channels blocked by the spider toxin omega-Aga-IVA
    • Mintz, I. M.; Venema, V. J.; Swiderek, K. M.; Lee, T. D.; Bean, B. P.; Adams, M. E. P-type calcium channels blocked by the spider toxin omega-Aga-IVA. Nature, 199, 355(6363), 827-9.
    • Nature , vol.199-355 , Issue.6363 , pp. 827-829
    • Mintz, I.M.1    Venema, V.J.2    Swiderek, K.M.3    Lee, T.D.4    Bean, B.P.5    Adams, M.E.6
  • 71
    • 0018873513 scopus 로고
    • Neurotoxins that act on voltage-sensitive sodium channels in excitable membranes
    • Catterall, W. A. Neurotoxins that act on voltage-sensitive sodium channels in excitable membranes. Annu. Rev. Pharmacol. Toxicol., 1980, 20, 15-43.
    • (1980) Annu. Rev. Pharmacol. Toxicol , vol.20 , pp. 15-43
    • Catterall, W.A.1
  • 72
    • 0028983387 scopus 로고
    • The charybdotoxin family of K+ channel-blocking peptides
    • Miller, C. The charybdotoxin family of K+ channel-blocking peptides. Neuron, 1995, 15(1), 5-10.
    • (1995) Neuron , vol.15 , Issue.1 , pp. 5-10
    • Miller, C.1
  • 73
    • 77951558539 scopus 로고    scopus 로고
    • Use of venom peptides to probe ion channel structure and function
    • Dutertre, S.; Lewis, R. J. Use of venom peptides to probe ion channel structure and function. J. Biol. Chem., 2010, 285(18), 13315-20.
    • (2010) J. Biol. Chem , vol.285 , Issue.18 , pp. 13315-13320
    • Dutertre, S.1    Lewis, R.J.2
  • 76
    • 84870549155 scopus 로고    scopus 로고
    • Scorpion toxins specific for potassium (K+) channels: A historical overview of peptide bioengineering
    • Bergeron, Z. L.; Bingham, J. P. Scorpion toxins specific for potassium (K+) channels: a historical overview of peptide bioengineering. Toxins (Basel), 2012, 4(11), 1082-119.
    • (2012) Toxins (Basel) , vol.4 , Issue.11 , pp. 1082-1119
    • Bergeron, Z.L.1    Bingham, J.P.2
  • 77
    • 0037999227 scopus 로고    scopus 로고
    • Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: Selectivity between voltage-gated and Maxi-K channels
    • Gao, Y. D.; Garcia, M. L. Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: selectivity between voltage-gated and Maxi-K channels. Proteins, 2003, 52(2), 146-54.
    • (2003) Proteins , vol.52 , Issue.2 , pp. 146-154
    • Gao, Y.D.1    Garcia, M.L.2
  • 78
    • 6944247603 scopus 로고    scopus 로고
    • Mapping of maurotoxin binding sites on hKv1. 2, hKv1. 3, and hIKCa1 channels
    • Visan, V.; Fajloun, Z.; Sabatier, J. M.; Grissmer, S. Mapping of maurotoxin binding sites on hKv1. 2, hKv1. 3, and hIKCa1 channels. Mol. Pharmacol., 2004, 66(5), 1103-12.
    • (2004) Mol. Pharmacol , vol.66 , Issue.5 , pp. 1103-1112
    • Visan, V.1    Fajloun, Z.2    Sabatier, J.M.3    Grissmer, S.4
  • 80
    • 0025055598 scopus 로고
    • Omega-agatoxins: Novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom
    • Adams, M. E.; Bindokas, V. P.; Hasegawa, L.; Venema, V. J. Omega-agatoxins: novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom. J. boil. Chem., 1990, 265(2), 861-7.
    • (1990) J. boil. Chem , vol.265 , Issue.2 , pp. 861-867
    • Adams, M.E.1    Bindokas, V.P.2    Hasegawa, L.3    Venema, V.J.4
  • 81
    • 28244475780 scopus 로고    scopus 로고
    • An inhibitor of TRPV1 channels isolated from funnel Web spider venom
    • Kitaguchi, T.; Swartz, K. J. An inhibitor of TRPV1 channels isolated from funnel Web spider venom. Biochemistry, 2005, 44(47), 15544-9.
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15544-15549
    • Kitaguchi, T.1    Swartz, K.J.2
  • 82
    • 1942438979 scopus 로고    scopus 로고
    • Agatoxins: Ion channel specific toxins from the American funnel web spider, Agelenopsis aperta
    • Adams, M. E. Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta. TOXICON: J. I. S. T. 2004, 43(5), 509-25.
    • (2004) TOXICON: J.I.S.T , vol.43 , Issue.5 , pp. 509-525
    • Adams, M.E.1
  • 83
    • 33847403885 scopus 로고    scopus 로고
    • Modulation of insect Ca(v) channels by peptidic spider toxins
    • King, G. F. Modulation of insect Ca(v) channels by peptidic spider toxins. Toxicon: J. I. S. T., 2007, 49(4), 513-30.
    • (2007) Toxicon: J.I.S.T , vol.49 , Issue.4 , pp. 513-530
    • King, G.F.1
  • 84
    • 79952130482 scopus 로고    scopus 로고
    • Peptide neurotoxins that affect voltage-gated calcium channels: A close-up on ω-agatoxins
    • Pringos, E.; Vignes, M.; Martinez, J.; Rolland, V. Peptide neurotoxins that affect voltage-gated calcium channels: a close-up on ω-agatoxins. Toxins, 2011, 3(1), 17-42.
    • (2011) Toxins , vol.3 , Issue.1 , pp. 17-42
    • Pringos, E.1    Vignes, M.2    Martinez, J.3    Rolland, V.4
  • 85
    • 0028725229 scopus 로고
    • Structure-activity relationships for P-type calcium channelselective omega-agatoxins
    • Reily, M. D.; Holub, K. E.; Gray, W. R.; Norris, T. M.; Adams, M. E. Structure-activity relationships for P-type calcium channelselective omega-agatoxins. Nat. Struct. Biol., 1994, 1(12), 853-6.
    • (1994) Nat. Struct. Biol , vol.1 , Issue.12 , pp. 853-856
    • Reily, M.D.1    Holub, K.E.2    Gray, W.R.3    Norris, T.M.4    Adams, M.E.5
  • 86
    • 0028171637 scopus 로고
    • Omega-agatoxin-TK containing D-serine at position 46, but not synthetic omega-[L-Ser46]agatoxin-TK, exerts blockade of P-type calcium channels in cerebellar Purkinje neurons
    • Kuwada, M.; Teramoto, T.; Kumagaye, K. Y.; Nakajima, K.; Watanabe, T.; Kawai, T.; Kawakami, Y.; Niidome, T.; Sawada, K.; Nishizawa, Y. Omega-agatoxin-TK containing D-serine at position 46, but not synthetic omega-[L-Ser46]agatoxin-TK, exerts blockade of P-type calcium channels in cerebellar Purkinje neurons. Mol. Pharmacol., 1994, 46(4), 587-93.
    • (1994) Mol. Pharmacol , vol.46 , Issue.4 , pp. 587-593
    • Kuwada, M.1    Teramoto, T.2    Kumagaye, K.Y.3    Nakajima, K.4    Watanabe, T.5    Kawai, T.6    Kawakami, Y.7    Niidome, T.8    Sawada, K.9    Nishizawa, Y.10
  • 87
    • 0344256589 scopus 로고    scopus 로고
    • Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels
    • Lee, H. C.; Wang, J. M.; Swartz, K. J. Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels. Neuron, 2003, 40(3), 527-36.
    • (2003) Neuron , vol.40 , Issue.3 , pp. 527-536
    • Lee, H.C.1    Wang, J.M.2    Swartz, K.J.3
  • 88
    • 33846444703 scopus 로고    scopus 로고
    • Tarantula toxins interacting with voltage sensors in potassium channels
    • Swartz, K. J. Tarantula toxins interacting with voltage sensors in potassium channels. Toxicon: I. T. S., 2007, 49(2), 213-30.
    • (2007) Toxicon: I.T.S , vol.49 , Issue.2 , pp. 213-230
    • Swartz, K.J.1
  • 89
    • 0034103610 scopus 로고    scopus 로고
    • Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels
    • Suchyna, T. M.; Johnson, J. H.; Hamer, K.; Leykam, J. F.; Gage, D. A.; Clemo, H. F.; Baumgarten, C. M.; Sachs, F. Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels. J. Gen. Physiol., 2000, 115(5), 583-98.
    • (2000) J. Gen. Physiol , vol.115 , Issue.5 , pp. 583-598
    • Suchyna, T.M.1    Johnson, J.H.2    Hamer, K.3    Leykam, J.F.4    Gage, D.A.5    Clemo, H.F.6    Baumgarten, C.M.7    Sachs, F.8
  • 91
    • 77953271751 scopus 로고    scopus 로고
    • A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain
    • Bohlen, C. J.; Priel, A.; Zhou, S.; King, D.; Siemens, J.; Julius D. A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain. Cell, 2010, 141(5), 834-45.
    • (2010) Cell , vol.141 , Issue.5 , pp. 834-845
    • Bohlen, C.J.1    Priel, A.2    Zhou, S.3    King, D.4    Siemens, J.5    Julius, D.6
  • 92
    • 33845992556 scopus 로고    scopus 로고
    • Conus peptides: Biodiversity-based discovery and exogenomics
    • Olivera, B. M. Conus peptides: biodiversity-based discovery and exogenomics. J. biol. chem., 2006, 281(42), 31173-7.
    • (2006) J. biol. chem , vol.281 , Issue.42 , pp. 31173-31177
    • Olivera, B.M.1
  • 93
    • 35349014163 scopus 로고    scopus 로고
    • Diversity of the neurotoxic Conus peptides: A model for concerted pharmacological discovery
    • Olivera, B. M.; Teichert, R. W. Diversity of the neurotoxic Conus peptides: a model for concerted pharmacological discovery. Mol. Interventions, 2007, 7(5), 251-60.
    • (2007) Mol. Interventions , vol.7 , Issue.5 , pp. 251-260
    • Olivera, B.M.1    Teichert, R.W.2
  • 94
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • Terlau, H.; Olivera, B. M. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol. Rev., 2004, 84(1), 41-68.
    • (2004) Physiol. Rev , vol.84 , Issue.1 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 95
    • 33847411379 scopus 로고    scopus 로고
    • Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na+ channels
    • Bosmans, F.; Tytgat, J. Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na+ channels. Toxicon, 2007, 49(4), 550-60.
    • (2007) Toxicon , vol.49 , Issue.4 , pp. 550-560
    • Bosmans, F.1    Tytgat, J.2
  • 96
    • 33144485759 scopus 로고    scopus 로고
    • Peptide toxins in sea anemones: Structural and functional aspects
    • Honma, T.; Shiomi, K. Peptide toxins in sea anemones: structural and functional aspects. Marine biotechnology (New York, N. Y.), 2006, 8, 1-10.
    • (2006) Marine biotechnology (New York, N.Y.) , vol.8 , pp. 1-10
    • Honma, T.1    Shiomi, K.2
  • 97
    • 0019483409 scopus 로고
    • Structure-function relationships of sea anemone toxin II from Anemonia sulcata
    • Barhanin, J.; Hugues, M.; Schweitz, H.; Vincent, J. P.; Lazdunski, M. Structure-function relationships of sea anemone toxin II from Anemonia sulcata. J. Biol. Chem., 1981, 256(11), 5764-9.
    • (1981) J. Biol. Chem , vol.256 , Issue.11 , pp. 5764-5769
    • Barhanin, J.1    Hugues, M.2    Schweitz, H.3    Vincent, J.P.4    Lazdunski, M.5
  • 98
    • 0031972937 scopus 로고    scopus 로고
    • A specific interaction between the cardiac sodium channel and site-3 toxin anthopleurin B
    • Benzinger, G. R.; Kyle, J. W.; Blumenthal, K. M.; Hanck, D. A. A specific interaction between the cardiac sodium channel and site-3 toxin anthopleurin B. J. Biol. Chem., 1998, 273(1), 80-4.
    • (1998) J. Biol. Chem , vol.273 , Issue.1 , pp. 80-84
    • Benzinger, G.R.1    Kyle, J.W.2    Blumenthal, K.M.3    Hanck, D.A.4
  • 99
    • 0029911653 scopus 로고    scopus 로고
    • Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurin B
    • Khera, P. K.; Blumenthal, K. M. Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurin B. Biochemistry, 1996, 35(11), 3503-7.
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3503-3507
    • Khera, P.K.1    Blumenthal, K.M.2
  • 100
    • 0021767567 scopus 로고
    • Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones
    • Gooley, P. R.; Blunt, J. W.; Norton, R. S. Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones. FEBS Lett., 1984, 174(1), 15-9.
    • (1984) FEBS Lett , vol.174 , Issue.1 , pp. 15-19
    • Gooley, P.R.1    Blunt, J.W.2    Norton, R.S.3
  • 101
    • 2642553090 scopus 로고    scopus 로고
    • Role of Asn-16 and Ser-19 in anthopleurin B binding. Implications for the electrostatic nature of Na(V) site 3
    • Seibert, A. L.; Liu, J.; Hanck, D. A.; Blumenthal, K. M. Role of Asn-16 and Ser-19 in anthopleurin B binding. Implications for the electrostatic nature of Na(V) site 3. Biochemistry, 2004, 43(22), 7082-9.
    • (2004) Biochemistry , vol.43 , Issue.22 , pp. 7082-7089
    • Seibert, A.L.1    Liu, J.2    Hanck, D.A.3    Blumenthal, K.M.4
  • 103
    • 0037040249 scopus 로고    scopus 로고
    • Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain
    • Racape, J.; Lecoq, A.; Romi-Lebrun, R.; Liu, J.; Kohler, M.; Garcia, M. L.; Menez, A; Gasparini, S. Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain. J. Biol. Chem., 2002, 277(6), 3886-93.
    • (2002) J. Biol. Chem , vol.277 , Issue.6 , pp. 3886-3893
    • Racape, J.1    Lecoq, A.2    Romi-Lebrun, R.3    Liu, J.4    Kohler, M.5    Garcia, M.L.6    Menez, A.7    Gasparini, S.8
  • 104
    • 22844448219 scopus 로고    scopus 로고
    • A variable residue in the pore of Kv1 channels is critical for the high affinity of blockers from sea anemones and scorpions
    • Gilquin, B.; Braud, S.; Eriksson, M. A.; Roux, B.; Bailey, T. D.; Priest, B. T.; Garcia, M. L.; Menez, A.; Gasparini, S. A variable residue in the pore of Kv1 channels is critical for the high affinity of blockers from sea anemones and scorpions. J. Biol. Chem., 2005, 280(29), 27093-102.
    • (2005) J. Biol. Chem , vol.280 , Issue.29 , pp. 27093-27102
    • Gilquin, B.1    Braud, S.2    Eriksson, M.A.3    Roux, B.4    Bailey, T.D.5    Priest, B.T.6    Garcia, M.L.7    Menez, A.8    Gasparini, S.9
  • 105
    • 0023728715 scopus 로고
    • Structure and pharmacology of elapid cytotoxins
    • Dufton, M. J.; Hider, R. C. Structure and pharmacology of elapid cytotoxins. Pharmacol. Ther., 1988, 36(1), 1-40.
    • (1988) Pharmacol. Ther , vol.36 , Issue.1 , pp. 1-40
    • Dufton, M.J.1    Hider, R.C.2
  • 106
    • 0023502533 scopus 로고
    • Current view on the structure-function relationship of postsynaptic neurotoxins from snake venoms
    • Endo T., Tamiya N. Current view on the structure-function relationship of postsynaptic neurotoxins from snake venoms. Pharmacol. Ther., 1987, 34(3), 403-51.
    • (1987) Pharmacol. Ther , vol.34 , Issue.3 , pp. 403-451
    • Endo, T.1    Tamiya, N.2
  • 107
    • 84883837027 scopus 로고
    • Isolation of Neurotoxins from the Venom of Bungarus Multicinctus and Their Modes of Neuromuscular Blocking Action
    • Chang, C. C.; Lee, C. Y. Isolation of Neurotoxins from the Venom of Bungarus Multicinctus and Their Modes of Neuromuscular Blocking Action. Arch. Int. Pharmacodyn. Ther., 1963, 144, 241-57.
    • (1963) Arch. Int. Pharmacodyn. Ther , vol.144 , pp. 241-257
    • Chang, C.C.1    Lee, C.Y.2
  • 109
    • 0022943266 scopus 로고
    • The crystal structure of alphabungarotoxin at 2. 5 A resolution: Relation to solution structure and binding to acetylcholine receptor
    • Love, R. A.; Stroud, R. M. The crystal structure of alphabungarotoxin at 2. 5 A resolution: relation to solution structure and binding to acetylcholine receptor. Protein Eng., 1986, 1(1), 37-46.
    • (1986) Protein Eng , vol.1 , Issue.1 , pp. 37-46
    • Love, R.A.1    Stroud, R.M.2
  • 110
    • 0033168399 scopus 로고    scopus 로고
    • Alpha subunit compositions of Kv1. 1-containing K+ channel subtypes fractionated from rat brain using dendrotoxins
    • Wang, F. C.; Parcej, D. N.; Dolly, J. O. alpha subunit compositions of Kv1. 1-containing K+ channel subtypes fractionated from rat brain using dendrotoxins. Eur. J. Biochem., 1999, 263(1), 230-7.
    • (1999) Eur. J. Biochem , vol.263 , Issue.1 , pp. 230-237
    • Wang, F.C.1    Parcej, D.N.2    Dolly, J.O.3
  • 111
    • 84255169844 scopus 로고    scopus 로고
    • Snake toxins from mamba venoms: Unique tools for the physiologist
    • Rowan, E. G.; Harvey, A. L. Snake toxins from mamba venoms: unique tools for the physiologist. Acta. Chim. Slov., 2011, 58(4), 689-92.
    • (2011) Acta. Chim. Slov , vol.58 , Issue.4 , pp. 689-692
    • Rowan, E.G.1    Harvey, A.L.2
  • 112
    • 4344654516 scopus 로고
    • The constituents of the ovaries of globefish. VIII. Studies on tetrodotoxin
    • Tsuda, K.; Kawamura, M. The constituents of the ovaries of globefish. VIII. Studies on tetrodotoxin. Pharm Bull, 1953, 1(2), 112-3.
    • (1953) Pharm Bull , vol.1 , Issue.2 , pp. 112-113
    • Tsuda, K.1    Kawamura, M.2
  • 113
    • 34250690402 scopus 로고
    • The effect of tetrodotoxin on the neuromuscular junction and peripheral nerve of the toad
    • Matsumura, M.; Yamamoto, S. The effect of tetrodotoxin on the neuromuscular junction and peripheral nerve of the toad. Jpn. J. Pharmacol., 1954, 4(1), 62-8.
    • (1954) Jpn. J. Pharmacol , vol.4 , Issue.1 , pp. 62-68
    • Matsumura, M.1    Yamamoto, S.2
  • 114
    • 0014117811 scopus 로고
    • Tetrodotoxin. It is a powerful poison that is found in two almost totally unrelated kinds of animal: Puffer fish and newts. It has been serving as a tool in nerve physiology and may provide a model for new local anesthetics
    • Fuhrman, F. A. Tetrodotoxin. It is a powerful poison that is found in two almost totally unrelated kinds of animal: puffer fish and newts. It has been serving as a tool in nerve physiology and may provide a model for new local anesthetics. Sci. Am., 1967, 217(2), 60-71.
    • (1967) Sci. Am , vol.217 , Issue.2 , pp. 60-71
    • Fuhrman, F.A.1
  • 115
    • 0025909105 scopus 로고
    • Tetrodotoxin and derivatives in several species of the gastropod Naticidae
    • Hwang, D. F.; Tai, K. P.; Chueh, C. H.; Lin, L. C.; Jeng, S. S. Tetrodotoxin and derivatives in several species of the gastropod Naticidae. Toxicon: J. I. T. S, 1991, 29(8), 1019-24.
    • (1991) Toxicon: J.I.T. S , vol.29 , Issue.8 , pp. 1019-1024
    • Hwang, D.F.1    Tai, K.P.2    Chueh, C.H.3    Lin, L.C.4    Jeng, S.S.5
  • 116
    • 0024377774 scopus 로고
    • Occurrence of tetrodotoxin in the frog Atelopus oxyrhynchus
    • Mebs, D.; Schmidt, K. Occurrence of tetrodotoxin in the frog Atelopus oxyrhynchus. Toxicon: J. I. T. S, 1989, 27(7), 819-22.
    • (1989) Toxicon: J.I.T. S , vol.27 , Issue.7 , pp. 819-822
    • Mebs, D.1    Schmidt, K.2
  • 118
    • 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(6), 1016-24.
    • (2008) Mol. Biol. Evol , vol.25 , Issue.6 , 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
  • 119
    • 17044447156 scopus 로고    scopus 로고
    • TTX resistivity of Na+ channel in newt retinal neuron
    • Kaneko, Y.; Matsumoto, G.; Hanyu, Y. TTX resistivity of Na+ channel in newt retinal neuron. Biochem. Biophys. Res. Commun., 1997, 240(3), 651-6.
    • (1997) Biochem. Biophys. Res. Commun , vol.240 , Issue.3 , pp. 651-656
    • Kaneko, Y.1    Matsumoto, G.2    Hanyu, Y.3
  • 120
    • 39149133187 scopus 로고    scopus 로고
    • Two critical residues in p-loop regions of puffer fish Na+ channels on TTX sensitivity
    • Maruta, S.; Yamaoka, K.; Yotsu-Yamashita M. Two critical residues in p-loop regions of puffer fish Na+ channels on TTX sensitivity. Toxicon: J. I. T. S, 2008, 51(3), 381-7.
    • (2008) Toxicon: J.I.T. S , vol.51 , Issue.3 , pp. 381-387
    • Maruta, S.1    Yamaoka, K.2    Yotsu-Yamashita, M.3
  • 122
    • 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.; Ruben, P. C. Evolutionary diversification of TTX-resistant sodium channels in a predator-prey interaction. Nature, 2005, 434(7034), 759-63.
    • (2005) Nature , vol.434 , Issue.7034 , pp. 759-763
    • Geffeney, S.L.1    Fujimoto, E.2    Brodie, E.D.3    Ruben, P.C.4
  • 123
    • 84868331416 scopus 로고    scopus 로고
    • Expression of Nav1. 7 in DRG neurons extends from peripheral terminals in the skin to central preterminal branches and terminals in the dorsal horn
    • Black, J. A.; Frezel, N.; Dib-Hajj, S. D.; Waxman, S. G. Expression of Nav1. 7 in DRG neurons extends from peripheral terminals in the skin to central preterminal branches and terminals in the dorsal horn. Mol Pain, 2012, 8, 82.
    • (2012) Mol Pain , vol.8 , pp. 82
    • Black, J.A.1    Frezel, N.2    Dib-Hajj, S.D.3    Waxman, S.G.4
  • 124
    • 39149137158 scopus 로고    scopus 로고
    • Role of TTX-sensitive and TTX-resistant sodium channels in Adelta-and C-fiber conduction and synaptic transmission
    • Pinto, V.; Derkach, V. A.; Safronov, B. V. Role of TTX-sensitive and TTX-resistant sodium channels in Adelta-and C-fiber conduction and synaptic transmission. J. Neurophysiol., 2008, 99(2), 617-28.
    • (2008) J. Neurophysiol , vol.99 , Issue.2 , pp. 617-628
    • Pinto, V.1    Derkach, V.A.2    Safronov, B.V.3
  • 125
    • 0027050717 scopus 로고
    • Somal membrane properties of physiologically identified sensory neurons in the rat: Effects of nerve growth factor
    • Ritter, A. M.; Mendell, L. M. Somal membrane properties of physiologically identified sensory neurons in the rat: effects of nerve growth factor. J. Neurophysiol., 1992, 68(6), 2033-41.
    • (1992) J. Neurophysiol , vol.68 , Issue.6 , pp. 2033-2041
    • Ritter, A.M.1    Mendell, L.M.2
  • 126
    • 0029764479 scopus 로고    scopus 로고
    • Electrophysiological properties of neurons in intact rat dorsal root ganglia classified by conduction velocity and action potential duration
    • Villiere, V.; McLachlan, E. M. Electrophysiological properties of neurons in intact rat dorsal root ganglia classified by conduction velocity and action potential duration. J. Neurophysiol., 1996, 76(3), 1924-41.
    • (1996) J. Neurophysiol , vol.76 , Issue.3 , pp. 1924-1941
    • Villiere, V.1    McLachlan, E.M.2
  • 127
    • 0018751036 scopus 로고
    • Studies on sensory neurons of the mouse with intracellular-recording and horseradish peroxidase-injection techniques
    • Yoshida, S.; Matsuda, Y. Studies on sensory neurons of the mouse with intracellular-recording and horseradish peroxidase-injection techniques. J. Neurophysiol., 1979, 42(4), 1134-45.
    • (1979) J. Neurophysiol , vol.42 , Issue.4 , pp. 1134-1145
    • Yoshida, S.1    Matsuda, Y.2
  • 130
    • 0029881762 scopus 로고    scopus 로고
    • Nodal swelling produced by ciguatoxin-induced selective activation of sodium channels in myelinated nerve fibers
    • Benoit, E.; Juzans, P.; Legrand, A. M.; Molgo, J. Nodal swelling produced by ciguatoxin-induced selective activation of sodium channels in myelinated nerve fibers. Neuroscience, 1996, 71(4), 1121-31.
    • (1996) Neuroscience , vol.71 , Issue.4 , pp. 1121-1131
    • Benoit, E.1    Juzans, P.2    Legrand, A.M.3    Molgo, J.4
  • 131
    • 0023025984 scopus 로고
    • A study of toxin production by Gambierdiscus toxicus in culture
    • Durand-Clement, M. A study of toxin production by Gambierdiscus toxicus in culture. Toxicon, 1986, 24(11-12), 1153-7.
    • (1986) Toxicon , vol.24 , Issue.11-12 , pp. 1153-1157
    • Durand-Clement, M.1
  • 132
    • 0023666436 scopus 로고
    • Ciguatoxin and brevetoxins share a common receptor site on the neuronal voltagedependent Na+ channel
    • Lombet, A.; Bidard, J. N.; Lazdunski, M. Ciguatoxin and brevetoxins share a common receptor site on the neuronal voltagedependent Na+ channel. FEBS Lett., 1987, 219(2), 355-9.
    • (1987) FEBS Lett , vol.219 , Issue.2 , pp. 355-359
    • Lombet, A.1    Bidard, J.N.2    Lazdunski, M.3
  • 133
    • 0021824172 scopus 로고
    • Interaction of brevetoxin A with a new receptor site on the sodium channel
    • Catterall, W. A.; Gainer, M. Interaction of brevetoxin A with a new receptor site on the sodium channel. Toxicon, 1985, 23(3), 497-504.
    • (1985) Toxicon , vol.23 , Issue.3 , pp. 497-504
    • Catterall, W.A.1    Gainer, M.2
  • 134
    • 0026642271 scopus 로고
    • Binding of brevetoxins and ciguatoxin to the voltage-sensitive sodium channel and conformational analysis of brevetoxin B
    • Gawley, R. E.; Rein, K. S.; Kinoshita, M.; Baden, D. G. Binding of brevetoxins and ciguatoxin to the voltage-sensitive sodium channel and conformational analysis of brevetoxin B. Toxicon, 1992, 30(7), 780-5.
    • (1992) Toxicon , vol.30 , Issue.7 , pp. 780-785
    • Gawley, R.E.1    Rein, K.S.2    Kinoshita, M.3    Baden, D.G.4
  • 135
    • 0031025655 scopus 로고    scopus 로고
    • Euphorbium: Modern research on its active principle, resiniferatoxin, revives an ancient medicine
    • Appendino, G.; Szallasi, A. Euphorbium: modern research on its active principle, resiniferatoxin, revives an ancient medicine. Life Sci., 1997, 60(10), 681-96.
    • (1997) Life Sci , vol.60 , Issue.10 , pp. 681-696
    • Appendino, G.1    Szallasi, A.2
  • 136
    • 1542267774 scopus 로고    scopus 로고
    • Resiniferatoxin binds to the capsaicin receptor (TRPV1) near the extracellular side of the S4 transmembrane domain
    • Chou, M. Z.; Mtui, T.; Gao, Y. D.; Kohler, M.; Middleton, R. E. Resiniferatoxin binds to the capsaicin receptor (TRPV1) near the extracellular side of the S4 transmembrane domain. Biochemistry, 2004, 43(9), 2501-11.
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2501-2511
    • Chou, M.Z.1    Mtui, T.2    Gao, Y.D.3    Kohler, M.4    Middleton, R.E.5
  • 137
    • 17744406515 scopus 로고    scopus 로고
    • Current views on scorpion toxins specific for K+-channels
    • Rodriguez de la Vega R. C.; Possani, L. D. Current views on scorpion toxins specific for K+-channels. Toxicon, 2004, 43(8), 865-75.
    • (2004) Toxicon , vol.43 , Issue.8 , pp. 865-875
    • Rodriguez de la Vega, R.C.1    Possani, L.D.2
  • 138
    • 0023635053 scopus 로고
    • Charybdotoxin selectively blocks small Ca-activated K channels in Aplysia neurons
    • Hermann, A.; Erxleben, C. Charybdotoxin selectively blocks small Ca-activated K channels in Aplysia neurons. J. Gen. Physiol., 1987, 90(1), 27-47.
    • (1987) J. Gen. Physiol , vol.90 , Issue.1 , pp. 27-47
    • Hermann, A.1    Erxleben, C.2
  • 139
    • 0021918550 scopus 로고
    • Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle
    • Miller, C.; Moczydlowski, E.; Latorre, R.; Phillips, M. Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle. Nature, 1985, 313(6000), 316-8.
    • (1985) Nature , vol.313 , Issue.6000 , pp. 316-318
    • Miller, C.1    Moczydlowski, E.2    Latorre, R.3    Phillips, M.4
  • 140
    • 0027443836 scopus 로고
    • Mechanism of charybdotoxin block of a voltage-gated K+ channel
    • Goldstein, S. A.; Miller, C. Mechanism of charybdotoxin block of a voltage-gated K+ channel. Biophys. J., 1993, 65(4), 1613-9.
    • (1993) Biophys. J , vol.65 , Issue.4 , pp. 1613-1619
    • Goldstein, S.A.1    Miller, C.2
  • 141
    • 0025644364 scopus 로고
    • Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor
    • MacKinnon, R.; Heginbotham, L.; Abramson, T. Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor. Neuron, 1990, 5(6), 767-71.
    • (1990) Neuron , vol.5 , Issue.6 , pp. 767-771
    • McKinnon, R.1    Heginbotham, L.2    Abramson, T.3
  • 142
    • 0024426645 scopus 로고
    • Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor
    • MacKinnon, R.; Miller, C. Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor. Science, 1989, 245(4924), 1382-5.
    • (1989) Science , vol.245 , Issue.4924 , pp. 1382-1385
    • McKinnon, R.1    Miller, C.2
  • 143
    • 0023907940 scopus 로고
    • Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength
    • Anderson, C. S.; MacKinnon, R.; Smith, C.; Miller, C. Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength. J. Gen. Physiol., 1988, 91(3), 317-33.
    • (1988) J. Gen. Physiol , vol.91 , Issue.3 , pp. 317-333
    • Anderson, C.S.1    McKinnon, R.2    Smith, C.3    Miller, C.4
  • 144
    • 0023887273 scopus 로고
    • Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel
    • MacKinnon, R.; Miller, C. Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel. J. Gen. Physiol., 1988, 91(3), 335-49.
    • (1988) J. Gen. Physiol , vol.91 , Issue.3 , pp. 335-349
    • McKinnon, R.1    Miller, C.2
  • 145
    • 0026803224 scopus 로고
    • Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel
    • Park, C. S.; Miller, C. Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel. Neuron, 1992, 9(2), 307-13.
    • (1992) Neuron , vol.9 , Issue.2 , pp. 307-313
    • Park, C.S.1    Miller, C.2
  • 146
    • 84879061835 scopus 로고    scopus 로고
    • Structure of a pore-blocking toxin in complex with a eukaryotic voltagedependent K(+) channel
    • Banerjee, A.; Lee, A.; Campbell, E.; Mackinnon, R. Structure of a pore-blocking toxin in complex with a eukaryotic voltagedependent K(+) channel. Elife, 2013, 2, e00594.
    • (2013) Elife , vol.2
    • Banerjee, A.1    Lee, A.2    Campbell, E.3    Mackinnon, R.4
  • 147
    • 0027219545 scopus 로고
    • Influence of protein surface charge on the bimolecular kinetics of a potassium channel peptide inhibitor
    • Escobar, L.; Root, M. J.; MacKinnon, R. Influence of protein surface charge on the bimolecular kinetics of a potassium channel peptide inhibitor. Biochemistry, 1993, 32(27), 6982-7.
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 6982-6987
    • Escobar, L.1    Root, M.J.2    McKinnon, R.3
  • 148
    • 0028276482 scopus 로고
    • The charybdotoxin receptor of a Shaker K+ channel: Peptide and channel residues mediating molecular recognition
    • Goldstein, S. A.; Pheasant, D. J.; Miller, C. The charybdotoxin receptor of a Shaker K+ channel: peptide and channel residues mediating molecular recognition. Neuron, 1994, 12(6), 1377-88.
    • (1994) Neuron , vol.12 , Issue.6 , pp. 1377-1388
    • Goldstein, S.A.1    Pheasant, D.J.2    Miller, C.3
  • 149
    • 0030044863 scopus 로고    scopus 로고
    • A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K+ channel
    • Naranjo, D.; Miller, C. A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K+ channel. Neuron, 1996, 16(1), 123-30.
    • (1996) Neuron , vol.16 , Issue.1 , pp. 123-130
    • Naranjo, D.1    Miller, C.2
  • 150
    • 0028267224 scopus 로고
    • Mutations in the K+ channel signature sequence
    • Heginbotham, L.; Lu, Z.; Abramson, T.; MacKinnon, R. Mutations in the K+ channel signature sequence. Biophys. J., 1994, 66(4), 1061-7.
    • (1994) Biophys. J , vol.66 , Issue.4 , pp. 1061-1067
    • Heginbotham, L.1    Lu, Z.2    Abramson, T.3    McKinnon, R.4
  • 151
    • 0034668792 scopus 로고    scopus 로고
    • A residue in the intracellular vestibule of the pore is critical for gating and permeation in Ca2+-activated K+ (BKCa) channels
    • Lippiat, J. D.; Standen, N. B.; Davies, N. W. A residue in the intracellular vestibule of the pore is critical for gating and permeation in Ca2+-activated K+ (BKCa) channels. J. Physiol., 2000, 529 Pt 1, 131-8.
    • (2000) J. Physiol , vol.529 , pp. 131-138
    • Lippiat, J.D.1    Standen, N.B.2    Davies, N.W.3
  • 152
    • 0030064382 scopus 로고    scopus 로고
    • Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis
    • Ranganathan, R.; Lewis, J. H.; MacKinnon, R. Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis. Neuron, 1996, 16(1), 131-9.
    • (1996) Neuron , vol.16 , Issue.1 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    McKinnon, R.3
  • 153
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • Hidalgo, P.; MacKinnon, R. Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor. Science, 1995, 268(5208), 307-10.
    • (1995) Science , vol.268 , Issue.5208 , pp. 307-310
    • Hidalgo, P.1    McKinnon, R.2
  • 154
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • Lange, A.; Giller, K.; Hornig, S.; Martin-Eauclaire M. F.; Pongs, O.; Becker, S.; Baldus, M. Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR. Nature, 2006, 440(7086), 959-62.
    • (2006) Nature , vol.440 , Issue.7086 , pp. 959-962
    • Lange, A.1    Giller, K.2    Hornig, S.3    Martin-Eauclaire, M.F.4    Pongs, O.5    Becker, S.6    Baldus, M.7
  • 155
    • 0024153562 scopus 로고
    • Charybdotoxin block of Shaker K+ channels suggests that different types of K+ channels share common structural features
    • MacKinnon, R.; Reinhart, P. H.; White, M. M. Charybdotoxin block of Shaker K+ channels suggests that different types of K+ channels share common structural features. Neuron, 1988, 1(10), 997-1001.
    • (1988) Neuron , vol.1 , Issue.10 , pp. 997-1001
    • McKinnon, R.1    Reinhart, P.H.2    White, M.M.3
  • 156
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon, R. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature, 1991, 350(6315), 232-5.
    • (1991) Nature , vol.350 , Issue.6315 , pp. 232-235
    • McKinnon, R.1
  • 157
    • 0025719899 scopus 로고
    • Phosphorylation of an alpha 1-like subunit of an omega-conotoxin-sensitive brain calcium channel by cAMP-dependent protein kinase and protein kinase
    • Ahlijanian, M. K.; Striessnig, J.; Catterall, W. A. Phosphorylation of an alpha 1-like subunit of an omega-conotoxin-sensitive brain calcium channel by cAMP-dependent protein kinase and protein kinase. J. Biol. Chem., 1991, 266(30), 20192-7.
    • (1991) J. Biol. Chem , vol.266 , Issue.30 , pp. 20192-20197
    • Ahlijanian, M.K.1    Striessnig, J.2    Catterall, W.A.3
  • 158
    • 0033779406 scopus 로고    scopus 로고
    • Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus alpha-toxin in planar lipid bilayers
    • Krasilnikov, O. V.; Merzlyak, P. G.; Yuldasheva, L. N.; Rodrigues, C. G.; Bhakdi, S.; Valeva, A. Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus alpha-toxin in planar lipid bilayers. Mol. Microbiol., 2000, 37(6), 1372-8.
    • (2000) Mol. Microbiol , vol.37 , Issue.6 , pp. 1372-1378
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Yuldasheva, L.N.3    Rodrigues, C.G.4    Bhakdi, S.5    Valeva, A.6
  • 159
    • 8044235836 scopus 로고    scopus 로고
    • A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity
    • Cotton, J.; Crest, M.; Bouet, F.; Alessandri, N.; Gola, M.; Forest, E.; Karlsson, E.; Castaneda, O.; Harvey, A. L.; Vita C.; Menez, A. A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity. Eur. J. Biochem., 1997, 244(1), 192-202.
    • (1997) Eur. J. Biochem , vol.244 , Issue.1 , pp. 192-202
    • Cotton, J.1    Crest, M.2    Bouet, F.3    Alessandri, N.4    Gola, M.5    Forest, E.6    Karlsson, E.7    Castaneda, O.8    Harvey, A.L.9    Vita, C.10    Menez, A.11
  • 160
    • 0037020077 scopus 로고    scopus 로고
    • Structure of the BgK-Kv1. 1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers
    • Gilquin, B.; Racapé, J.; Wrisch, A.; Visan, V.; Lecoq, A.; Grissmer, S.; Ménez, A.; Gasparini, S. Structure of the BgK-Kv1. 1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers. J. biol. chem., 2002, 277(40), 37406-13.
    • (2002) J. biol. chem , vol.277 , Issue.40 , pp. 37406-37413
    • Gilquin, B.1    Racapé, J.2    Wrisch, A.3    Visan, V.4    Lecoq, A.5    Grissmer, S.6    Ménez, A.7    Gasparini, S.8
  • 161
    • 0032554613 scopus 로고    scopus 로고
    • Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails
    • Savarin, P.; Guenneugues, M.; Gilquin, B.; Lamthanh, H.; Gasparini, S.; Zinn-Justin, S.; Ménez, A. Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry, 1998, 37(16), 5407-16.
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5407-5416
    • Savarin, P.1    Guenneugues, M.2    Gilquin, B.3    Lamthanh, H.4    Gasparini, S.5    Zinn-Justin, S.6    Ménez, A.7
  • 162
    • 0036099413 scopus 로고    scopus 로고
    • Inhibition of single Shaker K channels by kappaconotoxin-PVIIA
    • Naranjo, D. Inhibition of single Shaker K channels by kappaconotoxin-PVIIA. Biophys. J., 2002, 82(6), 3003-11.
    • (2002) Biophys. J , vol.82 , Issue.6 , pp. 3003-3011
    • Naranjo, D.1
  • 164
    • 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(18), 3881-4.
    • (2005) FEBS Lett , vol.579 , Issue.18 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 165
    • 84863774312 scopus 로고    scopus 로고
    • Mapping of scorpion toxin receptor sites at voltagegated sodium channels
    • Gurevitz, M. Mapping of scorpion toxin receptor sites at voltagegated sodium channels. Toxicon, 2012, 60(4), 502-11.
    • (2012) Toxicon , vol.60 , Issue.4 , pp. 502-511
    • Gurevitz, M.1
  • 166
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestele S., Catterall W. A. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie, 2000, 82(9-10), 883-92.
    • (2000) Biochimie , vol.82 , Issue.9-10 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 168
    • 0036141825 scopus 로고    scopus 로고
    • Electrostatic and steric contributions to block of the skeletal muscle sodium channel by mu-conotoxin
    • Hui, K.; Lipkind, G.; Fozzard, H. A.; French, R. J. Electrostatic and steric contributions to block of the skeletal muscle sodium channel by mu-conotoxin. J. gen. physio., 2002, 119(1), 45-54.
    • (2002) J. gen. physio , vol.119 , Issue.1 , pp. 45-54
    • Hui, K.1    Lipkind, G.2    Fozzard, H.A.3    French, R.J.4
  • 169
    • 0030016085 scopus 로고    scopus 로고
    • Three-dimensional solution structure of mu-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels
    • Hill, J. M.; Alewood, P. F.; Craik, D. J. Three-dimensional solution structure of mu-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels. Biochemistry, 1996, 35(27), 8824-35.
    • (1996) Biochemistry , vol.35 , Issue.27 , pp. 8824-8835
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 170
    • 0027078665 scopus 로고
    • Structure-activity relationships of mu-conotoxin GIIIA: Structure determination of active and inactive sodium channel blocker peptide by NMR and simulated annealing calculations
    • Wakamatsu, K.; Kohda, D.; Hatanaka, H.; Lancelin, J. M.; Ishida, Y.; Oya, M.; Nakamura, H.; Inagaki, F.; Sato, K. Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptide by NMR and simulated annealing calculations. Biochemistry, 1992, 31(50), 12577-84.
    • (1992) Biochemistry , vol.31 , Issue.50 , pp. 12577-12584
    • Wakamatsu, K.1    Kohda, D.2    Hatanaka, H.3    Lancelin, J.M.4    Ishida, Y.5    Oya, M.6    Nakamura, H.7    Inagaki, F.8    Sato, K.9
  • 172
    • 0346614200 scopus 로고
    • Discrimination of muscle and neuronal Na-channel subtypes by binding competition between [3H]saxitoxin and mu-conotoxins
    • Moczydlowski, E.; Olivera, B. M.; Gray, W. R.; Strichartz, G. R. Discrimination of muscle and neuronal Na-channel subtypes by binding competition between [3H]saxitoxin and mu-conotoxins. Proc. N. Acad. Sci U S A, 1986, 83(14), 5321-5.
    • (1986) Proc. N. Acad. Sci U S A , vol.83 , Issue.14 , pp. 5321-5325
    • Moczydlowski, E.1    Olivera, B.M.2    Gray, W.R.3    Strichartz, G.R.4
  • 173
    • 0022931513 scopus 로고
    • Specific inhibition of [3H] saxitoxin binding to skeletal muscle sodium channels by geographutoxin II, a polypeptide channel blocker
    • Ohizumi, Y.; Nakamura, H.; Kobayashi, J.; Catterall, W. A. Specific inhibition of [3H] saxitoxin binding to skeletal muscle sodium channels by geographutoxin II, a polypeptide channel blocker. J. boil. Chem., 1986, 261(14), 6149-52.
    • (1986) J. boil. Chem , vol.261 , Issue.14 , pp. 6149-6152
    • Ohizumi, Y.1    Nakamura, H.2    Kobayashi, J.3    Catterall, W.A.4
  • 174
    • 0022559685 scopus 로고
    • Blockade of [3H]lysinetetrodotoxin binding to sodium channel proteins by conotoxin GIII
    • Yanagawa, Y.; Abe, T.; Satake, M. Blockade of [3H]lysinetetrodotoxin binding to sodium channel proteins by conotoxin GIII. Neurosci. Lett., 1986, 64(1), 7-12.
    • (1986) Neurosci. Lett , vol.64 , Issue.1 , pp. 7-12
    • Yanagawa, Y.1    Abe, T.2    Satake, M.3
  • 175
    • 0029417234 scopus 로고
    • Characterizing the mu-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations
    • Chahine, M.; Chen, L. Q.; Fotouhi, N.; Walsky, R.; Fry, D.; Santarelli, V.; Horn, R.; Kallen, R. G. Characterizing the mu-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations. Receptors & channels, 1995, 3(3), 161-74.
    • (1995) Receptors & channels , vol.3 , Issue.3 , pp. 161-174
    • Chahine, M.1    Chen, L.Q.2    Fotouhi, N.3    Walsky, R.4    Fry, D.5    Santarelli, V.6    Horn, R.7    Kallen, R.G.8
  • 176
    • 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 muconotoxin GIIIA binding site
    • Chahine, M.; Sirois, J.; Marcotte, P.; Chen, L.; 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 muconotoxin GIIIA binding site. Biophys. J., 1998, 75(1), 236-46.
    • (1998) Biophys. J , vol.75 , Issue.1 , pp. 236-246
    • Chahine, M.1    Sirois, J.2    Marcotte, P.3    Chen, L.4    Kallen, R.G.5
  • 177
    • 0028970541 scopus 로고
    • A muconotoxin-insensitive Na+ channel mutant: Possible localization of a binding site at the outer vestibule
    • Dudley, S. C.; Todt, H.; Lipkind, G.; Fozzard, H. A. A muconotoxin-insensitive Na+ channel mutant: possible localization of a binding site at the outer vestibule. Biophys. J., 1995, 69(5), 1657-65.
    • (1995) Biophys. J , vol.69 , Issue.5 , pp. 1657-1665
    • Dudley, S.C.1    Todt, H.2    Lipkind, G.3    Fozzard, H.A.4
  • 178
    • 0028180093 scopus 로고
    • The microI skeletal muscle sodium channel: Mutation E403Q eliminates sensitivity to tetrodotoxin but not to mu-conotoxins GIIIA and GIIIB
    • Stephan, M. M.; Potts, J. F.; Agnew, W. S. The microI skeletal muscle sodium channel: mutation E403Q eliminates sensitivity to tetrodotoxin but not to mu-conotoxins GIIIA and GIIIB. J. Membr. Biol., 1994, 137(1), 1-8.
    • (1994) J. Membr. Biol , vol.137 , Issue.1 , pp. 1-8
    • Stephan, M.M.1    Potts, J.F.2    Agnew, W.S.3
  • 179
    • 0026657359 scopus 로고
    • Action of derivatives of mu-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates
    • Becker, S.; Prusak-Sochaczewski, E.; Zamponi, G.; Beck-Sickinger, A. G.; Gordon, R. D.; French, R. J. Action of derivatives of mu-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry, 1992, 31(35), 8229-38.
    • (1992) Biochemistry , vol.31 , Issue.35 , pp. 8229-8238
    • Becker, S.1    Prusak-Sochaczewski, E.2    Zamponi, G.3    Beck-Sickinger, A.G.4    Gordon, R.D.5    French, R.J.6
  • 181
    • 0030058733 scopus 로고    scopus 로고
    • Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: An electrostatic approach to channel geometry
    • French, R. J.; Prusak-Sochaczewski, E.; Zamponi, G. W.; Becker, S.; Kularatna, A. S.; Horn R. Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: an electrostatic approach to channel geometry. Neuron, 1996, 16(2), 407-13.
    • (1996) Neuron , vol.16 , Issue.2 , pp. 407-413
    • French, R.J.1    Prusak-Sochaczewski, E.2    Zamponi, G.W.3    Becker, S.4    Kularatna, A.S.5    Horn, R.6
  • 182
    • 0037196391 scopus 로고    scopus 로고
    • Charge conversion enables quantification of the proximity between a normally-neutral mu-conotoxin (GIIIA) site and the Na+ channel pore
    • Li, R. A.; Sato, K.; Kodama, K.; Kohno, T.; Xue, T.; Tomaselli, G. F.; Marbán, E. Charge conversion enables quantification of the proximity between a normally-neutral mu-conotoxin (GIIIA) site and the Na+ channel pore. FEBS Lett., 2002, 511(1-3), 159-64.
    • (2002) FEBS Lett , vol.511 , Issue.1-3 , pp. 159-164
    • Li, R.A.1    Sato, K.2    Kodama, K.3    Kohno, T.4    Xue, T.5    Tomaselli, G.F.6    Marbán, E.7
  • 183
    • 0035815713 scopus 로고    scopus 로고
    • Clockwise domain arrangement of the sodium channel revealed by (mu)-conotoxin (GIIIA) docking orientation
    • Li, R. A.; Ennis, I. L.; French, R. J.; Dudley, S. C. Jr.; Tomaselli, G. F.; Marban, E. Clockwise domain arrangement of the sodium channel revealed by (mu)-conotoxin (GIIIA) docking orientation. J. Biol. Chem., 2001, 276(14), 11072-7.
    • (2001) J. Biol. Chem , vol.276 , Issue.14 , pp. 11072-11077
    • Li, R.A.1    Ennis, I.L.2    French, R.J.3    Dudley, S.C.4    Tomaselli, G.F.5    Marban, E.6
  • 184
    • 0033756777 scopus 로고    scopus 로고
    • mu-conotoxin GIIIA interactions with the voltagegated Na(+) channel predict a clockwise arrangement of the domains
    • Dudley, S. C.; Chang, N.; Hall, J.; Lipkind, G.; Fozzard, H. A.; French, R. J. mu-conotoxin GIIIA interactions with the voltagegated Na(+) channel predict a clockwise arrangement of the domains. J. gen. physio., 2000, 116(5), 679-90.
    • (2000) J. gen. physio , vol.116 , Issue.5 , pp. 679-690
    • Dudley, S.C.1    Chang, N.2    Hall, J.3    Lipkind, G.4    Fozzard, H.A.5    French, R.J.6
  • 185
    • 0015970876 scopus 로고
    • Gating currents of the sodium channels: Three ways to block them
    • Bezanilla, F.; Armstrong, C. M. Gating currents of the sodium channels: three ways to block them. Science (New York, N. Y.), 1974, 183(4126), 753-4.
    • (1974) Science (New York, N.Y.) , vol.183 , Issue.4126 , pp. 753-754
    • Bezanilla, F.1    Armstrong, C.M.2
  • 186
    • 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(6), 615-9.
    • (1975) Biophys. J , vol.15 , Issue.6 , pp. 615-619
    • Hille, B.1
  • 187
    • 0013797237 scopus 로고
    • Actions of saxitoxin on peripheral neuromuscular systems
    • Kao C. Y., Nishiyama A. Actions of saxitoxin on peripheral neuromuscular systems. J. Physiol, 1965, 180(1), 50-66.
    • (1965) J. Physiol , vol.180 , Issue.1 , pp. 50-66
    • Kao, C.Y.1    Nishiyama, A.2
  • 188
    • 0016196463 scopus 로고
    • Kinetics and steady-state properties of the charged system controlling sodium conductance in the squid giant axon
    • Keynes, R. D.; Rojas, E. Kinetics and steady-state properties of the charged system controlling sodium conductance in the squid giant axon. J. physio., 1974, 239(2), 393-434.
    • (1974) J. physio , vol.239 , Issue.2 , pp. 393-434
    • Keynes, R.D.1    Rojas, E.2
  • 189
    • 84903900359 scopus 로고    scopus 로고
    • Animal toxins influence voltage-gated sodium channel function
    • 2212014
    • Gilchrist, J.; Olivera, B. M.; Bosmans, F. Animal toxins influence voltage-gated sodium channel function. Handb Exp Pharmacol. 2212014. p. 203-29.
    • Handb Exp Pharmacol , pp. 203-229
    • Gilchrist, J.1    Olivera, B.M.2    Bosmans, F.3
  • 192
    • 0014253550 scopus 로고
    • Charges and potentials at the nerve surface. Divalent ions and pH
    • Hille, B. Charges and potentials at the nerve surface. Divalent ions and pH. J. Gen. Physiol., 1968, 51(2), 221-36.
    • (1968) J. Gen. Physiol , vol.51 , Issue.2 , pp. 221-236
    • Hille, B.1
  • 193
    • 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(6), 599-619.
    • (1971) J. Gen. Physiol , vol.58 , Issue.6 , pp. 599-619
    • Hille, B.1
  • 195
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J.; Scheuer, T.; Zheng, N.; Catterall, W. A. The crystal structure of a voltage-gated sodium channel. Nature, 2011, 475(7356), 353-8.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 196
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J.; Gamal, El-Din T. M.; Scheuer, T.; Zheng, N.; Catterall, W. A. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature, 2012, 486(7401), 135-9.
    • (2012) Nature , vol.486 , Issue.7401 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 197
    • 0016246702 scopus 로고
    • Chemicals as tools in the study of excitable membranes
    • Narahashi, T. Chemicals as tools in the study of excitable membranes. Physiol. Rev., 1974, 54(4), 813-89.
    • (1974) Physiol. Rev , vol.54 , Issue.4 , pp. 813-889
    • Narahashi, T.1
  • 198
    • 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, 965-74.
    • (1964) J. Gen. Physiol , vol.47 , pp. 965-974
    • Narahashi, T.1    Moore, J.W.2    Scott, W.R.3
  • 199
    • 0017327105 scopus 로고
    • The binding of saxitoxin and tetrodotoxin to excitable tissue
    • Ritchie, J. M.; Rogart, R. B. The binding of saxitoxin and tetrodotoxin 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
  • 200
    • 0016263666 scopus 로고
    • Evidence that tetrodotoxin and saxitoxin act at a metal cation binding site in the sodium channels of nerve membrane
    • Henderson, R.; Ritchie, J. M.; Strichartz, G. R. Evidence that tetrodotoxin and saxitoxin act at a metal cation binding site in the sodium channels of nerve membrane. Proc. Natl. Acad. Sci. U S A, 1974, 71(10), 3936-40.
    • (1974) Proc. Natl. Acad. Sci. U S A , vol.71 , Issue.10 , pp. 3936-3940
    • Henderson, R.1    Ritchie, J.M.2    Strichartz, G.R.3
  • 201
    • 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), 1-13.
    • (1994) Biophys. J , vol.66 , Issue.1 , pp. 1-13
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 202
    • 84862561580 scopus 로고    scopus 로고
    • Architecture and pore block of eukaryotic voltage-gated sodium channels in view of NavAb bacterial sodium channel structure
    • Tikhonov, D. B.; Zhorov, B. S. Architecture and pore block of eukaryotic voltage-gated sodium channels in view of NavAb bacterial sodium channel structure. Mol. Pharmacol., 2012, 82(1), 97-104.
    • (2012) Mol. Pharmacol , vol.82 , Issue.1 , pp. 97-104
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 203
    • 84856747852 scopus 로고    scopus 로고
    • Binding modes of mu-conotoxin to the bacterial sodium channel (NavAb)
    • Chen, R.; Chung, S. H. Binding modes of mu-conotoxin to the bacterial sodium channel (NavAb). Biophys. J., 2012, 102(3), 483-8.
    • (2012) Biophys. J , vol.102 , Issue.3 , pp. 483-488
    • Chen, R.1    Chung, S.H.2
  • 204
    • 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(6), 2647-57.
    • (1998) Biophys. J , vol.75 , Issue.6 , pp. 2647-2657
    • Penzotti, J.L.1    Fozzard, H.A.2    Lipkind, G.M.3    Dudley, S.C.4
  • 205
    • 0026072218 scopus 로고
    • Mapping the site of block by tetrodotoxin and saxitoxin of sodium channel II
    • Terlau, H.; Heinemann, S. H.; Stühmer, W.; Pusch, M.; Conti, F.; Imoto, K.; Numa, S. Mapping the site of block by tetrodotoxin and saxitoxin of sodium channel II. FEBS Lett., 1991, 293(1-2), 93-6.
    • (1991) FEBS Lett , vol.293 , Issue.1-2 , pp. 93-96
    • Terlau, H.1    Heinemann, S.H.2    Stühmer, W.3    Pusch, M.4    Conti, F.5    Imoto, K.6    Numa, S.7
  • 206
    • 84897998566 scopus 로고    scopus 로고
    • Mechanism of tetrodotoxin block and resistance in sodium channels
    • Chen, R.; Chung, S. H. Mechanism of tetrodotoxin block and resistance in sodium channels. Biochem. Biophys. Res. Commun., 2014, 446, 370-4.
    • (2014) Biochem. Biophys. Res. Commun , vol.446 , pp. 370-374
    • Chen, R.1    Chung, S.H.2
  • 207
    • 84858631162 scopus 로고    scopus 로고
    • Constraint shapes convergence in tetrodotoxin-resistant sodium channels of snakes
    • Feldman, C. R.; Brodie, E. D. Jr.; Brodie, E. D.; 3rd, Pfrender M. E. Constraint shapes convergence in tetrodotoxin-resistant sodium channels of snakes. Proc. Natl. Acad. Sci. U S A, 2012, 109(12), 4556-61.
    • (2012) Proc. Natl. Acad. Sci. U S A , vol.109 , Issue.12 , pp. 4556-4561
    • Feldman, C.R.1    Brodie, E.D.2    Brodie, E.D.3    Pfrender, M.E.4
  • 208
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J.; Scheuer, T.; Zheng, N.; Catterall, W. A. The crystal structure of a voltage-gated sodium channel. Nature, 2011, 475(7356), 353-8.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 209
    • 67649604544 scopus 로고    scopus 로고
    • Mapping the structure and conformational movements of proteins with transition metal ion FRET
    • Taraska, J. W., Puljung, M. C.; Olivier, N. B.; Flynn, G. E.; Zagotta, W. N. Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nat. Methods, 2009, 6(7), 532-7.
    • (2009) Nat. Methods , vol.6 , Issue.7 , pp. 532-537
    • Taraska, J.W.1    Puljung, M.C.2    Olivier, N.B.3    Flynn, G.E.4    Zagotta, W.N.5
  • 210
    • 0021247688 scopus 로고
    • Fluorescence resonance energy transfer on the voltage-dependent sodium channel. Spatial relationship and site coupling between the batrachotoxin and Leiurus quinquestriatus quinquestriatus alpha-scorpion toxin receptors
    • Angelides, K. J.; Brown, G. B. Fluorescence resonance energy transfer on the voltage-dependent sodium channel. Spatial relationship and site coupling between the batrachotoxin and Leiurus quinquestriatus quinquestriatus alpha-scorpion toxin receptors. J. Biol. Chem., 1984, 259(10), 6117-26.
    • (1984) J. Biol. Chem , vol.259 , Issue.10 , pp. 6117-6126
    • Angelides, K.J.1    Brown, G.B.2
  • 211
    • 80051988895 scopus 로고    scopus 로고
    • Batrachotoxin, pyrethroids, and BTG 502 share overlapping binding sites on insect sodium channels
    • Du, Y.; Garden, D.; Khambay, B.; Zhorov, B. S.; Dong, K. Batrachotoxin, pyrethroids, and BTG 502 share overlapping binding sites on insect sodium channels. Mol. Pharmacol., 2011, 80(3), 426-33.
    • (2011) Mol. Pharmacol , vol.80 , Issue.3 , pp. 426-433
    • Du, Y.1    Garden, D.2    Khambay, B.3    Zhorov, B.S.4    Dong, K.5
  • 212
    • 33644844639 scopus 로고    scopus 로고
    • How batrachotoxin modifies the sodium channel permeation pathway: Computer modeling and site-directed mutagenesis
    • Wang, S. Y.; Mitchell, J.; Tikhonov, D. B.; Zhorov, B. S.; Wang, G. K. How batrachotoxin modifies the sodium channel permeation pathway: computer modeling and site-directed mutagenesis. Mol. Pharmacol., 2006, 69(3), 788-95.
    • (2006) Mol. Pharmacol , vol.69 , Issue.3 , pp. 788-795
    • Wang, S.Y.1    Mitchell, J.2    Tikhonov, D.B.3    Zhorov, B.S.4    Wang, G.K.5
  • 213
    • 48649093428 scopus 로고    scopus 로고
    • Alphascorpion toxin impairs a conformational change that leads to fast inactivation of muscle sodium channels
    • Campos, F. V.; Chanda, B.; Beirao, P. S.; Bezanilla, F. Alphascorpion toxin impairs a conformational change that leads to fast inactivation of muscle sodium channels. J. Gen. Physiol., 2008, 132(2), 251-63.
    • (2008) J. Gen. Physiol , vol.132 , Issue.2 , pp. 251-263
    • Campos, F.V.1    Chanda, B.2    Beirao, P.S.3    Bezanilla, F.4
  • 214
    • 0020563347 scopus 로고
    • Mapping the molecular structure of the voltage-dependent sodium channel. Distances between the tetrodotoxin and Leiurus quinquestriatus quinquestriatus scorpion toxin receptors
    • Angelides, K. J.; Nutter, T. J. Mapping the molecular structure of the voltage-dependent sodium channel. Distances between the tetrodotoxin and Leiurus quinquestriatus quinquestriatus scorpion toxin receptors. J. Biol. Chem., 1983, 258(19), 11958-67.
    • (1983) J. Biol. Chem , vol.258 , Issue.19 , pp. 11958-11967
    • Angelides, K.J.1    Nutter, T.J.2
  • 215
    • 0030960732 scopus 로고    scopus 로고
    • Preferential interaction of omega-conotoxins with inactivated N-type Ca2+ channels
    • Stocker, J. W.; Nadasdi, L.; Aldrich, R. W.; Tsien, R. W. Preferential interaction of omega-conotoxins with inactivated N-type Ca2+ channels. J. Neurosci., 1997, 17(9), 3002-13.
    • (1997) J. Neurosci , vol.17 , Issue.9 , pp. 3002-3013
    • Stocker, J.W.1    Nadasdi, L.2    Aldrich, R.W.3    Tsien, R.W.4
  • 217
    • 33847198227 scopus 로고    scopus 로고
    • Alternative splicing controls G protein-dependent inhibition of N-type calcium channels in nociceptors
    • Raingo, J.; Castiglioni, A. J.; Lipscombe, D. Alternative splicing controls G protein-dependent inhibition of N-type calcium channels in nociceptors. Nat. Neurosci., 2007, 10(3), 285-92.
    • (2007) Nat. Neurosci , vol.10 , Issue.3 , pp. 285-292
    • Raingo, J.1    Castiglioni, A.J.2    Lipscombe, D.3
  • 218
    • 77951652246 scopus 로고    scopus 로고
    • Ziconotide for treatment of severe chronic pain
    • Schmidtko, A.; Lötsch, J.; Freynhagen, R.; Geisslinger, G. Ziconotide for treatment of severe chronic pain. Lancet, 2010, 375(9725), 1569-77.
    • (2010) Lancet , vol.375 , Issue.9725 , pp. 1569-1577
    • Schmidtko, A.1    Lötsch, J.2    Freynhagen, R.3    Geisslinger, G.4
  • 219
    • 0037345806 scopus 로고    scopus 로고
    • An examination of calcium current function on heterotopic neurons in hippocampal slices from rats exposed to methylazoxymethanol
    • Calcagnotto, M. E.; Baraban, S. C. An examination of calcium current function on heterotopic neurons in hippocampal slices from rats exposed to methylazoxymethanol. Epilepsia, 2003, 44(3), 315-21.
    • (2003) Epilepsia , vol.44 , Issue.3 , pp. 315-321
    • Calcagnotto, M.E.1    Baraban, S.C.2
  • 220
    • 0033616414 scopus 로고    scopus 로고
    • The role of voltage-gated Ca2+ channels in anoxic injury of spinal cord white matter
    • Imaizumi T., Kocsis J. D., Waxman S. G. The role of voltage-gated Ca2+ channels in anoxic injury of spinal cord white matter. Brain Res., 1999, 817(1-2), 84-92.
    • (1999) Brain Res , vol.817 , Issue.1-2 , pp. 84-92
    • Imaizumi, T.1    Kocsis, J.D.2    Waxman, S.G.3
  • 221
  • 222
    • 0034647343 scopus 로고    scopus 로고
    • CaV2. 2 and CaV2. 3 (N-and R-type) Ca2+ channels in depolarization-evoked entry of Ca2+ into mouse sperm
    • Wennemuth, G.; Westenbroek, R. E.; Xu, T.; Hille, B.; Babcock, D. F. CaV2. 2 and CaV2. 3 (N-and R-type) Ca2+ channels in depolarization-evoked entry of Ca2+ into mouse sperm. J. biol. chem., 2000, 275(28), 21210-7.
    • (2000) J. biol. chem , vol.275 , Issue.28 , pp. 21210-21217
    • Wennemuth, G.1    Westenbroek, R.E.2    Xu, T.3    Hille, B.4    Babcock, D.F.5
  • 223
    • 0028292145 scopus 로고
    • Calcium channel diversity and neurotransmitter release: The omegaconotoxins and omega-agatoxins
    • Olivera, B. M.; Miljanich, G. P.; Ramachandran, J.; Adams, M. E. Calcium channel diversity and neurotransmitter release: the omegaconotoxins and omega-agatoxins. Annu. Rev. Biochem., 1994, 63, 823-67.
    • (1994) Annu. Rev. Biochem , vol.63 , pp. 823-867
    • Olivera, B.M.1    Miljanich, G.P.2    Ramachandran, J.3    Adams, M.E.4
  • 224
    • 9144272640 scopus 로고    scopus 로고
    • Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain
    • Miljanich, G. P. Ziconotide: neuronal calcium channel blocker for treating severe chronic pain. Curr. Med. Chem., 2004, 11(23), 3029-40.
    • (2004) Curr. Med. Chem , vol.11 , Issue.23 , pp. 3029-3040
    • Miljanich, G.P.1
  • 225
    • 77949433165 scopus 로고    scopus 로고
    • Safety and efficacy of intrathecal ziconotide in the management of severe chronic pain
    • Smith, H. S.; Deer, T. R. Safety and efficacy of intrathecal ziconotide in the management of severe chronic pain. Ther. Clin. Risk. Manag., 2009, 5(3), 521-34.
    • (2009) Ther. Clin. Risk. Manag , vol.5 , Issue.3 , pp. 521-534
    • Smith, H.S.1    Deer, T.R.2
  • 226
    • 84876932229 scopus 로고    scopus 로고
    • Mechanisms of conotoxin inhibition of N-type (Ca(v)2. 2) calcium channels
    • Adams D. J.; Berecki, G. Mechanisms of conotoxin inhibition of N-type (Ca(v)2. 2) calcium channels. Biochim. Biophys. Acta, 2013, 1828(7), 1619-28.
    • (2013) Biochim. Biophys. Acta , vol.1828 , Issue.7 , pp. 1619-1628
    • Adams, D.J.1    Berecki, G.2
  • 227
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA
    • Scanlon, M. J.; Naranjo, D.; Thomas, L.; Alewood, P. F.; Lewis, R. J.; Craik, D. J. Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA. Structure (London, England: 1993), 1997, 5(12), 1585-97.
    • (1997) Structure (London, England: 1993) , vol.5 , Issue.12 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5    Craik, D.J.6
  • 229
    • 0034060567 scopus 로고    scopus 로고
    • Structure-activity relationships of omega-conotoxins at N-type voltage-sensitive calcium channels
    • Nielsen, K. J.; Schroeder, T.; Lewis, R. Structure-activity relationships of omega-conotoxins at N-type voltage-sensitive calcium channels. J. Mol. Recognit, 2000, 13(2), 55-70.
    • (2000) J. Mol. Recognit , vol.13 , Issue.2 , pp. 55-70
    • Nielsen, K.J.1    Schroeder, T.2    Lewis, R.3
  • 231
    • 84878306447 scopus 로고    scopus 로고
    • Complex structures between the N-type calcium channel (CaV2. 2) and ω-conotoxin GVIA predicted via molecular dynamics
    • Chen, R.; Chung, S.-H. Complex structures between the N-type calcium channel (CaV2. 2) and ω-conotoxin GVIA predicted via molecular dynamics. Biochemistry, 2013, 52(21), 3765-72.
    • (2013) Biochemistry , vol.52 , Issue.21 , pp. 3765-3772
    • Chen, R.1    Chung, S.-H.2
  • 233
    • 0028782785 scopus 로고
    • Hydroxyl group of Tyr13 is essential for the activity of omegaconotoxin GVIA, a peptide toxin for N-type calcium channel
    • Kim, J. I.; Takahashi, M.; Ogura, A.; Kohno, T.; Kudo, Y.; Sato, K. Hydroxyl group of Tyr13 is essential for the activity of omegaconotoxin GVIA, a peptide toxin for N-type calcium channel. J. biol. chem., 1994, 269(39), 23876-8.
    • (1994) J. biol. chem , vol.269 , Issue.39 , pp. 23876-23878
    • Kim, J.I.1    Takahashi, M.2    Ogura, A.3    Kohno, T.4    Kudo, Y.5    Sato, K.6
  • 235
    • 0028096838 scopus 로고
    • Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin
    • Ellinor, P. T.; Zhang, J. F.; Horne, W. A.; Tsien, R. W. Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin. Nature, 1994, 372(6503), 272-5.
    • (1994) Nature , vol.372 , Issue.6503 , pp. 272-275
    • Ellinor, P.T.1    Zhang, J.F.2    Horne, W.A.3    Tsien, R.W.4
  • 236
    • 0036229869 scopus 로고    scopus 로고
    • Interactions among toxins that inhibit N-type and P-type calcium channels
    • McDonough, S. I.; Boland, L. M.; Mintz, I. M.; Bean, B. P. Interactions among toxins that inhibit N-type and P-type calcium channels. J. gen. physio., 2002, 119(4), 313-28.
    • (2002) J. gen. physio , vol.119 , Issue.4 , pp. 313-328
    • McDonough, S.I.1    Boland, L.M.2    Mintz, I.M.3    Bean, B.P.4
  • 237
    • 0016717231 scopus 로고
    • Purification of three polypeptides with neuro-and cardiotoxic activity from the sea anemone Anemonia sulcata
    • Beress, L.; Beress, R. Purification of three polypeptides with neuro-and cardiotoxic activity from the sea anemone Anemonia sulcata. Toxicon, 1975, 13(5), 359-67.
    • (1975) Toxicon , vol.13 , Issue.5 , pp. 359-367
    • Beress, L.1    Beress, R.2
  • 238
    • 0024583588 scopus 로고
    • A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: Sequential and stereospecific resonance assignment and secondary structure
    • Driscoll, P. C.; Clore, G. M.; Beress, L.; Gronenborn, A. M. A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. Biochemistry, 1989, 28(5), 2178-87.
    • (1989) Biochemistry , vol.28 , Issue.5 , pp. 2178-2187
    • Driscoll, P.C.1    Clore, G.M.2    Beress, L.3    Gronenborn, A.M.4
  • 239
    • 25444516499 scopus 로고    scopus 로고
    • Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: Significance for CNS and biophysical studies
    • Yeung, S. Y.; Thompson, D.; Wang, Z.; Fedida, D.; Robertson, B. Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies. J. Neurosci., 2005, 25(38), 8735-45.
    • (2005) J. Neurosci , vol.25 , Issue.38 , pp. 8735-8745
    • Yeung, S.Y.1    Thompson, D.2    Wang, Z.3    Fedida, D.4    Robertson, B.5
  • 240
    • 0032549630 scopus 로고    scopus 로고
    • Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3. 4
    • Diochot, S.; Schweitz, H.; Beress, L.; Lazdunski, M. Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3. 4. J. Biol. Chem., 1998, 273(12), 6744-9.
    • (1998) J. Biol. Chem , vol.273 , Issue.12 , pp. 6744-6749
    • Diochot, S.1    Schweitz, H.2    Beress, L.3    Lazdunski, M.4
  • 241
    • 0026008949 scopus 로고
    • Binding of the sea anemone polypeptide BDS II to the voltage-gated sodium channel
    • Llewellyn, L. E.; Norton, R. S. Binding of the sea anemone polypeptide BDS II to the voltage-gated sodium channel. Biochem Int, 1991, 24(5), 937-46.
    • (1991) Biochem Int , vol.24 , Issue.5 , pp. 937-946
    • Llewellyn, L.E.1    Norton, R.S.2
  • 242
    • 84861881276 scopus 로고    scopus 로고
    • Modulation of neuronal sodium channels by the sea anemone peptide BDS-I
    • Liu, P.; Jo, S.; Bean, B. P. Modulation of neuronal sodium channels by the sea anemone peptide BDS-I. J. Neurophysiol., 2012, 107(11), 3155-67.
    • (2012) J. Neurophysiol , vol.107 , Issue.11 , pp. 3155-3167
    • Liu, P.1    Jo, S.2    Bean, B.P.3
  • 243
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2. 1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz, K. J.; MacKinnon, R. An inhibitor of the Kv2. 1 potassium channel isolated from the venom of a Chilean tarantula. Neuron, 1995, 15(4), 941-9.
    • (1995) Neuron , vol.15 , Issue.4 , pp. 941-949
    • Swartz, K.J.1    McKinnon, R.2
  • 244
    • 0030952979 scopus 로고    scopus 로고
    • Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites
    • Swartz, K. J.; MacKinnon, R. Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron, 1997, 18(4), 665-73.
    • (1997) Neuron , vol.18 , Issue.4 , pp. 665-673
    • Swartz, K.J.1    McKinnon, R.2
  • 245
    • 0030935699 scopus 로고    scopus 로고
    • Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels
    • Swartz, K. J.; MacKinnon, R. Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron, 1997, 18, 675-82.
    • (1997) Neuron , vol.18 , pp. 675-682
    • Swartz, K.J.1    McKinnon, R.2
  • 247
    • 0034130607 scopus 로고    scopus 로고
    • Localization and molecular determinants of the Hanatoxin receptors on the voltage-sensing domains of a K(+) channel
    • Li-Smerin, Y.; Swartz, K. J. Localization and molecular determinants of the Hanatoxin receptors on the voltage-sensing domains of a K(+) channel. J. gen. physio., 2000, 115(6), 673-84.
    • (2000) J. gen. physio , vol.115 , Issue.6 , pp. 673-684
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 248
    • 3142580385 scopus 로고    scopus 로고
    • A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom
    • Lee, S. Y.; MacKinnon, R. A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature, 2004, 430(6996), 232-5.
    • (2004) Nature , vol.430 , Issue.6996 , pp. 232-235
    • Lee, S.Y.1    McKinnon, R.2
  • 249
    • 17644381598 scopus 로고    scopus 로고
    • Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel
    • Jung, H. J.; Lee, J. Y.; Kim, S. H.; Eu, Y. J.; Shin, S. Y.; Milescu, M.; Swartz, K. J.; Kim, J. I. Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel. Biochemistry, 2005, 44(16), 6015-23.
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6015-6023
    • Jung, H.J.1    Lee, J.Y.2    Kim, S.H.3    Eu, Y.J.4    Shin, S.Y.5    Milescu, M.6    Swartz, K.J.7    Kim, J.I.8
  • 250
    • 0030872270 scopus 로고    scopus 로고
    • Site-directed mutagenesis of dendrotoxin K reveals amino acids critical for its interaction with neuronal K+ channels
    • Smith, L. A.; Reid, P. F.; Wang, F. C.; Parcej, D. N.; Schmidt, J. J.; Olson, M. A.; Dolly, J. O. Site-directed mutagenesis of dendrotoxin K reveals amino acids critical for its interaction with neuronal K+ channels. Biochemistry, 1997, 36(25), 7690-6.
    • (1997) Biochemistry , vol.36 , Issue.25 , pp. 7690-7696
    • Smith, L.A.1    Reid, P.F.2    Wang, F.C.3    Parcej, D.N.4    Schmidt, J.J.5    Olson, M.A.6    Dolly, J.O.7
  • 251
    • 0034628896 scopus 로고    scopus 로고
    • Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel
    • Imredy, J. P.; MacKinnon, R. Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel. J. Mol. Biol., 2000, 296(5), 1283-94.
    • (2000) J. Mol. Biol , vol.296 , Issue.5 , pp. 1283-1294
    • Imredy, J.P.1    McKinnon, R.2
  • 252
    • 0034628896 scopus 로고    scopus 로고
    • Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel
    • Imredy, J. P.; MacKinnon R. Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel. J. mol. boil., 2000, 296(5), 1283-94.
    • (2000) J. mol. boil , vol.296 , Issue.5 , pp. 1283-1294
    • Imredy, J.P.1    McKinnon, R.2
  • 253
    • 15644375485 scopus 로고    scopus 로고
    • Delineation of the functional site of alpha-dendrotoxin. The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channelblocking toxins
    • Gasparini, S.; Danse, J. M.; Lecoq, A.; Pinkasfeld, S.; Zinn-Justin, S.; Young, L. C.; de Medeiros, C. C.; Rowan, E. G.; Harvey, a. L.; Ménez, A. Delineation of the functional site of alpha-dendrotoxin. The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channelblocking toxins. J. boil. chem., 1998, 273(39), 25393-403.
    • (1998) J. boil. chem , vol.273 , Issue.39 , pp. 25393-25403
    • Gasparini, S.1    Danse, J.M.2    Lecoq, A.3    Pinkasfeld, S.4    Zinn-Justin, S.5    Young, L.C.6    de Medeiros, C.C.7    Rowan, E.G.8    Harvey, L.9    Ménez, A.10
  • 255
    • 23844434005 scopus 로고    scopus 로고
    • Small vertical movement of a K+ channel voltage sensor measured with luminescence energy transfer
    • Posson, D. J.; Ge, P.; Miller, C.; Bezanilla, F.; Selvin, P. R. Small vertical movement of a K+ channel voltage sensor measured with luminescence energy transfer. Nature, 2005, 436(7052), 848-51.
    • (2005) Nature , vol.436 , Issue.7052 , pp. 848-851
    • Posson, D.J.1    Ge, P.2    Miller, C.3    Bezanilla, F.4    Selvin, P.R.5
  • 256
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestèle, S.; Catterall, W. a. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie, 2000, 82(9-10), 883-92.
    • (2000) Biochimie , vol.82 , Issue.9-10 , pp. 883-892
    • Cestèle, S.1    Catterall, W.A.2
  • 257
    • 55549098112 scopus 로고    scopus 로고
    • Interaction of ladder-shaped polyethers with transmembrane??-helix of glycophorin A as evidenced by saturation transfer difference NMR and surface plasmon resonance
    • Ujihara, S.; Oishi, T.; Torikai, K.; Konoki, K.; Matsumori, N.; Murata, M.; Oshima, Y.; Aimoto, S. Interaction of ladder-shaped polyethers with transmembrane??-helix of glycophorin A as evidenced by saturation transfer difference NMR and surface plasmon resonance. Bioorg. Med. Chem. Lett., 2008, 18(23), 6115-8.
    • (2008) Bioorg. Med. Chem. Lett , vol.18 , Issue.23 , pp. 6115-6118
    • Ujihara, S.1    Oishi, T.2    Torikai, K.3    Konoki, K.4    Matsumori, N.5    Murata, M.6    Oshima, Y.7    Aimoto, S.8
  • 258
    • 84878778505 scopus 로고    scopus 로고
    • Scorpion beta-toxins and voltage-gated sodium channels: Interactions and effects
    • Pedraza, Escalona M.; Possani, L. D. Scorpion beta-toxins and voltage-gated sodium channels: interactions and effects. Front. Biosci. (Landmark Ed), 2013, 18, 572-87.
    • (2013) Front. Biosci. (Landmark Ed) , vol.18 , pp. 572-587
    • Pedraza Escalona, M.1    Possani, L.D.2
  • 259
    • 33746369777 scopus 로고    scopus 로고
    • Structure and function of the voltage sensor of sodium channels probed by a beta-scorpion toxin
    • Cestele, S.; Yarov-Yarovoy, V.; Qu, Y.; Sampieri, F.; Scheuer, T.; Catterall, W. A. Structure and function of the voltage sensor of sodium channels probed by a beta-scorpion toxin. J. Biol. Chem., 2006, 281(30), 21332-44.
    • (2006) J. Biol. Chem , vol.281 , Issue.30 , pp. 21332-21344
    • Cestele, S.1    Yarov-Yarovoy, V.2    Qu, Y.3    Sampieri, F.4    Scheuer, T.5    Catterall, W.A.6
  • 260
    • 0030037704 scopus 로고    scopus 로고
    • Molecular Determinants of High Affinity Binding of-Scorpion Toxin and Sea Anemone Toxin in the S3-S4 Extracellular Loop in Domain IV of the Na+ Channel Subunit
    • Rogers, J. C.; Qu, Y.; Tanada, T. N.; Scheuer, T.; Catterall, W. A. Molecular Determinants of High Affinity Binding of-Scorpion Toxin and Sea Anemone Toxin in the S3-S4 Extracellular Loop in Domain IV of the Na+ Channel Subunit. J. Biol. Chem., 1996, 271(27), 15950-62.
    • (1996) J. Biol. Chem , vol.271 , Issue.27 , pp. 15950-15962
    • Rogers, J.C.1    Qu, Y.2    Tanada, T.N.3    Scheuer, T.4    Catterall, W.A.5
  • 261
    • 0030010219 scopus 로고    scopus 로고
    • Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel
    • Dias-Kadambi, B. L.; Drum, C. L.; Hanck, D. A.; Blumenthal, K. M. Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel. J. Biol. Chem., 1996, 271(16), 9422-8.
    • (1996) J. Biol. Chem , vol.271 , Issue.16 , pp. 9422-9428
    • Dias-Kadambi, B.L.1    Drum, C.L.2    Hanck, D.A.3    Blumenthal, K.M.4
  • 262
    • 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(18), 3881-4.
    • (2005) FEBS lett , vol.579 , Issue.18 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 263
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • Terlau, H.; Olivera, B. M. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol. Rev., 2004, 84(1), 41-68.
    • (2004) Physiol. Rev , vol.84 , Issue.1 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 264
    • 0033767401 scopus 로고    scopus 로고
    • A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels
    • Winterfield, J. R.; Swartz, K. J. A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels. J. gen. physio., 2000, 116(5), 637-44.
    • (2000) J. gen. physio , vol.116 , Issue.5 , pp. 637-644
    • Winterfield, J.R.1    Swartz, K.J.2
  • 265
    • 0030037704 scopus 로고    scopus 로고
    • Molecular determinants of high affinity binding of alpha-scorpion toxin and sea anemone toxin in the S3-S4 extracellular loop in domain IV of the Na+ channel alpha subunit
    • Rogers, J. C.; Qu, Y.; Tanada, T. N.; Scheuer, T.; Catterall, W. A. Molecular determinants of high affinity binding of alpha-scorpion toxin and sea anemone toxin in the S3-S4 extracellular loop in domain IV of the Na+ channel alpha subunit. j. biol. chem., 1996, 271(27), 15950-62.
    • (1996) J. biol. chem , vol.271 , Issue.27 , pp. 15950-15962
    • Rogers, J.C.1    Qu, Y.2    Tanada, T.N.3    Scheuer, T.4    Catterall, W.A.5
  • 266
    • 0028850614 scopus 로고
    • Comparative actions of synthetic omegagrammotoxin SIA and synthetic omega-Aga-IVA on neuronal calcium entry and evoked release of neurotransmitters in vitro and in vivo
    • Keith, R. A.; Mangano, T. J.; Lampe, R. A.; DeFeo, P. A.; Hyde, M. J.; Donzanti, B. A. Comparative actions of synthetic omegagrammotoxin SIA and synthetic omega-Aga-IVA on neuronal calcium entry and evoked release of neurotransmitters in vitro and in vivo. Neuropharmacology, 1995, 34(11), 1515-28.
    • (1995) Neuropharmacology , vol.34 , Issue.11 , pp. 1515-1528
    • Keith, R.A.1    Mangano, T.J.2    Lampe, R.A.3    DeFeo, P.A.4    Hyde, M.J.5    Donzanti, B.A.6
  • 267
    • 0027186445 scopus 로고
    • Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses
    • Lampe, R.; Defeo, P.; Davison, M.; Young, J.; Herman, J.; Spreen, R.; Horn, M.; Mangano, T.; Keith, R. Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses. Mol. Pharmacol., 1993, 44(2), 451-60.
    • (1993) Mol. Pharmacol , vol.44 , Issue.2 , pp. 451-460
    • Lampe, R.1    Defeo, P.2    Davison, M.3    Young, J.4    Herman, J.5    Spreen, R.6    Horn, M.7    Mangano, T.8    Keith, R.9
  • 268
    • 0032249498 scopus 로고    scopus 로고
    • Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin
    • Chuang, R. S.; Jaffe, H.; Cribbs, L.; Perez-Reyes, E.; Swartz, K. J. Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin. Nat. Neurosci., 1998, 1(8), 668-74.
    • (1998) Nat. Neurosci , vol.1 , Issue.8 , pp. 668-674
    • Chuang, R.S.1    Jaffe, H.2    Cribbs, L.3    Perez-Reyes, E.4    Swartz, K.J.5
  • 271
    • 0034022011 scopus 로고    scopus 로고
    • Block of voltagedependent calcium channel by the green mamba toxin calcicludine
    • Stotz, S. C.; Spaetgens, R. L.; Zamponi, G. W. Block of voltagedependent calcium channel by the green mamba toxin calcicludine. J. memb. boil., 2000, 174(2), 157-65.
    • (2000) J. memb. boil , vol.174 , Issue.2 , pp. 157-165
    • Stotz, S.C.1    Spaetgens, R.L.2    Zamponi, G.W.3
  • 272
    • 34250802056 scopus 로고    scopus 로고
    • Calcicludine binding to the outer pore of L-type calcium channels is allosterically coupled to dihydropyridine binding
    • Wang, X.; Du, L.; Peterson, B. Z. Calcicludine binding to the outer pore of L-type calcium channels is allosterically coupled to dihydropyridine binding. Biochemistry, 2007, 46(25), 7590-8.
    • (2007) Biochemistry , vol.46 , Issue.25 , pp. 7590-7598
    • Wang, X.1    Du, L.2    Peterson, B.Z.3
  • 274
    • 59449083489 scopus 로고    scopus 로고
    • Properties of the inner pore region of TRPV1 channels revealed by block with quaternary ammoniums
    • Jara-Oseguera, A.; Llorente, I.; Rosenbaum, T.; Islas, L. D. Properties of the inner pore region of TRPV1 channels revealed by block with quaternary ammoniums. J. Gen. Physiol., 2008, 132(5), 547-62.
    • (2008) J. Gen. Physiol , vol.132 , Issue.5 , pp. 547-562
    • Jara-Oseguera, A.1    Llorente, I.2    Rosenbaum, T.3    Islas, L.D.4
  • 277
    • 34447515681 scopus 로고    scopus 로고
    • Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1)
    • Susankova, K.; Ettrich, R.; Vyklicky, L.; Teisinger, J.; Vlachova, V. Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1). J. Neurosci., 2007, 27(28), 7578-85.
    • (2007) J. Neurosci , vol.27 , Issue.28 , pp. 7578-7585
    • Susankova, K.1    Ettrich, R.2    Vyklicky, L.3    Teisinger, J.4    Vlachova, V.5
  • 278
    • 0014877189 scopus 로고
    • Use of a snake venom toxin to characterize the cholinergic receptor protein
    • Changeux, J. P.; Kasai, M.; Lee, C. Y. Use of a snake venom toxin to characterize the cholinergic receptor protein. Proc. Natl. Acad. Sci. U S A, 1970, 67(3), 1241-7.
    • (1970) Proc. Natl. Acad. Sci. U S A , vol.67 , Issue.3 , pp. 1241-1247
    • Changeux, J.P.1    Kasai, M.2    Lee, C.Y.3
  • 279
    • 0015853065 scopus 로고
    • Purification and molecular properties of the acetylcholine receptor from Torpedo electroplax
    • Eldefrawi, M. E.; Eldefrawi, A. T. Purification and molecular properties of the acetylcholine receptor from Torpedo electroplax. Arch. Biochem. Biophys., 1973, 159(1), 362-73.
    • (1973) Arch. Biochem. Biophys , vol.159 , Issue.1 , pp. 362-373
    • Eldefrawi, M.E.1    Eldefrawi, A.T.2
  • 280
    • 0022297959 scopus 로고
    • Determination of the primary amino acid sequence specifying the alpha-bungarotoxin binding site on the alpha subunit of the acetylcholine receptor from Torpedo californica
    • Wilson, P. T.; Lentz, T. L.; Hawrot, E. Determination of the primary amino acid sequence specifying the alpha-bungarotoxin binding site on the alpha subunit of the acetylcholine receptor from Torpedo californica. Proc. Natl. Acad. Sci. U S A, 1985, 82(24), 8790-4.
    • (1985) Proc. Natl. Acad. Sci. U S A , vol.82 , Issue.24 , pp. 8790-8794
    • Wilson, P.T.1    Lentz, T.L.2    Hawrot, E.3
  • 281
    • 0027371744 scopus 로고
    • NMR solution structure of an alpha-bungarotoxin/nicotinic receptor peptide complex
    • Basus, V. J.; Song, G.; Hawrot, E. NMR solution structure of an alpha-bungarotoxin/nicotinic receptor peptide complex. Biochemistry, 1993, 32(46), 12290-8.
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12290-12298
    • Basus, V.J.1    Song, G.2    Hawrot, E.3
  • 282
    • 0037130458 scopus 로고    scopus 로고
    • The mechanism for acetylcholine receptor inhibition by alphaneurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR
    • Samson, A.; Scherf, T.; Eisenstein, M.; Chill, J.; Angliste, J. The mechanism for acetylcholine receptor inhibition by alphaneurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR. Neuron, 2002, 35(2), 319-32.
    • (2002) Neuron , vol.35 , Issue.2 , pp. 319-332
    • Samson, A.1    Scherf, T.2    Eisenstein, M.3    Chill, J.4    Angliste, J.5
  • 283
    • 0035933887 scopus 로고    scopus 로고
    • The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica
    • Zeng, H.; Moise, L.; Grant, M. A.; Hawrot, E. The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica. J. Biol. Chem., 2001, 276(25), 22930-40.
    • (2001) J. Biol. Chem , vol.276 , Issue.25 , pp. 22930-22940
    • Zeng, H.1    Moise, L.2    Grant, M.A.3    Hawrot, E.4
  • 285
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1. 94 A resolution
    • Dellisanti, C. D.; Yao, Y.; Stroud, J. C.; Wang, Z. Z.; Chen, L. Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1. 94 A resolution. Nat. Neurosci., 2007, 10(8), 953-62.
    • (2007) Nat. Neurosci , vol.10 , Issue.8 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.Z.4    Chen, L.5
  • 286
    • 84881515004 scopus 로고    scopus 로고
    • Complex between alpha-bungarotoxin and an alpha7 nicotinic receptor ligand-binding domain chimaera
    • Huang, S.; Li, S. X.; Bren, N.; Cheng, K.; Gomoto, R.; Chen, L.; Sine, S. M. Complex between alpha-bungarotoxin and an alpha7 nicotinic receptor ligand-binding domain chimaera. Biochem. J., 2013, 454(2), 303-10.
    • (2013) Biochem. J , vol.454 , Issue.2 , pp. 303-310
    • Huang, S.1    Li, S.X.2    Bren, N.3    Cheng, K.4    Gomoto, R.5    Chen, L.6    Sine, S.M.7
  • 287
    • 41449097191 scopus 로고    scopus 로고
    • Inhibition mechanism of the acetylcholine receptor by alpha-neurotoxins as revealed by normal-mode dynamics
    • Samson, A. O.; Levitt, M. Inhibition mechanism of the acetylcholine receptor by alpha-neurotoxins as revealed by normal-mode dynamics. Biochemistry, 2008, 47(13), 4065-70.
    • (2008) Biochemistry , vol.47 , Issue.13 , pp. 4065-4070
    • Samson, A.O.1    Levitt, M.2
  • 288
    • 0038711752 scopus 로고    scopus 로고
    • Alpha-conotoxins PnIA and [A10L]PnIA stabilize different states of the alpha7-L247T nicotinic acetylcholine receptor
    • Hogg, R. C.; Hopping, G.; Alewood, P. F.; Adams, D. J.; Bertrand, D. Alpha-conotoxins PnIA and [A10L]PnIA stabilize different states of the alpha7-L247T nicotinic acetylcholine receptor. J. Biol. Chem., 2003, 278(29), 26908-14.
    • (2003) J. Biol. Chem , vol.278 , Issue.29 , pp. 26908-26914
    • Hogg, R.C.1    Hopping, G.2    Alewood, P.F.3    Adams, D.J.4    Bertrand, D.5
  • 289
    • 33748756414 scopus 로고    scopus 로고
    • Alpha-conotoxin analogs with additional positive charge show increased selectivity towards Torpedo californica and some neuronal subtypes of nicotinic acetylcholine receptors
    • Kasheverov, I. E.; Zhmak, M. N.; Vulfius, C. A.; Gorbacheva, E. V.; Mordvintsev, D. Y.; Utkin, Y. N.; van Elk R., Smit A. B.; Tsetlin, V. I. Alpha-conotoxin analogs with additional positive charge show increased selectivity towards Torpedo californica and some neuronal subtypes of nicotinic acetylcholine receptors. FEBS J., 2006, 273(19), 4470-81.
    • (2006) FEBS J , vol.273 , Issue.19 , pp. 4470-4481
    • Kasheverov, I.E.1    Zhmak, M.N.2    Vulfius, C.A.3    Gorbacheva, E.V.4    Mordvintsev, D.Y.5    Utkin, Y.N.6    van Elk, R.7    Smit, A.B.8    Tsetlin, V.I.9
  • 290
    • 84879622348 scopus 로고    scopus 로고
    • Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold
    • Gao, B.; Harvey, P. J.; Craik, D. J.; Ronjat, M.; De, Waard M.; Zhu, S. Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold. Biosci. Rep., 2013, 33(3).
    • (2013) Biosci. Rep , vol.33 , Issue.3
    • Gao, B.1    Harvey, P.J.2    Craik, D.J.3    Ronjat, M.4    De Waard, M.5    Zhu, S.6
  • 291
    • 52949110988 scopus 로고    scopus 로고
    • Animal toxins acting on voltage-gated potassium channels
    • Mouhat, S.; Andreotti, N.; Jouirou, B.; Sabatier, J. M. Animal toxins acting on voltage-gated potassium channels. Curr. Pharm. Des., 2008, 14(24), 2503-18.
    • (2008) Curr. Pharm. Des , vol.14 , Issue.24 , pp. 2503-2518
    • Mouhat, S.1    Andreotti, N.2    Jouirou, B.3    Sabatier, J.M.4
  • 293
    • 34548214197 scopus 로고    scopus 로고
    • Is lipid bilayer binding a common property of inhibitor cysteine knot ion-channel blockers?
    • Posokhov, Y. O.; Gottlieb, P. A.; Morales, M. J.; Sachs, F.; Ladokhin, A. S. Is lipid bilayer binding a common property of inhibitor cysteine knot ion-channel blockers? Biophys. J., 2007, 93(4), L20-2.
    • (2007) Biophys. J , vol.93 , Issue.4 , pp. 20-22
    • Posokhov, Y.O.1    Gottlieb, P.A.2    Morales, M.J.3    Sachs, F.4    Ladokhin, A.S.5
  • 294
    • 79960498823 scopus 로고    scopus 로고
    • The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4
    • Bae, C.; Sachs, F.; Gottlieb, P. A. The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4. Biochemistry, 2011, 50(29), 6295-300.
    • (2011) Biochemistry , vol.50 , Issue.29 , pp. 6295-6300
    • Bae, C.1    Sachs, F.2    Gottlieb, P.A.3
  • 295
    • 78349242176 scopus 로고    scopus 로고
    • Effects of GsMTx4 on bacterial mechanosensitive channels in inside-out patches from giant spheroplasts
    • Kamaraju, K.; Gottlieb, P. A.; Sachs, F.; Sukharev, S. Effects of GsMTx4 on bacterial mechanosensitive channels in inside-out patches from giant spheroplasts. Biophys. J., 2010, 99(9), 2870-8.
    • (2010) Biophys. J , vol.99 , Issue.9 , pp. 2870-2878
    • Kamaraju, K.1    Gottlieb, P.A.2    Sachs, F.3    Sukharev, S.4
  • 296
    • 84883041172 scopus 로고    scopus 로고
    • Human PIEZO1: Removing inactivation
    • Bae, C.; Gottlieb, P. A.; Sachs, F. Human PIEZO1: removing inactivation. Biophys. J., 2013, 105(4), 880-6.
    • (2013) Biophys. J , vol.105 , Issue.4 , pp. 880-886
    • Bae, C.1    Gottlieb, P.A.2    Sachs, F.3


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