메뉴 건너뛰기




Volumn 64, Issue 2, 2012, Pages 259-298

Conus venom peptide pharmacology

Author keywords

[No Author keywords available]

Indexed keywords

ALANYLCYSTEINYLSERYLLYSLLYSLTRYPTOPHYLGLUTAMYLTYROSYLCYSTEINYLISOLEUCYLVALYLPROLYLISOLEUCYLISOLEUCYLGLYCYLPHENYLALANYLISOLEUCYLTYROSYLCYSTEINYLCYSTEINYLPROLYLGLYCLLEUCYLISOLEUCYLCYSTEINYLGLYCYLPROLYLPHENYLALANYLLVALYLCYSTEINYLVALINE; ASPARAGINYLCYSTEINYLCYSTEINYLASPARAGINYLGLYCYLGLCYLCYSTEINYLSERYLSERYLLYSYLTRYPTOPHYLCYSTEINYLASPARTYLHISTIDYLALANYLARGINYLCYSTEINYLCYSTEINE; ASPARTYLASPARTYLCYSTEINYLISOLEUCYLLYSYLTYROSYLGLYCYLPHENYLALANYLCYSTEINYLSERYLLEUCYLPROLYLISOLEUCYLLYSYLASPARAGINYLGLYCYLALANYLCYTEINYLCYSTEINYLSERYLGLYCYLALANYLCYTEINYLVALYLGLYCYLVALYLCYSTEINYLALANYLASPARTYLLEUCINE; CYSTEINYLARGINYLISOLEUCYLASPARAGINYLGLUTAMINYLLYSYLCYSTEINYLPHENYLALANYLGLUTAMINYLHISTIDYLLEUCYLASPARTYLASPARTYLCYSTEINYLCYSTEINYLSERYLARGINYLLYSYLCYSTEINYLASPARAGINYLASPARAGINYLARGINYLPHENYLALANYLASPARAGINYLLYSYLCYSTEINYLVALINE; CYSTEINYLLYSYLGLYCYLLYSYLGLYCYLALANYLLYSYLCYSTEINYLSERYLARGINYLLEUCYLMETHIONYLTYROSYLASPARTYLCYSTEINYLTHREONYLGLYCYLSERYLGLYCYLSERYLCYSTEINYLARGINYLSERLYGLYCYLLYSYLCYSTEINE; G PROTEIN COUPLED RECEPTOR; GLYCYLCYSTEINYLTHREONYLARGINYLTHREONYLCYSTEINYLGLYCYLGLYCYLLYSYLCYSTEINYLTHREONYLGLYCYLTHREONYLCYSTEINYLTHREONYLCYSTEINYLTHREONYLASPARAGINYLSERYLSERYLLYSYLCYSTEINYLGLYCYLARGINYLTYROSYLASPARAGINYLVALYLALANYLPROLYLSERYLGLYCYLGLCYLCYSTEINYLGLYCYSTEINE; GLYCYLVALYLLCYSTEINYLCYSTEINYLGLYCYLTYROSYLLYSYSLCYSTEINYLHISTIDYLCYSTEINE; ION CHANNEL; NEUROTRANSMITTER; PEPTIDE DERIVATIVE; PHENYLALALNYLASPARAGINYLTRYTOPHYLARGINYLCYSTEINYLCYSTEINYLLEUCYLISOLEUCYLPROLYLALANYLCYSTEINYLARGINYLARGINYLASPARAGINYLHISTIDYLLYSYLLYSYLCYSTEINE; UNCLASSIFIED DRUG; VOLTAGE GATED ION CHANNEL;

EID: 84858178207     PISSN: 00316997     EISSN: 15210081     Source Type: Journal    
DOI: 10.1124/pr.111.005322     Document Type: Review
Times cited : (377)

References (416)
  • 1
    • 0028181746 scopus 로고
    • Different ω-conotoxins mark the development of Swiss Webster mouse cortex suggesting N-type voltage sensitive calcium channel subtypes
    • Abbott JR and Litzinger MJ (1994) Different ω-conotoxins mark the development of Swiss Webster mouse cortex suggesting N-type voltage sensitive calcium channel subtypes. Int J Dev Neurosci 12:43-47.
    • (1994) Int J Dev Neurosci , vol.12 , pp. 43-47
    • Abbott, J.R.1    Litzinger, M.J.2
  • 2
    • 0023655647 scopus 로고
    • Identification of the receptor for ω-conotoxin in brain. Probable components of the calcium channel
    • Abe T and Saisu H (1987) Identification of the receptor for ω-conotoxin in brain. Probable components of the calcium channel. J Biol Chem 262:9877-9882.
    • (1987) J Biol Chem , vol.262 , pp. 9877-9882
    • Abe, T.1    Saisu, H.2
  • 9
    • 34249103242 scopus 로고    scopus 로고
    • An assessment of the antinociceptive efficacy of intrathecal and epidural contulakin-G in rats and dogs
    • Allen JW, Hofer K, McCumber D, Wagstaff JD, Layer RT, McCabe RT, and Yaksh TL (2007) An assessment of the antinociceptive efficacy of intrathecal and epidural contulakin-G in rats and dogs. Anesth Analg 104:1505-1513.
    • (2007) Anesth Analg , vol.104 , pp. 1505-1513
    • Allen, J.W.1    Hofer, K.2    McCumber, D.3    Wagstaff, J.D.4    Layer, R.T.5    McCabe, R.T.6    Yaksh, T.L.7
  • 12
  • 14
    • 12844251304 scopus 로고    scopus 로고
    • α-Conotoxin BuIA, a novel peptide from Conus bullatus, distinguishes among neuronal nicotinic acetylcholine receptors
    • Azam L, Dowell C, Watkins M, Stitzel JA, Olivera BM, and McIntosh JM (2005) α-Conotoxin BuIA, a novel peptide from Conus bullatus, distinguishes among neuronal nicotinic acetylcholine receptors. J Biol Chem 280:80-87.
    • (2005) J Biol Chem , vol.280 , pp. 80-87
    • Azam, L.1    Dowell, C.2    Watkins, M.3    Stitzel, J.A.4    Olivera, B.M.5    McIntosh, J.M.6
  • 15
    • 0034671899 scopus 로고    scopus 로고
    • lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus
    • Balaji RA, Ohtake A, Sato K, Gopalakrishnakone P, Kini RM, Seow KT, and Bay BH (2000) lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus. J Biol Chem 275:39516-39522.
    • (2000) J Biol Chem , vol.275 , pp. 39516-39522
    • Balaji, R.A.1    Ohtake, A.2    Sato, K.3    Gopalakrishnakone, P.4    Kini, R.M.5    Seow, K.T.6    Bay, B.H.7
  • 16
    • 0032504712 scopus 로고    scopus 로고
    • ABT-594, a novel cholinergic channel modulator, is efficacious in nerve ligation and diabetic neuropathy models of neuropathic pain
    • Bannon AW, Decker MW, Kim DJ, Campbell JE, and Arneric SP (1998) ABT-594, a novel cholinergic channel modulator, is efficacious in nerve ligation and diabetic neuropathy models of neuropathic pain. Brain Res 801:158-163.
    • (1998) Brain Res , vol.801 , pp. 158-163
    • Bannon, A.W.1    Decker, M.W.2    Kim, D.J.3    Campbell, J.E.4    Arneric, S.P.5
  • 18
    • 77953235348 scopus 로고    scopus 로고
    • The anti-allodynic α2δ ligand pregabalin inhibits the trafficking of the calcium channel α2δ-1 subunit to presynaptic terminals in vivo
    • Bauer CS, Rahman W, Tran-van-Minh A, Lujan R, Dickenson AH, and Dolphin AC (2010) The anti-allodynic α2δ ligand pregabalin inhibits the trafficking of the calcium channel α2δ-1 subunit to presynaptic terminals in vivo. Biochem Soc Trans 38:525-528.
    • (2010) Biochem Soc Trans , vol.38 , pp. 525-528
    • Bauer, C.S.1    Rahman, W.2    Tran-van-Minh, A.3    Lujan, R.4    Dickenson, A.H.5    Dolphin, A.C.6
  • 20
    • 0026657359 scopus 로고
    • Action of derivatives of μ-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 AG, Gordon RD, and French RJ (1992) Action of derivatives of μ-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry 31:8229-8238.
    • (1992) Biochemistry , vol.31 , 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
  • 21
    • 0347224274 scopus 로고    scopus 로고
    • Cell-specific alternative splicing increases calcium channel current density in the pain pathway
    • Bell TJ, Thaler C, Castiglioni AJ, Helton TD, and Lipscombe D (2004) Cell-specific alternative splicing increases calcium channel current density in the pain pathway. Neuron 41:127-138.
    • (2004) Neuron , vol.41 , pp. 127-138
    • Bell, T.J.1    Thaler, C.2    Castiglioni, A.J.3    Helton, T.D.4    Lipscombe, D.5
  • 25
    • 58149232445 scopus 로고    scopus 로고
    • Multiple sodium channel isoforms and mitogen-activated protein kinases are present in painful human neuromas
    • Black JA, Nikolajsen L, Kroner K, Jensen TS, and Waxman SG (2008) Multiple sodium channel isoforms and mitogen-activated protein kinases are present in painful human neuromas. Ann Neurol 64:644-653.
    • (2008) Ann Neurol , vol.64 , pp. 644-653
    • Black, J.A.1    Nikolajsen, L.2    Kroner, K.3    Jensen, T.S.4    Waxman, S.G.5
  • 28
    • 79960271986 scopus 로고    scopus 로고
    • Functional properties and toxin pharmacology of a dorsal root ganglion sodium channel viewed through its voltage sensors
    • Bosmans F, Puopolo M, Martin-Eauclaire MF, Bean BP, and Swartz KJ (2011) Functional properties and toxin pharmacology of a dorsal root ganglion sodium channel viewed through its voltage sensors. J Gen Physiol 138:59-72.
    • (2011) J Gen Physiol , vol.138 , pp. 59-72
    • Bosmans, F.1    Puopolo, M.2    Martin-Eauclaire, M.F.3    Bean, B.P.4    Swartz, K.J.5
  • 29
    • 0030434482 scopus 로고    scopus 로고
    • Selective N-type neuronal voltage-sensitive calcium channel blocker, SNX-111, produces spinal antinociception in rat models of acute, persistent and neuropathic pain
    • Bowersox SS, Gadbois T, Singh T, Pettus M, Wang YX, and Luther RR (1996) Selective N-type neuronal voltage-sensitive calcium channel blocker, SNX-111, produces spinal antinociception in rat models of acute, persistent and neuropathic pain. J Pharmacol Exp Ther 279:1243-1249.
    • (1996) J Pharmacol Exp Ther , vol.279 , pp. 1243-1249
    • Bowersox, S.S.1    Gadbois, T.2    Singh, T.3    Pettus, M.4    Wang, Y.X.5    Luther, R.R.6
  • 30
    • 0032987252 scopus 로고    scopus 로고
    • Selective NMDA NR2B antagonists induce antinociception without motor dysfunction: Correlation with restricted localisation of NR2B subunit in dorsal horn
    • Boyce S, Wyatt A, Webb JK, O'Donnell R, Mason G, Rigby M, Sirinathsinghji D, Hill RG, and Rupniak NM (1999) Selective NMDA NR2B antagonists induce antinociception without motor dysfunction: correlation with restricted localisation of NR2B subunit in dorsal horn. Neuropharmacology 38:611-623.
    • (1999) Neuropharmacology , vol.38 , pp. 611-623
    • Boyce, S.1    Wyatt, A.2    Webb, J.K.3    O'Donnell, R.4    Mason, G.5    Rigby, M.6    Sirinathsinghji, D.7    Hill, R.G.8    Rupniak, N.M.9
  • 38
    • 75749113276 scopus 로고    scopus 로고
    • Analgesic α-conotoxins Vc1.1 and RgIA inhibit N-type calcium channels in sensory neurons of α9 nicotinic receptor knockout mice
    • Callaghan B and Adams DJ (2010) Analgesic α-conotoxins Vc1.1 and RgIA inhibit N-type calcium channels in sensory neurons of α9 nicotinic receptor knockout mice. Channels (Austin) 4:51-54.
    • (2010) Channels (Austin) , vol.4 , pp. 51-54
    • Callaghan, B.1    Adams, D.J.2
  • 41
    • 78049359992 scopus 로고    scopus 로고
    • Signaling complexes of voltage-gated sodium and calcium channels
    • Catterall WA (2010) Signaling complexes of voltage-gated sodium and calcium channels. Neurosci Lett 486:107-116.
    • (2010) Neurosci Lett , vol.486 , pp. 107-116
    • Catterall, W.A.1
  • 43
    • 29844438166 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels
    • Catterall WA, Goldin AL, and Waxman SG (2005a) International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels. Pharmacol Rev 57:397-409.
    • (2005) Pharmacol Rev , vol.57 , pp. 397-409
    • Catterall, W.A.1    Goldin, A.L.2    Waxman, S.G.3
  • 44
    • 29844439240 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels
    • Catterall WA, Perez-Reyes E, Snutch TP, and Striessnig J (2005b) International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels. Pharmacol Rev 57:411-425.
    • (2005) Pharmacol Rev , vol.57 , pp. 411-425
    • Catterall, W.A.1    Perez-Reyes, E.2    Snutch, T.P.3    Striessnig, J.4
  • 46
    • 0029417234 scopus 로고
    • Characterizing the μ-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations
    • Chahine M, Chen LQ, Fotouhi N, Walsky R, Fry D, Santarelli V, Horn R, and Kallen RG (1995) Characterizing the μ-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations. Receptors Channels 3:161-174.
    • (1995) Receptors Channels , vol.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
  • 48
    • 34547953003 scopus 로고    scopus 로고
    • v2.2 channels to voltage-dependent inactivation: Dynamic palmitoylation and voltage sensitivity
    • Chan AW, Owens S, Tung C, and Stanley EF (2007) Resistance of presynaptic Cav2.2 channels to voltage-dependent inactivation: dynamic palmitoylation and voltage sensitivity. Cell Calcium 42:419-425.
    • (2007) Cell Calcium , vol.42 , pp. 419-425
    • Chan, A.W.1    Owens, S.2    Tung, C.3    Stanley, E.F.4
  • 50
    • 77952033673 scopus 로고    scopus 로고
    • v1.2 channel blocker: Evaluation of cardioprotective effects of κM-conotoxins
    • Chen P, Dendorfer A, Finol-Urdaneta RK, Terlau H, and Olivera BM (2010) Biochemical characterization of κM-RIIIJ, a Kv1.2 channel blocker: evaluation of cardioprotective effects of κM-conotoxins. J Biol Chem 285:14882-14889.
    • (2010) J Biol Chem , vol.285 , pp. 14882-14889
    • Chen, P.1    Dendorfer, A.2    Finol-Urdaneta, R.K.3    Terlau, H.4    Olivera, B.M.5
  • 51
    • 33646588654 scopus 로고    scopus 로고
    • Pharmacological insights obtained from structurefunction studies of ionotropic glutamate receptors
    • Chen PE and Wyllie DJ (2006) Pharmacological insights obtained from structurefunction studies of ionotropic glutamate receptors. Br J Pharmacol 147:839-853.
    • (2006) Br J Pharmacol , vol.147 , pp. 839-853
    • Chen, P.E.1    Wyllie, D.J.2
  • 52
    • 4143122196 scopus 로고    scopus 로고
    • Subtype-selective noncompetitive or competitive inhibition of human α1-adrenergic receptors by ρ-TIA
    • Chen Z, Rogge G, Hague C, Alewood D, Colless B, Lewis RJ, and Minneman KP (2004) Subtype-selective noncompetitive or competitive inhibition of human α1-adrenergic receptors by ρ-TIA. J Biol Chem 279:35326-35333.
    • (2004) J Biol Chem , vol.279 , pp. 35326-35333
    • Chen, Z.1    Rogge, G.2    Hague, C.3    Alewood, D.4    Colless, B.5    Lewis, R.J.6    Minneman, K.P.7
  • 59
    • 0028973158 scopus 로고
    • Cloning and characterization of chi-1: A developmentally regulated member of a novel class of the ionotropic glutamate receptor family
    • Ciabarra AM, Sullivan JM, Gahn LG, Pecht G, Heinemann S, and Sevarino KA (1995) Cloning and characterization of chi-1: a developmentally regulated member of a novel class of the ionotropic glutamate receptor family. J Neurosci 15:6498-6508.
    • (1995) J Neurosci , vol.15 , pp. 6498-6508
    • Ciabarra, A.M.1    Sullivan, J.M.2    Gahn, L.G.3    Pecht, G.4    Heinemann, S.5    Sevarino, K.A.6
  • 60
    • 33747372837 scopus 로고    scopus 로고
    • The synthesis, structural characterization, and receptor specificity of the α-conotoxin Vc1.1
    • Clark RJ, Fischer H, Nevin ST, Adams DJ, and Craik DJ (2006) The synthesis, structural characterization, and receptor specificity of the α-conotoxin Vc1.1. J Biol Chem 281:23254-23263.
    • (2006) J Biol Chem , vol.281 , pp. 23254-23263
    • Clark, R.J.1    Fischer, H.2    Nevin, S.T.3    Adams, D.J.4    Craik, D.J.5
  • 62
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: A novel approach for the treatment of CNS disorders
    • Conn PJ, Christopoulos A, and Lindsley CW (2009) Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nat Rev Drug Discov 8:41-54.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 63
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland RA, Pompliano DL, and Meek TD (2006) Drug-target residence time and its implications for lead optimization. Nat Rev Drug Discov 5:730-739.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 66
    • 0035188758 scopus 로고    scopus 로고
    • Enzymatic glycosylation of contulakin-G, a glycopeptide isolated from Conus venom, with a mammalian ppGalNAc-transferase
    • Craig AG, Park M, Fischer WH, Kang J, Compain P, and Piller F (2001) Enzymatic glycosylation of contulakin-G, a glycopeptide isolated from Conus venom, with a mammalian ppGalNAc-transferase. Toxicon 39:809-815.
    • (2001) Toxicon , vol.39 , pp. 809-815
    • Craig, A.G.1    Park, M.2    Fischer, W.H.3    Kang, J.4    Compain, P.5    Piller, F.6
  • 68
    • 0023665377 scopus 로고
    • Invertebrate vasopressin/oxytocin homologs. Characterization of peptides from Conus geographus and Conus straitus venoms
    • Cruz LJ, de Santos V, Zafaralla GC, Ramilo CA, Zeikus R, Gray WR, and Olivera BM (1987) Invertebrate vasopressin/oxytocin homologs. Characterization of peptides from Conus geographus and Conus straitus venoms. J Biol Chem 262:15821-15824.
    • (1987) J Biol Chem , vol.262 , pp. 15821-15824
    • Cruz, L.J.1    de Santos, V.2    Zafaralla, G.C.3    Ramilo, C.A.4    Zeikus, R.5    Gray, W.R.6    Olivera, B.M.7
  • 70
    • 0032400799 scopus 로고    scopus 로고
    • Slow closed-state inactivation: A novel mechanism underlying ramp currents in cells expressing the hNE/PN1 sodium channel
    • Cummins TR, Howe JR, and Waxman SG (1998) Slow closed-state inactivation: a novel mechanism underlying ramp currents in cells expressing the hNE/PN1 sodium channel. J Neurosci 18:9607-9619.
    • (1998) J Neurosci , vol.18 , pp. 9607-9619
    • Cummins, T.R.1    Howe, J.R.2    Waxman, S.G.3
  • 71
    • 36148978879 scopus 로고    scopus 로고
    • Voltage-gated sodium channel blockers for the treatment of neuropathic pain
    • Cummins TR and Rush AM (2007) Voltage-gated sodium channel blockers for the treatment of neuropathic pain. Expert Rev Neurother 7:1597-1612.
    • (2007) Expert Rev Neurother , vol.7 , pp. 1597-1612
    • Cummins, T.R.1    Rush, A.M.2
  • 72
    • 77958471998 scopus 로고    scopus 로고
    • v1.3 and affects fast inactivation via distinct intracellular regions
    • Cusdin FS, Nietlispach D, Maman J, Dale TJ, Powell AJ, Clare JJ, and Jackson AP (2010) The sodium channel {beta}3-subunit induces multiphasic gating in Nav1.3 and affects fast inactivation via distinct intracellular regions. J Biol Chem 285: 33404-33412.
    • (2010) J Biol Chem , vol.285 , pp. 33404-33412
    • Cusdin, F.S.1    Nietlispach, D.2    Maman, J.3    Dale, T.J.4    Powell, A.J.5    Clare, J.J.6    Jackson, A.P.7
  • 73
    • 2942554865 scopus 로고    scopus 로고
    • Structures of μO-conotoxins from Conus marmoreus. Inhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons
    • Daly NL, Ekberg JA, Thomas L, Adams DJ, Lewis RJ, and Craik DJ (2004) Structures of μO-conotoxins from Conus marmoreus. Inhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons. J Biol Chem 279:25774-25782.
    • (2004) J Biol Chem , vol.279 , pp. 25774-25782
    • Daly, N.L.1    Ekberg, J.A.2    Thomas, L.3    Adams, D.J.4    Lewis, R.J.5    Craik, D.J.6
  • 74
    • 67349175001 scopus 로고    scopus 로고
    • Remarkable inter- and intra-species complexity of conotoxins revealed by LC/MS
    • Davis J, Jones A, and Lewis RJ (2009) Remarkable inter- and intra-species complexity of conotoxins revealed by LC/MS. Peptides 30:1222-1227.
    • (2009) Peptides , vol.30 , pp. 1222-1227
    • Davis, J.1    Jones, A.2    Lewis, R.J.3
  • 76
    • 73949096000 scopus 로고    scopus 로고
    • Voltage-gated sodium channels: Therapeutic targets for pain
    • Dib-Hajj SD, Black JA, and Waxman SG (2009) Voltage-gated sodium channels: therapeutic targets for pain. Pain Med 10:1260-1269.
    • (2009) Pain Med , vol.10 , pp. 1260-1269
    • Dib-Hajj, S.D.1    Black, J.A.2    Waxman, S.G.3
  • 79
    • 0141850350 scopus 로고    scopus 로고
    • Reversal of experimental neuropathic pain by T-type calcium channel blockers
    • Dogrul A, Gardell LR, Ossipov MH, Tulunay FC, Lai J, and Porreca F (2003) Reversal of experimental neuropathic pain by T-type calcium channel blockers. Pain 105:159-168.
    • (2003) Pain , vol.105 , pp. 159-168
    • Dogrul, A.1    Gardell, L.R.2    Ossipov, M.H.3    Tulunay, F.C.4    Lai, J.5    Porreca, F.6
  • 82
    • 0028970541 scopus 로고
    • + channel mutant: Possible localization of a binding site at the outer vestibule
    • + channel mutant: possible localization of a binding site at the outer vestibule. Biophys J 69:1657-1665.
    • (1995) Biophys J , vol.69 , pp. 1657-1665
    • Dudley Jr., S.C.1    Todt, H.2    Lipkind, G.3    Fozzard, H.A.4
  • 84
    • 24044466131 scopus 로고    scopus 로고
    • 2 subunit contribution to 4/7 α-conotoxin binding to the nicotinic acetylcholine receptor
    • Dutertre S, Nicke A, and Lewis RJ (2005) 2 subunit contribution to 4/7 α-conotoxin binding to the nicotinic acetylcholine receptor. J Biol Chem 280:30460-30468.
    • (2005) J Biol Chem , vol.280 , pp. 30460-30468
    • Dutertre, S.1    Nicke, A.2    Lewis, R.J.3
  • 85
    • 3042572680 scopus 로고    scopus 로고
    • Determination of α-conotoxin binding modes on neuronal nicotinic acetylcholine receptors
    • Dutertre S, Nicke A, Tyndall JD, and Lewis RJ (2004) Determination of α-conotoxin binding modes on neuronal nicotinic acetylcholine receptors. J Mol Recognit 17: 339-347.
    • (2004) J Mol Recognit , vol.17 , pp. 339-347
    • Dutertre, S.1    Nicke, A.2    Tyndall, J.D.3    Lewis, R.J.4
  • 89
    • 0028096838 scopus 로고
    • Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin
    • Ellinor PT, Zhang JF, Horne WA, and Tsien RW (1994) Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin. Nature 372:272-275.
    • (1994) Nature , vol.372 , pp. 272-275
    • Ellinor, P.T.1    Zhang, J.F.2    Horne, W.A.3    Tsien, R.W.4
  • 90
    • 40849129937 scopus 로고    scopus 로고
    • α-RgIA, a novel conotoxin that blocks the α9α10 nAChR: Structure and identification of key receptor-binding residues
    • Ellison M, Feng ZP, Park AJ, Zhang X, Olivera BM, McIntosh JM, and Norton RS (2008) α-RgIA, a novel conotoxin that blocks the α9α10 nAChR: structure and identification of key receptor-binding residues. J Mol Biol 377:1216-1227.
    • (2008) J Mol Biol , vol.377 , pp. 1216-1227
    • Ellison, M.1    Feng, Z.P.2    Park, A.J.3    Zhang, X.4    Olivera, B.M.5    McIntosh, J.M.6    Norton, R.S.7
  • 91
    • 11144331404 scopus 로고    scopus 로고
    • α-Conotoxins ImI and ImII target distinct regions of the human α7 nicotinic acetylcholine receptor and distinguish human nicotinic receptor subtypes
    • Ellison M, Gao F, Wang HL, Sine SM, McIntosh JM, and Olivera BM (2004) α-Conotoxins ImI and ImII target distinct regions of the human α7 nicotinic acetylcholine receptor and distinguish human nicotinic receptor subtypes. Biochemistry 43:16019-16026.
    • (2004) Biochemistry , vol.43 , pp. 16019-16026
    • Ellison, M.1    Gao, F.2    Wang, H.L.3    Sine, S.M.4    McIntosh, J.M.5    Olivera, B.M.6
  • 94
    • 70350547576 scopus 로고    scopus 로고
    • Subtype-selective targeting of voltage-gated sodium channels
    • England S and de Groot MJ (2009) Subtype-selective targeting of voltage-gated sodium channels. Br J Pharmacol 158:1413-1425.
    • (2009) Br J Pharmacol , vol.158 , pp. 1413-1425
    • England, S.1    de Groot, M.J.2
  • 95
    • 0037622708 scopus 로고    scopus 로고
    • Identification of residues that confer α-conotoxin-PnIA sensitivity on the α3 subunit of neuronal nicotinic acetylcholine receptors
    • Everhart D, Reiller E, Mirzoian A, McIntosh JM, Malhotra A, and Luetje CW (2003) Identification of residues that confer α-conotoxin-PnIA sensitivity on the α3 subunit of neuronal nicotinic acetylcholine receptors. J Pharmacol Exp Ther 306:664-670.
    • (2003) J Pharmacol Exp Ther , vol.306 , pp. 664-670
    • Everhart, D.1    Reiller, E.2    Mirzoian, A.3    McIntosh, J.M.4    Malhotra, A.5    Luetje, C.W.6
  • 97
    • 0028049479 scopus 로고
    • A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in molluscs and acts as an antagonist in rat brain
    • Fainzilber M, Kofman O, Zlotkin E, and Gordon D (1994b) A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in molluscs and acts as an antagonist in rat brain. J Biol Chem 269:2574-2580.
    • (1994) J Biol Chem , vol.269 , pp. 2574-2580
    • Fainzilber, M.1    Kofman, O.2    Zlotkin, E.3    Gordon, D.4
  • 102
    • 0038645850 scopus 로고    scopus 로고
    • A novel conotoxin from Conus betulinus, κ-BtX, unique in cysteine pattern and in function as a specific BK channel modulator
    • Fan CX, Chen XK, Zhang C, Wang LX, Duan KL, He LL, Cao Y, Liu SY, Zhong MN, Ulens C, et al. (2003) A novel conotoxin from Conus betulinus, κ-BtX, unique in cysteine pattern and in function as a specific BK channel modulator. J Biol Chem 278:12624-12633.
    • (2003) J Biol Chem , vol.278 , pp. 12624-12633
    • Fan, C.X.1    Chen, X.K.2    Zhang, C.3    Wang, L.X.4    Duan, K.L.5    He, L.L.6    Cao, Y.7    Liu, S.Y.8    Zhong, M.N.9    Ulens, C.10
  • 103
  • 106
    • 0031127498 scopus 로고    scopus 로고
    • Sodium channel α-subunit mRNAs I, II, III, NaG, Na6 and hNE (PN1): Different expression patterns in developing rat nervous system
    • Felts PA, Yokoyama S, Dib-Hajj S, Black JA, and Waxman SG (1997) Sodium channel α-subunit mRNAs I, II, III, NaG, Na6 and hNE (PN1): different expression patterns in developing rat nervous system. Brain Res Mol Brain Res 45: 71-82.
    • (1997) Brain Res Mol Brain Res , vol.45 , pp. 71-82
    • Felts, P.A.1    Yokoyama, S.2    Dib-Hajj, S.3    Black, J.A.4    Waxman, S.G.5
  • 107
    • 0035844171 scopus 로고    scopus 로고
    • Residue Gly1326 of the N-type calcium channel α1B subunit controls reversibility of ω-conotoxin GVIA and MVIIA block
    • Feng ZP, Hamid J, Doering C, Bosey GM, Snutch TP, and Zamponi GW (2001) Residue Gly1326 of the N-type calcium channel α1B subunit controls reversibility of ω-conotoxin GVIA and MVIIA block. J Biol Chem 276:15728-15735.
    • (2001) J Biol Chem , vol.276 , pp. 15728-15735
    • Feng, Z.P.1    Hamid, J.2    Doering, C.3    Bosey, G.M.4    Snutch, T.P.5    Zamponi, G.W.6
  • 108
    • 2942687339 scopus 로고    scopus 로고
    • Identification of a mammalian target of κM-conotoxin RIIIK
    • Ferber M, Al-Sabi A, Stocker M, Olivera BM, and Terlau H (2004) Identification of a mammalian target of κM-conotoxin RIIIK. Toxicon 43:915-921.
    • (2004) Toxicon , vol.43 , pp. 915-921
    • Ferber, M.1    Al-Sabi, A.2    Stocker, M.3    Olivera, B.M.4    Terlau, H.5
  • 112
    • 0033152766 scopus 로고    scopus 로고
    • Roles of key functional groups in ω-conotoxin GVIA synthesis, structure and functional assay of selected peptide analogues
    • Flinn JP, Pallaghy PK, Lew MJ, Murphy R, Angus JA, and Norton RS (1999) Roles of key functional groups in ω-conotoxin GVIA synthesis, structure and functional assay of selected peptide analogues. Eur J Biochem 262:447-455.
    • (1999) Eur J Biochem , vol.262 , pp. 447-455
    • Flinn, J.P.1    Pallaghy, P.K.2    Lew, M.J.3    Murphy, R.4    Angus, J.A.5    Norton, R.S.6
  • 114
    • 77649213717 scopus 로고    scopus 로고
    • The tetrodotoxin binding site is within the outer vestibule of the sodium channel
    • Fozzard HA and Lipkind GM (2010) The tetrodotoxin binding site is within the outer vestibule of the sodium channel. Mar Drugs 8:219-234.
    • (2010) Mar Drugs , vol.8 , pp. 219-234
    • Fozzard, H.A.1    Lipkind, G.M.2
  • 117
    • 50249127742 scopus 로고    scopus 로고
    • Comparative study of the distribution of the α-subunits of voltage-gated sodium channels in normal and axotomized rat dorsal root ganglion neurons
    • Fukuoka T, Kobayashi K, Yamanaka H, Obata K, Dai Y, and Noguchi K (2008) Comparative study of the distribution of the α-subunits of voltage-gated sodium channels in normal and axotomized rat dorsal root ganglion neurons. J Comp Neurol 510:188-206.
    • (2008) J Comp Neurol , vol.510 , pp. 188-206
    • Fukuoka, T.1    Kobayashi, K.2    Yamanaka, H.3    Obata, K.4    Dai, Y.5    Noguchi, K.6
  • 118
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa H and Gouaux E (2003) Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J 22:2873-2885.
    • (2003) EMBO J , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 119
    • 27744500994 scopus 로고    scopus 로고
    • Subunit arrangement and function in NMDA receptors
    • Furukawa H, Singh SK, Mancusso R, and Gouaux E (2005) Subunit arrangement and function in NMDA receptors. Nature 438:185-192.
    • (2005) Nature , vol.438 , pp. 185-192
    • Furukawa, H.1    Singh, S.K.2    Mancusso, R.3    Gouaux, E.4
  • 122
    • 0033001555 scopus 로고    scopus 로고
    • A marine snail neurotoxin shares with scorpion toxins a convergent mechanism of blockade on the pore of voltage-gated K channels
    • García E, Scanlon M, and Naranjo D (1999) A marine snail neurotoxin shares with scorpion toxins a convergent mechanism of blockade on the pore of voltage-gated K channels. J Gen Physiol 114:141-157.
    • (1999) J Gen Physiol , vol.114 , pp. 141-157
    • García, E.1    Scanlon, M.2    Naranjo, D.3
  • 123
    • 75649108958 scopus 로고    scopus 로고
    • v2.2 identified in presynaptic membrane by mass spectrometric analysis
    • Gardezi SR, Taylor P, and Stanley EF (2010) Long C terminal splice variant Cav2.2 identified in presynaptic membrane by mass spectrometric analysis. Channels (Austin) 4:58-62.
    • (2010) Channels (Austin) , vol.4 , pp. 58-62
    • Gardezi, S.R.1    Taylor, P.2    Stanley, E.F.3
  • 124
    • 11844291367 scopus 로고    scopus 로고
    • Nicotinic modulation of GABAergic synaptic transmission in the spinal cord dorsal horn
    • Genzen JR and McGehee DS (2005) Nicotinic modulation of GABAergic synaptic transmission in the spinal cord dorsal horn. Brain Res 1031:229-237.
    • (2005) Brain Res , vol.1031 , pp. 229-237
    • Genzen, J.R.1    McGehee, D.S.2
  • 129
    • 0029874397 scopus 로고    scopus 로고
    • α1-Adrenergic receptor subtypes. Molecular structure, function, and signaling
    • Graham RM, Perez DM, Hwa J, and Piascik MT (1996) α1-Adrenergic receptor subtypes. Molecular structure, function, and signaling. Circ Res 78:737-749.
    • (1996) Circ Res , vol.78 , pp. 737-749
    • Graham, R.M.1    Perez, D.M.2    Hwa, J.3    Piascik, M.T.4
  • 131
    • 77954598197 scopus 로고    scopus 로고
    • Alpha-conotoxin AuIB isomers exhibit distinct inhibitory mechanisms and differential sensitivity to stoichiometry of alpha3beta4 nicotinic acetylcholine receptors
    • Grishin AA, Wang CI, Muttenthaler M, Alewood PF, Lewis RJ, and Adams DJ (2010) Alpha-conotoxin AuIB isomers exhibit distinct inhibitory mechanisms and differential sensitivity to stoichiometry of alpha3beta4 nicotinic acetylcholine receptors. J Biol Chem 285:22254-22263.
    • (2010) J Biol Chem , vol.285 , pp. 22254-22263
    • Grishin, A.A.1    Wang, C.I.2    Muttenthaler, M.3    Alewood, P.F.4    Lewis, R.J.5    Adams, D.J.6
  • 132
    • 0027426430 scopus 로고
    • Biotinylated derivatives of ω-conotoxins GVIA and MVIID: Probes for neuronal calcium channels
    • Haack JA, Kinser P, Yoshikami D, and Olivera BM (1993) Biotinylated derivatives of ω-conotoxins GVIA and MVIID: probes for neuronal calcium channels. Neuropharmacology 32:1151-1159.
    • (1993) Neuropharmacology , vol.32 , pp. 1151-1159
    • Haack, J.A.1    Kinser, P.2    Yoshikami, D.3    Olivera, B.M.4
  • 133
    • 0025241893 scopus 로고
    • Conantokin-T. A gamma-carboxyglutamate containing peptide with N-methyl-daspartate antagonist activity
    • Haack JA, Rivier J, Parks TN, Mena EE, Cruz LJ, and Olivera BM (1990) Conantokin-T. A gamma-carboxyglutamate containing peptide with N-methyl-daspartate antagonist activity. J Biol Chem 265:6025-6029.
    • (1990) J Biol Chem , vol.265 , pp. 6025-6029
    • Haack, J.A.1    Rivier, J.2    Parks, T.N.3    Mena, E.E.4    Cruz, L.J.5    Olivera, B.M.6
  • 134
    • 0141529982 scopus 로고    scopus 로고
    • v1.3 and functional involvement in neuronal hyperexcitability associated with central neuropathic pain after spinal cord injury
    • Hains BC, Klein JP, Saab CY, Craner MJ, Black JA, and Waxman SG (2003) Upregulation of sodium channel Nav1.3 and functional involvement in neuronal hyperexcitability associated with central neuropathic pain after spinal cord injury. J Neurosci 23:8881-8892.
    • (2003) J Neurosci , vol.23 , pp. 8881-8892
    • Hains, B.C.1    Klein, J.P.2    Saab, C.Y.3    Craner, M.J.4    Black, J.A.5    Waxman, S.G.6
  • 135
    • 67749118310 scopus 로고    scopus 로고
    • Scanning mutagenesis of α-conotoxin Vc1.1 reveals residues crucial for activity at the α9α10 nicotinic acetylcholine receptor
    • Halai R, Clark RJ, Nevin ST, Jensen JE, Adams DJ, and Craik DJ (2009) Scanning mutagenesis of α-conotoxin Vc1.1 reveals residues crucial for activity at the α9α10 nicotinic acetylcholine receptor. J Biol Chem 284:20275-20284.
    • (2009) J Biol Chem , vol.284 , pp. 20275-20284
    • Halai, R.1    Clark, R.J.2    Nevin, S.T.3    Jensen, J.E.4    Adams, D.J.5    Craik, D.J.6
  • 137
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, and Bourne Y (2005) Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J 24:3635-3646.
    • (2005) EMBO J , vol.24 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 138
    • 53249121457 scopus 로고    scopus 로고
    • Novel insights into GPCR-peptide interactions: Mutations in extracellular loop 1, ligand backbone methylations and molecular modeling of neurotensin receptor 1
    • Härterich S, Koschatzky S, Einsiedel J, and Gmeiner P (2008) Novel insights into GPCR-peptide interactions: mutations in extracellular loop 1, ligand backbone methylations and molecular modeling of neurotensin receptor 1. Bioorg Med Chem 16:9359-9368.
    • (2008) Bioorg Med Chem , vol.16 , pp. 9359-9368
    • Härterich, S.1    Koschatzky, S.2    Einsiedel, J.3    Gmeiner, P.4
  • 139
    • 0031026798 scopus 로고    scopus 로고
    • Determinants of specificity for α-conotoxin MII on α3β2 neuronal nicotinic receptors
    • Harvey SC, McIntosh JM, Cartier GE, Maddox FN, and Luetje CW (1997) Determinants of specificity for α-conotoxin MII on α3β2 neuronal nicotinic receptors. Mol Pharmacol 51:336-342.
    • (1997) Mol Pharmacol , vol.51 , pp. 336-342
    • Harvey, S.C.1    McIntosh, J.M.2    Cartier, G.E.3    Maddox, F.N.4    Luetje, C.W.5
  • 140
    • 0028922707 scopus 로고
    • Alterations of voltageactivated sodium current by a novel conotoxin from the venom of Conus gloriamaris
    • Hasson A, Shon KJ, Olivera BM, and Spira ME (1995) Alterations of voltageactivated sodium current by a novel conotoxin from the venom of Conus gloriamaris. J Neurophysiol 73:1295-1301.
    • (1995) J Neurophysiol , vol.73 , pp. 1295-1301
    • Hasson, A.1    Shon, K.J.2    Olivera, B.M.3    Spira, M.E.4
  • 141
    • 1642580583 scopus 로고    scopus 로고
    • + channels to nociceptive transmission in rat spinal lamina I neurons
    • + channels to nociceptive transmission in rat spinal lamina I neurons. Eur J Neurosci 19:103-111.
    • (2004) Eur J Neurosci , vol.19 , pp. 103-111
    • Heinke, B.1    Balzer, E.2    Sandkühler, J.3
  • 142
    • 79251565513 scopus 로고    scopus 로고
    • Multiple targets of μ-opioid receptormediated presynaptic inhibition at primary afferent Aδ- and C-fibers
    • Heinke B, Gingl E, and Sandkühler J (2011) Multiple targets of μ-opioid receptormediated presynaptic inhibition at primary afferent Aδ- and C-fibers. J Neurosci 31:1313-1322.
    • (2011) J Neurosci , vol.31 , pp. 1313-1322
    • Heinke, B.1    Gingl, E.2    Sandkühler, J.3
  • 143
    • 0028210965 scopus 로고
    • Nerve growth factor increases nicotinic ACh receptor gene expression and current density in wild-type and protein kinase A-deficient PC12 cells
    • Henderson LP, Gdovin MJ, Liu C, Gardner PD, and Maue RA (1994) Nerve growth factor increases nicotinic ACh receptor gene expression and current density in wild-type and protein kinase A-deficient PC12 cells. J Neurosci 14:1153-1163.
    • (1994) J Neurosci , vol.14 , pp. 1153-1163
    • Henderson, L.P.1    Gdovin, M.J.2    Liu, C.3    Gardner, P.D.4    Maue, R.A.5
  • 144
    • 73749087526 scopus 로고    scopus 로고
    • Cyclotides as templates in drug design
    • Henriques ST and Craik DJ (2010) Cyclotides as templates in drug design. Drug Discov Today 15:57-64.
    • (2010) Drug Discov Today , vol.15 , pp. 57-64
    • Henriques, S.T.1    Craik, D.J.2
  • 146
    • 0031826026 scopus 로고    scopus 로고
    • Mechanisms of regulation of neurotensin receptors
    • Hermans E and Maloteaux JM (1998) Mechanisms of regulation of neurotensin receptors. Pharmacol Ther 79:89-104.
    • (1998) Pharmacol Ther , vol.79 , pp. 89-104
    • Hermans, E.1    Maloteaux, J.M.2
  • 147
    • 0030109784 scopus 로고    scopus 로고
    • The use of α-adrenoceptor antagonists in the pharmacological management of benign prostatic hypertrophy: An overview
    • Hieble JP and Ruffolo RR, Jr. (1996) The use of α-adrenoceptor antagonists in the pharmacological management of benign prostatic hypertrophy: an overview. Pharmacol Res 33:145-160.
    • (1996) Pharmacol Res , vol.33 , pp. 145-160
    • Hieble, J.P.1    Ruffolo Jr., R.R.2
  • 149
    • 0031569801 scopus 로고    scopus 로고
    • Solution structure of the sodium channel antagonist conotoxin GS: A new molecular caliper for probing sodium channel geometry
    • Hill JM, Alewood PF, and Craik DJ (1997) Solution structure of the sodium channel antagonist conotoxin GS: a new molecular caliper for probing sodium channel geometry. Structure 5:571-583.
    • (1997) Structure , vol.5 , pp. 571-583
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 151
    • 0033579496 scopus 로고    scopus 로고
    • Single amino acid substitutions in α-conotoxin PnIA shift selectivity for subtypes of the mammalian neuronal nicotinic acetylcholine receptor
    • Hogg RC, Miranda LP, Craik DJ, Lewis RJ, Alewood PF, and Adams DJ (1999) Single amino acid substitutions in α-conotoxin PnIA shift selectivity for subtypes of the mammalian neuronal nicotinic acetylcholine receptor. J Biol Chem 274: 36559-36564.
    • (1999) J Biol Chem , vol.274 , pp. 36559-36564
    • Hogg, R.C.1    Miranda, L.P.2    Craik, D.J.3    Lewis, R.J.4    Alewood, P.F.5    Adams, D.J.6
  • 155
    • 18644376965 scopus 로고    scopus 로고
    • Electrostatic recognition and induced fit in the κ-PVIIA toxin binding to Shaker potassium channel
    • Huang X, Dong F, and Zhou HX (2005) Electrostatic recognition and induced fit in the κ-PVIIA toxin binding to Shaker potassium channel. J Am Chem Soc 127: 6836-6849.
    • (2005) J Am Chem Soc , vol.127 , pp. 6836-6849
    • Huang, X.1    Dong, F.2    Zhou, H.X.3
  • 156
    • 0036141825 scopus 로고    scopus 로고
    • Electrostatic and steric contributions to block of the skeletal muscle sodium channel by μ-conotoxin
    • Hui K, Lipkind G, Fozzard HA, and French RJ (2002) Electrostatic and steric contributions to block of the skeletal muscle sodium channel by μ-conotoxin. J Gen Physiol 119:45-54.
    • (2002) J Gen Physiol , vol.119 , pp. 45-54
    • Hui, K.1    Lipkind, G.2    Fozzard, H.A.3    French, R.J.4
  • 157
    • 0037488179 scopus 로고    scopus 로고
    • Conotoxins as sensors of local pH and electrostatic potential in the outer vestibule of the sodium channel
    • Hui K, McIntyre D, and French RJ (2003) Conotoxins as sensors of local pH and electrostatic potential in the outer vestibule of the sodium channel. J Gen Physiol 122:63-79.
    • (2003) J Gen Physiol , vol.122 , pp. 63-79
    • Hui, K.1    McIntyre, D.2    French, R.J.3
  • 158
    • 0037458899 scopus 로고    scopus 로고
    • Synaptic plasticity in spinal lamina I projection neurons that mediate hyperalgesia
    • Ikeda H, Heinke B, Ruscheweyh R, and Sandkühler J (2003) Synaptic plasticity in spinal lamina I projection neurons that mediate hyperalgesia. Science 299:1237-1240.
    • (2003) Science , vol.299 , pp. 1237-1240
    • Ikeda, H.1    Heinke, B.2    Ruscheweyh, R.3    Sandkühler, J.4
  • 160
    • 0029921401 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels by Gprotein βγ subunits
    • Ikeda SR (1996) Voltage-dependent modulation of N-type calcium channels by Gprotein βγ subunits. Nature 380:255-258.
    • (1996) Nature , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 167
    • 34547637063 scopus 로고    scopus 로고
    • αC-conotoxin PrXA: A new family of nicotinic acetylcholine receptor antagonists
    • Jimenez EC, Olivera BM, and Teichert RW (2007) αC-conotoxin PrXA: a new family of nicotinic acetylcholine receptor antagonists. Biochemistry 46:8717-8724.
    • (2007) Biochemistry , vol.46 , pp. 8717-8724
    • Jimenez, E.C.1    Olivera, B.M.2    Teichert, R.W.3
  • 170
    • 3242706871 scopus 로고    scopus 로고
    • Differential expression of calcium channels in sympathetic and parasympathetic preganglionic inputs to neurons in paracervical ganglia of guinea-pigs
    • Jobling P, Gibbins IL, Lewis RJ, and Morris JL (2004) Differential expression of calcium channels in sympathetic and parasympathetic preganglionic inputs to neurons in paracervical ganglia of guinea-pigs. Neuroscience 127:455-466.
    • (2004) Neuroscience , vol.127 , pp. 455-466
    • Jobling, P.1    Gibbins, I.L.2    Lewis, R.J.3    Morris, J.L.4
  • 176
    • 34249060579 scopus 로고    scopus 로고
    • The pharmacokinetics of the conopeptide contulakin-G (CGX-1160) after intrathecal administration: An analysis of data from studies in beagles
    • Kern SE, Allen J, Wagstaff J, Shafer SL, and Yaksh T (2007) The pharmacokinetics of the conopeptide contulakin-G (CGX-1160) after intrathecal administration: an analysis of data from studies in beagles. Anesth Analg 104:1514-1520.
    • (2007) Anesth Analg , vol.104 , pp. 1514-1520
    • Kern, S.E.1    Allen, J.2    Wagstaff, J.3    Shafer, S.L.4    Yaksh, T.5
  • 178
    • 0035976724 scopus 로고    scopus 로고
    • Changes in voltage-gated calcium channel α1 gene expression in rat dorsal root ganglia following peripheral nerve injury
    • Kim DS, Yoon CH, Lee SJ, Park SY, Yoo HJ, and Cho HJ (2001) Changes in voltage-gated calcium channel α1 gene expression in rat dorsal root ganglia following peripheral nerve injury. Brain Res Mol Brain Res 96:151-156.
    • (2001) Brain Res Mol Brain Res , vol.96 , pp. 151-156
    • Kim, D.S.1    Yoon, C.H.2    Lee, S.J.3    Park, S.Y.4    Yoo, H.J.5    Cho, H.J.6
  • 179
    • 0028782785 scopus 로고
    • Hydroxyl group of Tyr13 is essential for the activity of ω-conotoxin GVIA, a peptide toxin for N-type calcium channel
    • Kim JI, Takahashi M, Ogura A, Kohno T, Kudo Y, and Sato K (1994) Hydroxyl group of Tyr13 is essential for the activity of ω-conotoxin GVIA, a peptide toxin for N-type calcium channel. J Biol Chem 269:23876-23878.
    • (1994) J Biol Chem , vol.269 , pp. 23876-23878
    • Kim, J.I.1    Takahashi, M.2    Ogura, A.3    Kohno, T.4    Kudo, Y.5    Sato, K.6
  • 180
    • 0028985407 scopus 로고
    • Tyr13 is essential for the activity of ω-conotoxin MVIIA and GVIA, specific N-type calcium channel blockers
    • Kim JI, Takahashi M, Ohtake A, Wakamiya A, and Sato K (1995) Tyr13 is essential for the activity of ω-conotoxin MVIIA and GVIA, specific N-type calcium channel blockers. Biochem Biophys Res Commun 206:449-454.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 449-454
    • Kim, J.I.1    Takahashi, M.2    Ohtake, A.3    Wakamiya, A.4    Sato, K.5
  • 181
    • 80051621439 scopus 로고    scopus 로고
    • v1.7 maintains the membrane potential and regulates the activation and chemokine-induced migration of a monocyte-derived dendritic cell subset
    • Kis-Toth K, Hajdu P, Bacskai I, Szilagyi O, Papp F, Szanto A, Posta E, Gogolak P, Panyi G, and Rajnavolgyi E (2011) Voltage-gated sodium channel Nav1.7 maintains the membrane potential and regulates the activation and chemokine-induced migration of a monocyte-derived dendritic cell subset. J Immunol 187:1273-1280.
    • (2011) J Immunol , vol.187 , pp. 1273-1280
    • Kis-Toth, K.1    Hajdu, P.2    Bacskai, I.3    Szilagyi, O.4    Papp, F.5    Szanto, A.6    Posta, E.7    Gogolak, P.8    Panyi, G.9    Rajnavolgyi, E.10
  • 182
    • 0029848978 scopus 로고    scopus 로고
    • Novel ω-conotoxins block dihydropyridine-insensitive high voltageactivated calcium channels in molluscan neurons
    • Kits KS, Lodder JC, van der Schors RC, Li KW, Geraerts WP, and Fainzilber M (1996) Novel ω-conotoxins block dihydropyridine-insensitive high voltageactivated calcium channels in molluscan neurons. J Neurochem 67:2155-2163.
    • (1996) J Neurochem , vol.67 , pp. 2155-2163
    • Kits, K.S.1    Lodder, J.C.2    van der Schors, R.C.3    Li, K.W.4    Geraerts, W.P.5    Fainzilber, M.6
  • 183
    • 0035920125 scopus 로고    scopus 로고
    • The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-D-aspartate receptors
    • Klein RC, Prorok M, Galdzicki Z, and Castellino FJ (2001) The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-D-aspartate receptors. J Biol Chem 276: 26860-26867.
    • (2001) J Biol Chem , vol.276 , pp. 26860-26867
    • Klein, R.C.1    Prorok, M.2    Galdzicki, Z.3    Castellino, F.J.4
  • 184
    • 78651488405 scopus 로고    scopus 로고
    • A novel mechanism of inhibition of high-voltage activated calcium channels by α-conotoxins contributes to relief of nerve injury-induced neuropathic pain
    • Klimis H, Adams DJ, Callaghan B, Nevin S, Alewood PF, Vaughan CW, Mozar CA, and Christie MJ (2011) A novel mechanism of inhibition of high-voltage activated calcium channels by α-conotoxins contributes to relief of nerve injury-induced neuropathic pain. Pain 152:259-266.
    • (2011) Pain , vol.152 , pp. 259-266
    • Klimis, H.1    Adams, D.J.2    Callaghan, B.3    Nevin, S.4    Alewood, P.F.5    Vaughan, C.W.6    Mozar, C.A.7    Christie, M.J.8
  • 186
    • 79959244402 scopus 로고    scopus 로고
    • Intravenous injection of leconotide, an ω conotoxin: Synergistic antihyperalgesic effects with morphine in a rat model of bone cancer pain
    • Kolosov A, Aurini L, Williams ED, Cooke I, and Goodchild CS (2011) Intravenous injection of leconotide, an ω conotoxin: synergistic antihyperalgesic effects with morphine in a rat model of bone cancer pain. Pain Med 12:923-941.
    • (2011) Pain Med , vol.12 , pp. 923-941
    • Kolosov, A.1    Aurini, L.2    Williams, E.D.3    Cooke, I.4    Goodchild, C.S.5
  • 187
    • 75249106626 scopus 로고    scopus 로고
    • CNSB004 (Leconotide) causes antihyperalgesia without side effects when given intravenously: A comparison with ziconotide in a rat model of diabetic neuropathic pain
    • Kolosov A, Goodchild CS, and Cooke I (2010) CNSB004 (Leconotide) causes antihyperalgesia without side effects when given intravenously: a comparison with ziconotide in a rat model of diabetic neuropathic pain. Pain Med 11:262-273.
    • (2010) Pain Med , vol.11 , pp. 262-273
    • Kolosov, A.1    Goodchild, C.S.2    Cooke, I.3
  • 189
    • 16444381003 scopus 로고    scopus 로고
    • A Conus peptide blocks nicotinic receptors of unmyelinated axons in human nerves
    • Lang PM, Burgstahler R, Haberberger RV, Sippel W, and Grafe P (2005) A Conus peptide blocks nicotinic receptors of unmyelinated axons in human nerves. Neuroreport 16:479-483.
    • (2005) Neuroreport , vol.16 , pp. 479-483
    • Lang, P.M.1    Burgstahler, R.2    Haberberger, R.V.3    Sippel, W.4    Grafe, P.5
  • 190
    • 0242677114 scopus 로고    scopus 로고
    • Characterization of neuronal nicotinic acetylcholine receptors in the membrane of unmyelinated human C-fiber axons by in vitro studies
    • Lang PM, Burgstahler R, Sippel W, Irnich D, Schlotter-Weigel B, and Grafe P (2003) Characterization of neuronal nicotinic acetylcholine receptors in the membrane of unmyelinated human C-fiber axons by in vitro studies. J Neurophysiol 90:3295-3303.
    • (2003) J Neurophysiol , vol.90 , pp. 3295-3303
    • Lang, P.M.1    Burgstahler, R.2    Sippel, W.3    Irnich, D.4    Schlotter-Weigel, B.5    Grafe, P.6
  • 191
    • 0016258318 scopus 로고
    • Presynaptic regulation of catecholamine release
    • Langer SZ (1974) Presynaptic regulation of catecholamine release. Biochem Pharmacol 23:1793-1800.
    • (1974) Biochem Pharmacol , vol.23 , pp. 1793-1800
    • Langer, S.Z.1
  • 192
    • 9144236304 scopus 로고    scopus 로고
    • Conantokins: Peptide antagonists of NMDA receptors
    • Layer RT, Wagstaff JD, and White HS (2004) Conantokins: peptide antagonists of NMDA receptors. Curr Med Chem 11:3073-3084.
    • (2004) Curr Med Chem , vol.11 , pp. 3073-3084
    • Layer, R.T.1    Wagstaff, J.D.2    White, H.S.3
  • 195
    • 33745228127 scopus 로고    scopus 로고
    • Subtype specificity of scorpion beta-toxin Tz1 interaction with voltage-gated sodium channels is determined by the pore loop of domain 3
    • Leipold E, Hansel A, Borges A, and Heinemann SH (2006) Subtype specificity of scorpion beta-toxin Tz1 interaction with voltage-gated sodium channels is determined by the pore loop of domain 3. Mol Pharmacol 70:340-347.
    • (2006) Mol Pharmacol , vol.70 , pp. 340-347
    • Leipold, E.1    Hansel, A.2    Borges, A.3    Heinemann, S.H.4
  • 196
    • 21844466444 scopus 로고    scopus 로고
    • Molecular interaction of δ-conotoxins with voltage-gated sodium channels
    • Leipold E, Hansel A, Olivera BM, Terlau H, and Heinemann SH (2005) Molecular interaction of δ-conotoxins with voltage-gated sodium channels. FEBS Lett 579: 3881-3884.
    • (2005) FEBS Lett , vol.579 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 197
    • 79957868138 scopus 로고    scopus 로고
    • Molecular determinants for the subtype specificity of μ-conotoxin SIIIA targeting neuronal voltage-gated sodium channels
    • Leipold E, Markgraf R, Miloslavina A, Kijas M, Schirmeyer J, Imhof D, and Heinemann SH (2011) Molecular determinants for the subtype specificity of μ-conotoxin SIIIA targeting neuronal voltage-gated sodium channels. Neuropharmacology 61: 105-111.
    • (2011) Neuropharmacology , vol.61 , pp. 105-111
    • Leipold, E.1    Markgraf, R.2    Miloslavina, A.3    Kijas, M.4    Schirmeyer, J.5    Imhof, D.6    Heinemann, S.H.7
  • 198
    • 77951911566 scopus 로고    scopus 로고
    • v1.9 knockout mice
    • Leo S, D'Hooge R, and Meert T (2010) Exploring the role of nociceptor-specific sodium channels in pain transmission using Nav1.8 and Nav1.9 knockout mice. Behav Brain Res 208:149-157.
    • (2010) Behav Brain Res , vol.208 , pp. 149-157
    • Leo, S.1    D'hooge, R.2    Meert, T.3
  • 199
    • 0030973424 scopus 로고    scopus 로고
    • Structure-function relationships of ω-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues
    • Lew MJ, Flinn JP, Pallaghy PK, Murphy R, Whorlow SL, Wright CE, Norton RS, and Angus JA (1997) Structure-function relationships of ω-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues. J Biol Chem 272:12014-12023.
    • (1997) J Biol Chem , vol.272 , pp. 12014-12023
    • Lew, M.J.1    Flinn, J.P.2    Pallaghy, P.K.3    Murphy, R.4    Whorlow, S.L.5    Wright, C.E.6    Norton, R.S.7    Angus, J.A.8
  • 200
    • 84857049157 scopus 로고    scopus 로고
    • Discovery and development of the -conopeptide class of analgesic peptides
    • Lewis RJ (2011) Discovery and development of the -conopeptide class of analgesic peptides. Toxicon http://dx.doi.org/10.1016/j.toxicon.2011.07.012.
    • (2011) Toxicon
    • Lewis, R.J.1
  • 201
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis RJ and Garcia ML (2003) Therapeutic potential of venom peptides. Nat Rev Drug Discov 2:790-802.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 206
    • 0037424299 scopus 로고    scopus 로고
    • Effect of new O-superfamily conotoxin SO3 on sodium and potassium currents of cultured hippocampal neurons
    • Li Z, He XP, Xie ZP, Dai QY, and Huang PT (2003b) Effect of new O-superfamily conotoxin SO3 on sodium and potassium currents of cultured hippocampal neurons. Brain Res 965:155-158.
    • (2003) Brain Res , vol.965 , pp. 155-158
    • Li, Z.1    He, X.P.2    Xie, Z.P.3    Dai, Q.Y.4    Huang, P.T.5
  • 207
    • 0037449427 scopus 로고    scopus 로고
    • v1.3-like immunoreactivity in the adult rat central nervous system
    • Lindia JA and Abbadie C (2003) Distribution of the voltage gated sodium channel Nav1.3-like immunoreactivity in the adult rat central nervous system. Brain Res 960:132-141.
    • (2003) Brain Res , vol.960 , pp. 132-141
    • Lindia, J.A.1    Abbadie, C.2
  • 208
    • 28844448678 scopus 로고    scopus 로고
    • v1.3 expression and neuropathic pain behavior in rats
    • Lindia JA, Köhler MG, Martin WJ, and Abbadie C (2005) Relationship between sodium channel Nav1.3 expression and neuropathic pain behavior in rats. Pain 117:145-153.
    • (2005) Pain , vol.117 , pp. 145-153
    • Lindia, J.A.1    Köhler, M.G.2    Martin, W.J.3    Abbadie, C.4
  • 209
    • 0036700498 scopus 로고    scopus 로고
    • vα1
    • Lipscombe D, Pan JQ, and Gray AC (2002) Functional diversity in neuronal voltagegated calcium channels by alternative splicing of Cavα1. Mol Neurobiol 26:21-44.
    • (2002) Mol Neurobiol , vol.26 , pp. 21-44
    • Lipscombe, D.1    Pan, J.Q.2    Gray, A.C.3
  • 210
    • 36248939803 scopus 로고    scopus 로고
    • Isolation and characterization of a T-superfamily conotoxin from Conus litteratus with targeting tetrodotoxin-sensitive sodium channels
    • Liu J, Wu Q, Pi C, Zhao Y, Zhou M, Wang L, Chen S, and Xu A (2007a) Isolation and characterization of a T-superfamily conotoxin from Conus litteratus with targeting tetrodotoxin-sensitive sodium channels. Peptides 28:2313-2319.
    • (2007) Peptides , vol.28 , pp. 2313-2319
    • Liu, J.1    Wu, Q.2    Pi, C.3    Zhao, Y.4    Zhou, M.5    Wang, L.6    Chen, S.7    Xu, A.8
  • 213
    • 33750957742 scopus 로고    scopus 로고
    • Therapeutic applications of conotoxins that target the neuronal nicotinic acetylcholine receptor
    • Livett BG, Sandall DW, Keays D, Down J, Gayler KR, Satkunanathan N, and Khalil Z (2006) Therapeutic applications of conotoxins that target the neuronal nicotinic acetylcholine receptor. Toxicon 48:810-829.
    • (2006) Toxicon , vol.48 , pp. 810-829
    • Livett, B.G.1    Sandall, D.W.2    Keays, D.3    Down, J.4    Gayler, K.R.5    Satkunanathan, N.6    Khalil, Z.7
  • 215
    • 0037216407 scopus 로고    scopus 로고
    • The N-methyl-D-aspartate receptor subunit NR2B: Localization, functional properties, regulation, and clinical implications
    • Loftis JM and Janowsky A (2003) The N-methyl-D-aspartate receptor subunit NR2B: localization, functional properties, regulation, and clinical implications. Pharmacol Ther 97:55-85.
    • (2003) Pharmacol Ther , vol.97 , pp. 55-85
    • Loftis, J.M.1    Janowsky, A.2
  • 218
    • 34249072034 scopus 로고    scopus 로고
    • A novel α conotoxin (α-PIB) isolated from C. purpurascens is selective for skeletal muscle nicotinic acetylcholine receptors
    • López-Vera E, Jacobsen RB, Ellison M, Olivera BM, and Teichert RW (2007b) A novel α conotoxin (α-PIB) isolated from C. purpurascens is selective for skeletal muscle nicotinic acetylcholine receptors. Toxicon 49:1193-1199.
    • (2007) Toxicon , vol.49 , pp. 1193-1199
    • López-Vera, E.1    Jacobsen, R.B.2    Ellison, M.3    Olivera, B.M.4    Teichert, R.W.5
  • 220
    • 33747666931 scopus 로고    scopus 로고
    • Identification of a novel class of nicotinic receptor antagonists: Dimeric conotoxins VxXIIA, VxXIIB, and VxXIIC from Conus vexillum
    • Loughnan M, Nicke A, Jones A, Schroeder CI, Nevin ST, Adams DJ, Alewood PF, and Lewis RJ (2006) Identification of a novel class of nicotinic receptor antagonists: dimeric conotoxins VxXIIA, VxXIIB, and VxXIIC from Conus vexillum. J Biol Chem 281:24745-24755.
    • (2006) J Biol Chem , vol.281 , pp. 24745-24755
    • Loughnan, M.1    Nicke, A.2    Jones, A.3    Schroeder, C.I.4    Nevin, S.T.5    Adams, D.J.6    Alewood, P.F.7    Lewis, R.J.8
  • 221
    • 1242273820 scopus 로고    scopus 로고
    • Chemical and functional identification and characterization of novel sulfated α-conotoxins from the cone snail Conus anemone
    • Loughnan ML, Nicke A, Jones A, Adams DJ, Alewood PF, and Lewis RJ (2004) Chemical and functional identification and characterization of novel sulfated α-conotoxins from the cone snail Conus anemone. J Med Chem 47:1234-1241.
    • (2004) J Med Chem , vol.47 , pp. 1234-1241
    • Loughnan, M.L.1    Nicke, A.2    Jones, A.3    Adams, D.J.4    Alewood, P.F.5    Lewis, R.J.6
  • 222
    • 66049155827 scopus 로고    scopus 로고
    • Novel αD-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily
    • Loughnan ML, Nicke A, Lawrence N, and Lewis RJ (2009) Novel αD-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily. Biochemistry 48:3717-3729.
    • (2009) Biochemistry , vol.48 , pp. 3717-3729
    • Loughnan, M.L.1    Nicke, A.2    Lawrence, N.3    Lewis, R.J.4
  • 223
    • 0032714734 scopus 로고    scopus 로고
    • Conopeptides from Conus striatus and Conus textile by cDNA cloning
    • Lu BS, Yu F, Zhao D, Huang PT, and Huang CF (1999) Conopeptides from Conus striatus and Conus textile by cDNA cloning. Peptides 20:1139-1144.
    • (1999) Peptides , vol.20 , pp. 1139-1144
    • Lu, B.S.1    Yu, F.2    Zhao, D.3    Huang, P.T.4    Huang, C.F.5
  • 224
    • 23044503593 scopus 로고    scopus 로고
    • Postischemic administration of CGX-1051, a peptide from cone snail venom, reduces infarct size in both rat and dog models of myocardial ischemia and reperfusion
    • Lubbers NL, Campbell TJ, Polakowski JS, Bulaj G, Layer RT, Moore J, Gross GJ, and Cox BF (2005) Postischemic administration of CGX-1051, a peptide from cone snail venom, reduces infarct size in both rat and dog models of myocardial ischemia and reperfusion. J Cardiovasc Pharmacol 46:141-146.
    • (2005) J Cardiovasc Pharmacol , vol.46 , pp. 141-146
    • Lubbers, N.L.1    Campbell, T.J.2    Polakowski, J.S.3    Bulaj, G.4    Layer, R.T.5    Moore, J.6    Gross, G.J.7    Cox, B.F.8
  • 225
  • 226
    • 0032213318 scopus 로고    scopus 로고
    • α-Conotoxin AuIB selectively blocks α3β4 nicotinic acetylcholine receptors and nicotine-evoked norepinephrine release
    • Luo S, Kulak JM, Cartier GE, Jacobsen RB, Yoshikami D, Olivera BM, and McIntosh JM (1998) α-Conotoxin AuIB selectively blocks α3β4 nicotinic acetylcholine receptors and nicotine-evoked norepinephrine release. J Neurosci 18:8571-8579.
    • (1998) J Neurosci , vol.18 , pp. 8571-8579
    • Luo, S.1    Kulak, J.M.2    Cartier, G.E.3    Jacobsen, R.B.4    Yoshikami, D.5    Olivera, B.M.6    McIntosh, J.M.7
  • 228
    • 40849083674 scopus 로고    scopus 로고
    • v1.9 current and excitability in nociceptors through a coincident detection mechanism
    • Maingret F, Coste B, Padilla F, Clerc N, Crest M, Korogod SM, and Delmas P (2008) Inflammatory mediators increase Nav1.9 current and excitability in nociceptors through a coincident detection mechanism. J Gen Physiol 131:211-225.
    • (2008) J Gen Physiol , vol.131 , pp. 211-225
    • Maingret, F.1    Coste, B.2    Padilla, F.3    Clerc, N.4    Crest, M.5    Korogod, S.M.6    Delmas, P.7
  • 229
    • 34147126384 scopus 로고    scopus 로고
    • Recent advances in protein and peptide drug delivery systems
    • Malik DK, Baboota S, Ahuja A, Hasan S, and Ali J (2007) Recent advances in protein and peptide drug delivery systems. Curr Drug Deliv 4:141-151.
    • (2007) Curr Drug Deliv , vol.4 , pp. 141-151
    • Malik, D.K.1    Baboota, S.2    Ahuja, A.3    Hasan, S.4    Ali, J.5
  • 230
    • 0037219288 scopus 로고    scopus 로고
    • Powerful antinociceptive effects of the cone snail venom-derived subtype-selective NMDA receptor antagonists conantokins G and T
    • Malmberg AB, Gilbert H, McCabe RT, and Basbaum AI (2003) Powerful antinociceptive effects of the cone snail venom-derived subtype-selective NMDA receptor antagonists conantokins G and T. Pain 101:109-116.
    • (2003) Pain , vol.101 , pp. 109-116
    • Malmberg, A.B.1    Gilbert, H.2    McCabe, R.T.3    Basbaum, A.I.4
  • 231
    • 0027941058 scopus 로고
    • Voltage-sensitive calcium channels in spinal nociceptive processing: Blockade of N- and P-type channels inhibits formalininduced nociception
    • Malmberg AB and Yaksh TL (1994) Voltage-sensitive calcium channels in spinal nociceptive processing: blockade of N- and P-type channels inhibits formalininduced nociception. J Neurosci 14:4882-4890.
    • (1994) J Neurosci , vol.14 , pp. 4882-4890
    • Malmberg, A.B.1    Yaksh, T.L.2
  • 232
    • 0028836065 scopus 로고
    • Effect of continuous intrathecal infusion of ω-conopeptides, N-type calcium-channel blockers, on behavior and antinociception in the formalin and hot-plate tests in rats
    • Malmberg AB and Yaksh TL (1995) Effect of continuous intrathecal infusion of ω-conopeptides, N-type calcium-channel blockers, on behavior and antinociception in the formalin and hot-plate tests in rats. Pain 60:83-90.
    • (1995) Pain , vol.60 , pp. 83-90
    • Malmberg, A.B.1    Yaksh, T.L.2
  • 235
    • 34347389926 scopus 로고    scopus 로고
    • v2.3 calcium channel antagonist SNX-482 reduces dorsal horn neuronal responses in a rat model of chronic neuropathic pain
    • Matthews EA, Bee LA, Stephens GJ, and Dickenson AH (2007) The Cav2.3 calcium channel antagonist SNX-482 reduces dorsal horn neuronal responses in a rat model of chronic neuropathic pain. Eur J Neurosci 25:3561-3569.
    • (2007) Eur J Neurosci , vol.25 , pp. 3561-3569
    • Matthews, E.A.1    Bee, L.A.2    Stephens, G.J.3    Dickenson, A.H.4
  • 236
    • 2342462388 scopus 로고    scopus 로고
    • Structure and function of glutamate receptor ion channels
    • Mayer ML and Armstrong N (2004) Structure and function of glutamate receptor ion channels. Annu Rev Physiol 66:161-181.
    • (2004) Annu Rev Physiol , vol.66 , pp. 161-181
    • Mayer, M.L.1    Armstrong, N.2
  • 237
    • 80053200238 scopus 로고    scopus 로고
    • Interactions of key charged residues contributing to selective block of neuronal sodium channels by μ-conotoxin KIIIA
    • McArthur JR, Singh G, McMaster D, Winkfein R, Tieleman DP, and French RJ (2011) Interactions of key charged residues contributing to selective block of neuronal sodium channels by μ-conotoxin KIIIA. Mol Pharmacol 80:573-584.
    • (2011) Mol Pharmacol , vol.80 , pp. 573-584
    • McArthur, J.R.1    Singh, G.2    McMaster, D.3    Winkfein, R.4    Tieleman, D.P.5    French, R.J.6
  • 238
    • 23944483225 scopus 로고    scopus 로고
    • Decrease in α3*/α6* nicotinic receptors but not nicotine-evoked dopamine release in monkey brain after nigrostriatal damage
    • McCallum SE, Parameswaran N, Bordia T, McIntosh JM, Grady SR, and Quik M (2005) Decrease in α3*/α6* nicotinic receptors but not nicotine-evoked dopamine release in monkey brain after nigrostriatal damage. Mol Pharmacol 68:737-746.
    • (2005) Mol Pharmacol , vol.68 , pp. 737-746
    • McCallum, S.E.1    Parameswaran, N.2    Bordia, T.3    McIntosh, J.M.4    Grady, S.R.5    Quik, M.6
  • 239
    • 0036229869 scopus 로고    scopus 로고
    • Interactions among toxins that inhibit N-type and P-type calcium channels
    • McDonough SI, Boland LM, Mintz IM, and Bean BP (2002) Interactions among toxins that inhibit N-type and P-type calcium channels. J Gen Physiol 119:313-328.
    • (2002) J Gen Physiol , vol.119 , pp. 313-328
    • McDonough, S.I.1    Boland, L.M.2    Mintz, I.M.3    Bean, B.P.4
  • 240
    • 0031441105 scopus 로고    scopus 로고
    • Sympatholysis after neuron-specific, N-type, voltage-sensitive calcium channel blockade: First demonstration of N-channel function in humans
    • McGuire D, Bowersox S, Fellmann JD, and Luther RR (1997) Sympatholysis after neuron-specific, N-type, voltage-sensitive calcium channel blockade: first demonstration of N-channel function in humans. J Cardiovasc Pharmacol 30:400-403.
    • (1997) J Cardiovasc Pharmacol , vol.30 , pp. 400-403
    • McGuire, D.1    Bowersox, S.2    Fellmann, J.D.3    Luther, R.R.4
  • 244
    • 0037072765 scopus 로고    scopus 로고
    • α-Conotoxin GIC from Conus geographus, a novel peptide antagonist of nicotinic acetylcholine receptors
    • McIntosh JM, Dowell C, Watkins M, Garrett JE, Yoshikami D, and Olivera BM (2002) α-Conotoxin GIC from Conus geographus, a novel peptide antagonist of nicotinic acetylcholine receptors. J Biol Chem 277:33610-33615.
    • (2002) J Biol Chem , vol.277 , pp. 33610-33615
    • McIntosh, J.M.1    Dowell, C.2    Watkins, M.3    Garrett, J.E.4    Yoshikami, D.5    Olivera, B.M.6
  • 247
    • 24044496218 scopus 로고    scopus 로고
    • A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between rat α9α10 and α7 nicotinic cholinergic receptors
    • McIntosh JM, Plazas PV, Watkins M, Gomez-Casati ME, Olivera BM, and Elgoyhen AB (2005) A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between rat α9α10 and α7 nicotinic cholinergic receptors. J Biol Chem 280:30107-30112.
    • (2005) J Biol Chem , vol.280 , pp. 30107-30112
    • McIntosh, J.M.1    Plazas, P.V.2    Watkins, M.3    Gomez-Casati, M.E.4    Olivera, B.M.5    Elgoyhen, A.B.6
  • 248
    • 0032881372 scopus 로고    scopus 로고
    • Conus peptides targeted to specific nicotinic acetylcholine receptor subtypes
    • McIntosh JM, Santos AD, and Olivera BM (1999) Conus peptides targeted to specific nicotinic acetylcholine receptor subtypes. Annu Rev Biochem 68:59-88.
    • (1999) Annu Rev Biochem , vol.68 , pp. 59-88
    • McIntosh, J.M.1    Santos, A.D.2    Olivera, B.M.3
  • 251
    • 0026777101 scopus 로고
    • A vasotocin-like peptide in Aplysia kurodai ganglia: HPLC and RIA evidence for its identity with Lys-conopressin G
    • McMaster D, Kobayashi Y, and Lederis K (1992) A vasotocin-like peptide in Aplysia kurodai ganglia: HPLC and RIA evidence for its identity with Lys-conopressin G. Peptides 13:413-421.
    • (1992) Peptides , vol.13 , pp. 413-421
    • McMaster, D.1    Kobayashi, Y.2    Lederis, K.3
  • 253
    • 9144272640 scopus 로고    scopus 로고
    • Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain
    • Miljanich GP (2001) Ziconotide: neuronal calcium channel blocker for treating severe chronic pain. Curr Med Chem 11:3029-3040.
    • (2001) Curr Med Chem , vol.11 , pp. 3029-3040
    • Miljanich, G.P.1
  • 255
    • 0041731780 scopus 로고    scopus 로고
    • Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily
    • Milne TJ, Abbenante G, Tyndall JD, Halliday J, and Lewis RJ (2003) Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily. J Biol Chem 278:31105-31110.
    • (2003) J Biol Chem , vol.278 , pp. 31105-31110
    • Milne, T.J.1    Abbenante, G.2    Tyndall, J.D.3    Halliday, J.4    Lewis, R.J.5
  • 256
    • 34250767683 scopus 로고    scopus 로고
    • A vasopressin/oxytocin-related conopeptide with γ-carboxyglutamate at position 8
    • Möller C and Marí F (2007) A vasopressin/oxytocin-related conopeptide with γ-carboxyglutamate at position 8. Biochem J 404:413-419.
    • (2007) Biochem J , vol.404 , pp. 413-419
    • Möller, C.1    Marí, F.2
  • 257
    • 34548361322 scopus 로고    scopus 로고
    • In silico detection of binding mode of J-superfamily conotoxin pl14a with Kv1.6 channel
    • Mondal S, Babu RM, Bhavna R, and Ramakumar S (2007) In silico detection of binding mode of J-superfamily conotoxin pl14a with Kv1.6 channel. In Silico Biol 7:175-186.
    • (2007) In Silico Biol , vol.7 , pp. 175-186
    • Mondal, S.1    Babu, R.M.2    Bhavna, R.3    Ramakumar, S.4
  • 259
    • 1942536537 scopus 로고    scopus 로고
    • Differential involvement of N-type calcium channels in transmitter release from vasoconstrictor and vasodilator neurons
    • Morris JL, Ozols DI, Lewis RJ, Gibbins IL, and Jobling P (2004) Differential involvement of N-type calcium channels in transmitter release from vasoconstrictor and vasodilator neurons. Br J Pharmacol 141:961-970.
    • (2004) Br J Pharmacol , vol.141 , pp. 961-970
    • Morris, J.L.1    Ozols, D.I.2    Lewis, R.J.3    Gibbins, I.L.4    Jobling, P.5
  • 260
    • 50849107634 scopus 로고    scopus 로고
    • ω-Conotoxin inhibition of excitatory synaptic transmission evoked by dorsal root stimulation in rat superficial dorsal horn
    • Motin L and Adams DJ (2008) ω-Conotoxin inhibition of excitatory synaptic transmission evoked by dorsal root stimulation in rat superficial dorsal horn. Neuropharmacology 55:860-864.
    • (2008) Neuropharmacology , vol.55 , pp. 860-864
    • Motin, L.1    Adams, D.J.2
  • 261
    • 33847014577 scopus 로고    scopus 로고
    • ω-differentially inhibits native and recombinant N- and P/Q-type calcium channels
    • Motin L, Yasuda T, Schroeder CI, Lewis RJ, and Adams DJ (2007) ω-differentially inhibits native and recombinant N- and P/Q-type calcium channels. Eur J Neurosci 25:435-444.
    • (2007) Eur J Neurosci , vol.25 , pp. 435-444
    • Motin, L.1    Yasuda, T.2    Schroeder, C.I.3    Lewis, R.J.4    Adams, D.J.5
  • 264
    • 4644350854 scopus 로고    scopus 로고
    • Antinociceptive effect of different types of calcium channel inhibitors and the distribution of various calcium channel α1 subunits in the dorsal horn of spinal cord in mice
    • Murakami M, Nakagawasai O, Suzuki T, Mobarakeh II, Sakurada Y, Murata A, Yamadera F, Miyoshi I, Yanai K, Tan-No K, et al. (2004) Antinociceptive effect of different types of calcium channel inhibitors and the distribution of various calcium channel α1 subunits in the dorsal horn of spinal cord in mice. Brain Res 1024:122-129.
    • (2004) Brain Res , vol.1024 , pp. 122-129
    • Murakami, M.1    Nakagawasai, O.2    Suzuki, T.3    Mobarakeh, I.I.4    Sakurada, Y.5    Murata, A.6    Yamadera, F.7    Miyoshi, I.8    Yanai, K.9    Tan-No, K.10
  • 272
    • 0142153384 scopus 로고    scopus 로고
    • α-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors
    • Nicke A, Samochocki M, Loughnan ML, Bansal PS, Maelicke A, and Lewis RJ (2003b) α-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors. FEBS Lett 554:219-223.
    • (2003) FEBS Lett , vol.554 , pp. 219-223
    • Nicke, A.1    Samochocki, M.2    Loughnan, M.L.3    Bansal, P.S.4    Maelicke, A.5    Lewis, R.J.6
  • 274
    • 0028358717 scopus 로고
    • Isolation of Lysconopressin-G from the venom of the worm-hunting snail, Conus imperialis
    • Nielsen DB, Dykert J, Rivier JE, and McIntosh JM (1994) Isolation of Lysconopressin-G from the venom of the worm-hunting snail, Conus imperialis. Toxicon 32:845-848.
    • (1994) Toxicon , vol.32 , pp. 845-848
    • Nielsen, D.B.1    Dykert, J.2    Rivier, J.E.3    McIntosh, J.M.4
  • 275
    • 0033603390 scopus 로고    scopus 로고
    • Structure-activity relationships of ω-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels
    • Nielsen KJ, Adams D, Thomas L, Bond T, Alewood PF, Craik DJ, and Lewis RJ (1999a) Structure-activity relationships of ω-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels. J Mol Biol 289:1405-1421.
    • (1999) J Mol Biol , vol.289 , pp. 1405-1421
    • Nielsen, K.J.1    Adams, D.2    Thomas, L.3    Bond, T.4    Alewood, P.F.5    Craik, D.J.6    Lewis, R.J.7
  • 277
    • 0030601856 scopus 로고    scopus 로고
    • A consensus structure for ω-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: Comparison of MVIIA, SVIB and SNX-202
    • Nielsen KJ, Thomas L, Lewis RJ, Alewood PF, and Craik DJ (1996) A consensus structure for ω-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202. J Mol Biol 263:297-310.
    • (1996) J Mol Biol , vol.263 , pp. 297-310
    • Nielsen, K.J.1    Thomas, L.2    Lewis, R.J.3    Alewood, P.F.4    Craik, D.J.5
  • 278
    • 0037835606 scopus 로고    scopus 로고
    • Cloning, physical mapping and expression analysis of the human 5-HT3 serotonin receptor-like genes HTR3C, HTR3D and HTR3E
    • Niesler B, Frank B, Kapeller J, and Rappold GA (2003) Cloning, physical mapping and expression analysis of the human 5-HT3 serotonin receptor-like genes HTR3C, HTR3D and HTR3E. Gene 310:101-111.
    • (2003) Gene , vol.310 , pp. 101-111
    • Niesler, B.1    Frank, B.2    Kapeller, J.3    Rappold, G.A.4
  • 282
    • 12344302085 scopus 로고    scopus 로고
    • Spinal noradrenaline transporter inhibition by reboxetine and Xen2174 reduces tactile hypersensitivity after surgery in rats
    • Obata H, Conklin D, and Eisenach JC (2005) Spinal noradrenaline transporter inhibition by reboxetine and Xen2174 reduces tactile hypersensitivity after surgery in rats. Pain 113:271-276.
    • (2005) Pain , vol.113 , pp. 271-276
    • Obata, H.1    Conklin, D.2    Eisenach, J.C.3
  • 285
    • 0021749660 scopus 로고
    • Purification and sequence of a presynaptic peptide toxin from Conus geographus venom
    • Olivera BM, McIntosh JM, Cruz LJ, Luque FA, and Gray WR (1984) Purification and sequence of a presynaptic peptide toxin from Conus geographus venom. Biochemistry 23:5087-5090.
    • (1984) Biochemistry , vol.23 , pp. 5087-5090
    • Olivera, B.M.1    McIntosh, J.M.2    Cruz, L.J.3    Luque, F.A.4    Gray, W.R.5
  • 286
    • 0028292145 scopus 로고
    • Calcium channel diversity and neurotransmitter release: The ω-conotoxins and ω-agatoxins
    • Olivera BM, Miljanich GP, Ramachandran J, and Adams ME (1994) Calcium channel diversity and neurotransmitter release: the ω-conotoxins and ω-agatoxins. Annu Rev Biochem 63:823-867.
    • (1994) Annu Rev Biochem , vol.63 , pp. 823-867
    • Olivera, B.M.1    Miljanich, G.P.2    Ramachandran, J.3    Adams, M.E.4
  • 287
    • 66149088602 scopus 로고    scopus 로고
    • Subtype-selective conopeptides targeted to nicotinic receptors: Concerted discovery and biomedical applications
    • Olivera BM, Quik M, Vincler M, and McIntosh JM (2008) Subtype-selective conopeptides targeted to nicotinic receptors: Concerted discovery and biomedical applications. Channels (Austin) 2:143-152.
    • (2008) Channels (Austin) , vol.2 , pp. 143-152
    • Olivera, B.M.1    Quik, M.2    Vincler, M.3    McIntosh, J.M.4
  • 289
    • 77957017501 scopus 로고    scopus 로고
    • Phage display: Concept, innovations, applications and future
    • Pande J, Szewczyk MM, and Grover AK (2010) Phage display: concept, innovations, applications and future. Biotechnol Adv 28:849-858.
    • (2010) Biotechnol Adv , vol.28 , pp. 849-858
    • Pande, J.1    Szewczyk, M.M.2    Grover, A.K.3
  • 290
    • 0035840856 scopus 로고    scopus 로고
    • NMDA receptors as targets for drug action in neuropathic pain
    • Parsons CG (2001) NMDA receptors as targets for drug action in neuropathic pain. Eur J Pharmacol 429:71-78.
    • (2001) Eur J Pharmacol , vol.429 , pp. 71-78
    • Parsons, C.G.1
  • 291
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh J, Scheuer T, Zheng N, and Catterall WA (2011) The crystal structure of a voltage-gated sodium channel. Nature 475:353-358.
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 293
    • 43049092974 scopus 로고    scopus 로고
    • Identification of a novel class of conotoxins defined as V-conotoxins with a unique cysteine pattern and signal peptide sequence
    • Peng C, Liu L, Shao X, Chi C, and Wang C (2008) Identification of a novel class of conotoxins defined as V-conotoxins with a unique cysteine pattern and signal peptide sequence. Peptides 29:985-991.
    • (2008) Peptides , vol.29 , pp. 985-991
    • Peng, C.1    Liu, L.2    Shao, X.3    Chi, C.4    Wang, C.5
  • 294
    • 33747080261 scopus 로고    scopus 로고
    • Discovery of a novel class of conotoxin from Conus litteratus, lt14a, with a unique cysteine pattern
    • Peng C, Tang S, Pi C, Liu J, Wang F, Wang L, Zhou W, and Xu A (2006) Discovery of a novel class of conotoxin from Conus litteratus, lt14a, with a unique cysteine pattern. Peptides 27:2174-2181.
    • (2006) Peptides , vol.27 , pp. 2174-2181
    • Peng, C.1    Tang, S.2    Pi, C.3    Liu, J.4    Wang, F.5    Wang, L.6    Zhou, W.7    Xu, A.8
  • 295
    • 0033952153 scopus 로고    scopus 로고
    • Adverse effects associated with the intrathecal administration of ziconotide
    • Penn RD and Paice JA (2000) Adverse effects associated with the intrathecal administration of ziconotide. Pain 85:291-296.
    • (2000) Pain , vol.85 , pp. 291-296
    • Penn, R.D.1    Paice, J.A.2
  • 296
    • 34250771613 scopus 로고    scopus 로고
    • Chronic nicotine differentially regulates α6- and β3-containing nicotinic cholinergic receptors in rat brain
    • Perry DC, Mao D, Gold AB, McIntosh JM, Pezzullo JC, and Kellar KJ (2007) Chronic nicotine differentially regulates α6- and β3-containing nicotinic cholinergic receptors in rat brain. J Pharmacol Exp Ther 322:306-315.
    • (2007) J Pharmacol Exp Ther , vol.322 , pp. 306-315
    • Perry, D.C.1    Mao, D.2    Gold, A.B.3    McIntosh, J.M.4    Pezzullo, J.C.5    Kellar, K.J.6
  • 297
    • 28044432745 scopus 로고    scopus 로고
    • Upregulation of the voltage-gated sodium channel 2 subunit in neuropathic pain models: Characterization of expression in injured and non-injured primary sensory neurons
    • Pertin M, Ji RR, Berta T, Powell AJ, Karchewski L, Tate SN, Isom LL, Woolf CJ, Gilliard N, Spahn DR, et al. (2005) Upregulation of the voltage-gated sodium channel 2 subunit in neuropathic pain models: characterization of expression in injured and non-injured primary sensory neurons. J Neurosci 25:10970-10980.
    • (2005) J Neurosci , vol.25 , pp. 10970-10980
    • Pertin, M.1    Ji, R.R.2    Berta, T.3    Powell, A.J.4    Karchewski, L.5    Tate, S.N.6    Isom, L.L.7    Woolf, C.J.8    Gilliard, N.9    Spahn, D.R.10
  • 298
    • 0036456155 scopus 로고    scopus 로고
    • Cardiovascular effects of oxytocin
    • Petersson M (2002) Cardiovascular effects of oxytocin. Prog Brain Res 139:281-288.
    • (2002) Prog Brain Res , vol.139 , pp. 281-288
    • Petersson, M.1
  • 299
    • 33845761868 scopus 로고    scopus 로고
    • Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from Conus litteratus
    • Pi C, Liu J, Wang L, Jiang X, Liu Y, Peng C, Chen S, and Xu A (2007) Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from Conus litteratus. J Biotechnol 128:184-193.
    • (2007) J Biotechnol , vol.128 , pp. 184-193
    • Pi, C.1    Liu, J.2    Wang, L.3    Jiang, X.4    Liu, Y.5    Peng, C.6    Chen, S.7    Xu, A.8
  • 300
    • 0029905991 scopus 로고    scopus 로고
    • Separate agonist and peptide antagonist binding sites of the oxytocin receptor defined by their transfer into the V2 vasopressin receptor
    • Postina R, Kojro E, and Fahrenholz F (1996) Separate agonist and peptide antagonist binding sites of the oxytocin receptor defined by their transfer into the V2 vasopressin receptor. J Biol Chem 271:31593-31601.
    • (1996) J Biol Chem , vol.271 , pp. 31593-31601
    • Postina, R.1    Kojro, E.2    Fahrenholz, F.3
  • 302
    • 0942287662 scopus 로고    scopus 로고
    • Loss of α-conotoxinMII- and A85380-sensitive nicotinic receptors in Parkinson's disease striatum
    • Quik M, Bordia T, Forno L, and McIntosh JM (2004) Loss of α-conotoxinMII- and A85380-sensitive nicotinic receptors in Parkinson's disease striatum. J Neurochem 88:668-679.
    • (2004) J Neurochem , vol.88 , pp. 668-679
    • Quik, M.1    Bordia, T.2    Forno, L.3    McIntosh, J.M.4
  • 303
    • 0033538459 scopus 로고    scopus 로고
    • Pairwise interactions between neuronal α7 acetylcholine receptors and α-conotoxin ImI
    • Quiram PA, Jones JJ, and Sine SM (1999) Pairwise interactions between neuronal α7 acetylcholine receptors and α-conotoxin ImI. J Biol Chem 274:19517-19524.
    • (1999) J Biol Chem , vol.274 , pp. 19517-19524
    • Quiram, P.A.1    Jones, J.J.2    Sine, S.M.3
  • 304
    • 0032079457 scopus 로고    scopus 로고
    • Identification of residues in the neuronal α7 acetylcholine receptor that confer selectivity for conotoxin ImI
    • Quiram PA and Sine SM (1998a) Identification of residues in the neuronal α7 acetylcholine receptor that confer selectivity for conotoxin ImI. J Biol Chem 273:11001-11006.
    • (1998) J Biol Chem , vol.273 , pp. 11001-11006
    • Quiram, P.A.1    Sine, S.M.2
  • 305
    • 0032080235 scopus 로고    scopus 로고
    • Structural elements in α-conotoxin ImI essential for binding to neuronal α7 receptors
    • Quiram PA and Sine SM (1998b) Structural elements in α-conotoxin ImI essential for binding to neuronal α7 receptors. J Biol Chem 273:11007-11011.
    • (1998) J Biol Chem , vol.273 , pp. 11007-11011
    • Quiram, P.A.1    Sine, S.M.2
  • 306
    • 33847198227 scopus 로고    scopus 로고
    • Alternative splicing controls G protein-dependent inhibition of N-type calcium channels in nociceptors
    • Raingo J, Castiglioni AJ, and Lipscombe D (2007) Alternative splicing controls G protein-dependent inhibition of N-type calcium channels in nociceptors. Nat Neurosci 10:285-292.
    • (2007) Nat Neurosci , vol.10 , pp. 285-292
    • Raingo, J.1    Castiglioni, A.J.2    Lipscombe, D.3
  • 308
    • 0037145712 scopus 로고    scopus 로고
    • Neuropathy-specific analgesic action of intrathecal nicotinic agonists and its spinal GABA-mediated mechanism
    • Rashid MH and Ueda H (2002) Neuropathy-specific analgesic action of intrathecal nicotinic agonists and its spinal GABA-mediated mechanism. Brain Res 953: 53-62.
    • (2002) Brain Res , vol.953 , pp. 53-62
    • Rashid, M.H.1    Ueda, H.2
  • 312
    • 14144254799 scopus 로고    scopus 로고
    • Nicotinic AChR in subclassified capsaicin-sensitive and -insensitive nociceptors of the rat DRG
    • Rau KK, Johnson RD, and Cooper BY (2005) Nicotinic AChR in subclassified capsaicin-sensitive and -insensitive nociceptors of the rat DRG. J Neurophysiol 93: 1358-1371.
    • (2005) J Neurophysiol , vol.93 , pp. 1358-1371
    • Rau, K.K.1    Johnson, R.D.2    Cooper, B.Y.3
  • 313
    • 8544273283 scopus 로고    scopus 로고
    • Expression of alternatively spliced sodium channel α-subunit genes. Unique splicing patterns are observed in dorsal root ganglia
    • Raymond CK, Castle J, Garrett-Engele P, Armour CD, Kan Z, Tsinoremas N, and Johnson JM (2004) Expression of alternatively spliced sodium channel α-subunit genes. Unique splicing patterns are observed in dorsal root ganglia. J Biol Chem 279:46234-46241.
    • (2004) J Biol Chem , vol.279 , pp. 46234-46241
    • Raymond, C.K.1    Castle, J.2    Garrett-Engele, P.3    Armour, C.D.4    Kan, Z.5    Tsinoremas, N.6    Johnson, J.M.7
  • 317
    • 0041974814 scopus 로고    scopus 로고
    • v1.8 is essential for the expression of spontaneous activity in damaged sensory axons of mice
    • + channel Nav1.8 is essential for the expression of spontaneous activity in damaged sensory axons of mice. J Physiol 550:921-926.
    • (2003) J Physiol , vol.550 , pp. 921-926
    • Roza, C.1    Laird, J.M.2    Souslova, V.3    Wood, J.N.4    Cervero, F.5
  • 319
    • 34249862424 scopus 로고    scopus 로고
    • Inflammation reduces the contribution of N-type calcium channels to primary afferent synaptic transmission onto NK1 receptor-positive lamina I neurons in the rat dorsal horn
    • Rycroft BK, Vikman KS, and Christie MJ (2007) Inflammation reduces the contribution of N-type calcium channels to primary afferent synaptic transmission onto NK1 receptor-positive lamina I neurons in the rat dorsal horn. J Physiol 580:883-894.
    • (2007) J Physiol , vol.580 , pp. 883-894
    • Rycroft, B.K.1    Vikman, K.S.2    Christie, M.J.3
  • 321
    • 38549086800 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors of adrenal chromaffin cells
    • Sala F, Nistri A, and Criado M (2008) Nicotinic acetylcholine receptors of adrenal chromaffin cells. Acta Physiol (Oxf) 192:203-212.
    • (2008) Acta Physiol (Oxf) , vol.192 , pp. 203-212
    • Sala, F.1    Nistri, A.2    Criado, M.3
  • 322
    • 0027372947 scopus 로고
    • Isolation, structural characterization and biological function of a lysine-conopressin in the central nervous system of the pharyngobdellid leech Erpobdella octoculata
    • Salzet M, Bulet P, Van Dorsselaer A, and Malecha J (1993) Isolation, structural characterization and biological function of a lysine-conopressin in the central nervous system of the pharyngobdellid leech Erpobdella octoculata. Eur J Biochem 217:897-903.
    • (1993) Eur J Biochem , vol.217 , pp. 897-903
    • Salzet, M.1    Bulet, P.2    van Dorsselaer, A.3    Malecha, J.4
  • 325
    • 18844443166 scopus 로고    scopus 로고
    • Solution structure of δ-Am2766: A highly hydrophobic δ-conotoxin from Conus amadis that inhibits inactivation of neuronal voltagegated sodium channels
    • Sarma SP, Kumar GS, Sudarslal S, Iengar P, Ramasamy P, Sikdar SK, Krishnan KS, and Balaram P (2005) Solution structure of δ-Am2766: a highly hydrophobic δ-conotoxin from Conus amadis that inhibits inactivation of neuronal voltagegated sodium channels. Chem Biodivers 2:535-556.
    • (2005) Chem Biodivers , vol.2 , pp. 535-556
    • Sarma, S.P.1    Kumar, G.S.2    Sudarslal, S.3    Iengar, P.4    Ramasamy, P.5    Sikdar, S.K.6    Krishnan, K.S.7    Balaram, P.8
  • 326
    • 0033613178 scopus 로고    scopus 로고
    • Synthesis, bioactivity, and cloning of the L-type calcium channel blocker ω-conotoxin TxVII
    • Sasaki T, Feng ZP, Scott R, Grigoriev N, Syed NI, Fainzilber M, and Sato K (1999) Synthesis, bioactivity, and cloning of the L-type calcium channel blocker ω-conotoxin TxVII. Biochemistry 38:12876-12884.
    • (1999) Biochemistry , vol.38 , pp. 12876-12884
    • Sasaki, T.1    Feng, Z.P.2    Scott, R.3    Grigoriev, N.4    Syed, N.I.5    Fainzilber, M.6    Sato, K.7
  • 327
    • 26844476004 scopus 로고    scopus 로고
    • α-Conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones
    • Satkunanathan N, Livett B, Gayler K, Sandall D, Down J, and Khalil Z (2005) α-Conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones. Brain Res 1059:149-158.
    • (2005) Brain Res , pp. 149-158
    • Satkunanathan, N.1    Livett, B.2    Gayler, K.3    Sandall, D.4    Down, J.5    Khalil, Z.6
  • 330
  • 332
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA
    • Scanlon MJ, Naranjo D, Thomas L, Alewood PF, Lewis RJ, and Craik DJ (1997) Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA. Structure 5:1585-1597.
    • (1997) Structure , vol.5 , 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
  • 336
    • 3543031622 scopus 로고    scopus 로고
    • Development of small molecules that mimic the binding of ω-conotoxins at the N-type voltage-gated calcium channel
    • Schroeder CI, Smythe ML, and Lewis RJ (2004) Development of small molecules that mimic the binding of ω-conotoxins at the N-type voltage-gated calcium channel. Mol Divers 8:127-134.
    • (2004) Mol Divers , vol.8 , pp. 127-134
    • Schroeder, C.I.1    Smythe, M.L.2    Lewis, R.J.3
  • 337
    • 0037144134 scopus 로고    scopus 로고
    • Actions of intrathecal ω-conotoxins CVID, GVIA, MVIIA, and morphine in acute and neuropathic pain in the rat
    • Scott DA, Wright CE, and Angus JA (2002) Actions of intrathecal ω-conotoxins CVID, GVIA, MVIIA, and morphine in acute and neuropathic pain in the rat. Eur J Pharmacol 451:279-286.
    • (2002) Eur J Pharmacol , vol.451 , pp. 279-286
    • Scott, D.A.1    Wright, C.E.2    Angus, J.A.3
  • 338
    • 0033623464 scopus 로고    scopus 로고
    • 3, a novel auxiliary subunit for the voltage-gated sodium channel, is expressed preferentially in sensory neurons and is upregulated in the chronic constriction injury model of neuropathic pain
    • Shah BS, Stevens EB, Gonzalez MI, Bramwell S, Pinnock RD, Lee K, and Dixon AK (2000) 3, a novel auxiliary subunit for the voltage-gated sodium channel, is expressed preferentially in sensory neurons and is upregulated in the chronic constriction injury model of neuropathic pain. Eur J Neurosci 12:3985-3990.
    • (2000) Eur J Neurosci , vol.12 , pp. 3985-3990
    • Shah, B.S.1    Stevens, E.B.2    Gonzalez, M.I.3    Bramwell, S.4    Pinnock, R.D.5    Lee, K.6    Dixon, A.K.7
  • 342
    • 0029826273 scopus 로고    scopus 로고
    • Interactions of δ-conotoxins with alkaloid neurotoxins reveal differences between the silent and effective binding sites on voltage-sensitive sodium channels
    • Shichor I, Fainzilber M, Pelhate M, Malecot CO, Zlotkin E, and Gordon D (1996) Interactions of δ-conotoxins with alkaloid neurotoxins reveal differences between the silent and effective binding sites on voltage-sensitive sodium channels. J Neurochem 67:2451-2460.
    • (1996) J Neurochem , vol.67 , pp. 2451-2460
    • Shichor, I.1    Fainzilber, M.2    Pelhate, M.3    Malecot, C.O.4    Zlotkin, E.5    Gordon, D.6
  • 347
    • 0036217174 scopus 로고    scopus 로고
    • The novel N-type calcium channel blocker, AM336, produces potent dose-dependent antinociception after intrathecal dosing in rats and inhibits substance P release in rat spinal cord slices
    • Smith MT, Cabot PJ, Ross FB, Robertson AD, and Lewis RJ (2002) The novel N-type calcium channel blocker, AM336, produces potent dose-dependent antinociception after intrathecal dosing in rats and inhibits substance P release in rat spinal cord slices. Pain 96:119-127.
    • (2002) Pain , vol.96 , pp. 119-127
    • Smith, M.T.1    Cabot, P.J.2    Ross, F.B.3    Robertson, A.D.4    Lewis, R.J.5
  • 348
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky AI, Rosconi MP, and Gouaux E (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462:745-756.
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 351
    • 78751675268 scopus 로고    scopus 로고
    • Structurefunction relationship of conotoxin lt14a, a potential analgesic with low cytotoxicity
    • Sun D, Ren Z, Zeng X, You Y, Pan W, Zhou M, Wang L, and Xu A (2011) Structurefunction relationship of conotoxin lt14a, a potential analgesic with low cytotoxicity. Peptides 32:300-305.
    • (2011) Peptides , vol.32 , pp. 300-305
    • Sun, D.1    Ren, Z.2    Zeng, X.3    You, Y.4    Pan, W.5    Zhou, M.6    Wang, L.7    Xu, A.8
  • 352
    • 79953171481 scopus 로고    scopus 로고
    • The effects of intrathecal and systemic gabapentin on spinal substance P release
    • Takasusuki T and Yaksh TL (2011) The effects of intrathecal and systemic gabapentin on spinal substance P release. Anesth Analg 112:971-976.
    • (2011) Anesth Analg , vol.112 , pp. 971-976
    • Takasusuki, T.1    Yaksh, T.L.2
  • 353
    • 33747652956 scopus 로고    scopus 로고
    • α-Conotoxin OmIA is a potent ligand for the acetylcholine-binding protein as well as α3β2 and α7 nicotinic acetylcholine receptors
    • Talley TT, Olivera BM, Han KH, Christensen SB, Dowell C, Tsigelny I, Ho KY, Taylor P, and McIntosh JM (2006) α-Conotoxin OmIA is a potent ligand for the acetylcholine-binding protein as well as α3β2 and α7 nicotinic acetylcholine receptors. J Biol Chem 281:24678-24686.
    • (2006) J Biol Chem , vol.281 , pp. 24678-24686
    • Talley, T.T.1    Olivera, B.M.2    Han, K.H.3    Christensen, S.B.4    Dowell, C.5    Tsigelny, I.6    Ho, K.Y.7    Taylor, P.8    McIntosh, J.M.9
  • 354
    • 0025345759 scopus 로고
    • Structure and functional expression of the cloned rat neurotensin receptor
    • Tanaka K, Masu M, and Nakanishi S (1990) Structure and functional expression of the cloned rat neurotensin receptor. Neuron 4:847-854.
    • (1990) Neuron , vol.4 , pp. 847-854
    • Tanaka, K.1    Masu, M.2    Nakanishi, S.3
  • 355
    • 33846782930 scopus 로고    scopus 로고
    • Discovery and characterization of the short κA-conotoxins: A novel subfamily of excitatory conotoxins
    • Teichert RW, Jacobsen R, Terlau H, Yoshikami D, and Olivera BM (2007a) Discovery and characterization of the short κA-conotoxins: a novel subfamily of excitatory conotoxins. Toxicon 49:318-328.
    • (2007) Toxicon , vol.49 , pp. 318-328
    • Teichert, R.W.1    Jacobsen, R.2    Terlau, H.3    Yoshikami, D.4    Olivera, B.M.5
  • 356
    • 19644387101 scopus 로고    scopus 로고
    • αS-conotoxin RVIIIA: A structurally unique conotoxin that broadly targets nicotinic acetylcholine receptors
    • Teichert RW, Jimenez EC, and Olivera BM (2005a) αS-conotoxin RVIIIA: a structurally unique conotoxin that broadly targets nicotinic acetylcholine receptors. Biochemistry 44:7897-7902.
    • (2005) Biochemistry , vol.44 , pp. 7897-7902
    • Teichert, R.W.1    Jimenez, E.C.2    Olivera, B.M.3
  • 357
    • 37549069739 scopus 로고    scopus 로고
    • Novel conantokins from Conus parius venom are specific antagonists of N-methyl-D-aspartate receptors
    • Teichert RW, Jimenez EC, Twede V, Watkins M, Hollmann M, Bulaj G, and Olivera BM (2007b) Novel conantokins from Conus parius venom are specific antagonists of N-methyl-D-aspartate receptors. J Biol Chem 282:36905-36913.
    • (2007) J Biol Chem , vol.282 , pp. 36905-36913
    • Teichert, R.W.1    Jimenez, E.C.2    Twede, V.3    Watkins, M.4    Hollmann, M.5    Bulaj, G.6    Olivera, B.M.7
  • 358
    • 31544458674 scopus 로고    scopus 로고
    • Definition and characterization of the short αA-conotoxins: A single residue determines dissociation kinetics from the fetal muscle nicotinic acetylcholine receptor
    • Teichert RW, López-Vera E, Gulyas J, Watkins M, Rivier J, and Olivera BM (2006) Definition and characterization of the short αA-conotoxins: a single residue determines dissociation kinetics from the fetal muscle nicotinic acetylcholine receptor. Biochemistry 45:1304-1312.
    • (2006) Biochemistry , vol.45 , pp. 1304-1312
    • Teichert, R.W.1    López-Vera, E.2    Gulyas, J.3    Watkins, M.4    Rivier, J.5    Olivera, B.M.6
  • 360
    • 12744281120 scopus 로고    scopus 로고
    • A uniquely selective inhibitor of the mammalian fetal neuromuscular nicotinic acetylcholine receptor
    • Teichert RW, Rivier J, Torres J, Dykert J, Miller C, and Olivera BM (2005b) A uniquely selective inhibitor of the mammalian fetal neuromuscular nicotinic acetylcholine receptor. J Neurosci 25:732-736.
    • (2005) J Neurosci , vol.25 , pp. 732-736
    • Teichert, R.W.1    Rivier, J.2    Torres, J.3    Dykert, J.4    Miller, C.5    Olivera, B.M.6
  • 361
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channeltargeted peptides
    • Terlau H and Olivera BM (2004) Conus venoms: a rich source of novel ion channeltargeted peptides. Physiol Rev 84:41-68.
    • (2004) Physiol Rev , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 362
  • 364
    • 79955896976 scopus 로고    scopus 로고
    • T-type voltage-gated calcium channels as targets for the development of novel pain therapies
    • Todorovic SM and Jevtovic-Todorovic V (2011) T-type voltage-gated calcium channels as targets for the development of novel pain therapies. Br J Pharmacol 163:484-495.
    • (2011) Br J Pharmacol , vol.163 , pp. 484-495
    • Todorovic, S.M.1    Jevtovic-Todorovic, V.2
  • 365
    • 34249049430 scopus 로고    scopus 로고
    • Calcium channel antagonists: Clinical uses-past, present and future
    • Triggle DJ (2007) Calcium channel antagonists: clinical uses-past, present and future. Biochem Pharmacol 74:1-9.
    • (2007) Biochem Pharmacol , vol.74 , pp. 1-9
    • Triggle, D.J.1
  • 367
    • 0026607922 scopus 로고
    • P-type voltage-dependent calcium channel mediates presynaptic calcium influx and transmitter release in mammalian synapses
    • Uchitel OD, Protti DA, Sanchez V, Cherksey BD, Sugimori M, and Llinás R (1992) P-type voltage-dependent calcium channel mediates presynaptic calcium influx and transmitter release in mammalian synapses. Proc Natl Acad Sci USA 89: 3330-3333.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3330-3333
    • Uchitel, O.D.1    Protti, D.A.2    Sanchez, V.3    Cherksey, B.D.4    Sugimori, M.5    Llinás, R.6
  • 369
    • 33644870155 scopus 로고    scopus 로고
    • Structural determinants of selective α-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP
    • Ulens C, Hogg RC, Celie PH, Bertrand D, Tsetlin V, Smit AB, and Sixma TK (2006) Structural determinants of selective α-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP. Proc Natl Acad Sci USA 103:3615-3620.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3615-3620
    • Ulens, C.1    Hogg, R.C.2    Celie, P.H.3    Bertrand, D.4    Tsetlin, V.5    Smit, A.B.6    Sixma, T.K.7
  • 370
    • 80052503806 scopus 로고    scopus 로고
    • Importance of position 8 in μ-conotoxin KIIIA for voltage-gated sodium channel selectivity
    • Van Der Haegen A, Peigneur S, and Tytgat J (2011) Importance of position 8 in μ-conotoxin KIIIA for voltage-gated sodium channel selectivity. FEBS J 278: 3408-3418
    • (2011) FEBS J , vol.278 , pp. 3408-3418
    • van der Haegen, A.1    Peigneur, S.2    Tytgat, J.3
  • 371
    • 0029027071 scopus 로고
    • Structural and functional evolution of the vasopressin/oxytocin superfamily: Vasopressin-related conopressin is the only member present in Lymnaea, and is involved in the control of sexual behavior
    • Van Kesteren RE, Smit AB, De Lange RP, Kits KS, Van Golen FA, Van Der Schors RC, De With ND, Burke JF, and Geraerts WP (1995) Structural and functional evolution of the vasopressin/oxytocin superfamily: vasopressin-related conopressin is the only member present in Lymnaea, and is involved in the control of sexual behavior. J Neurosci 15:5989-5998.
    • (1995) J Neurosci , vol.15 , pp. 5989-5998
    • van Kesteren, R.E.1    Smit, A.B.2    de Lange, R.P.3    Kits, K.S.4    van Golen, F.A.5    van der Schors, R.C.6    de With, N.D.7    Burke, J.F.8    Geraerts, W.P.9
  • 372
    • 0038010721 scopus 로고    scopus 로고
    • Characterization and three-dimensional structure determination of ψ-conotoxin PIIIf, a novel noncompetitive antagonist of nicotinic acetylcholine receptors
    • Van Wagoner RM, Jacobsen RB, Olivera BM, and Ireland CM (2003) Characterization and three-dimensional structure determination of ψ-conotoxin PIIIf, a novel noncompetitive antagonist of nicotinic acetylcholine receptors. Biochemistry 42: 6353-6362.
    • (2003) Biochemistry , vol.42 , pp. 6353-6362
    • van Wagoner, R.M.1    Jacobsen, R.B.2    Olivera, B.M.3    Ireland, C.M.4
  • 373
    • 0033969834 scopus 로고    scopus 로고
    • Effects of antagonists to high-threshold calcium channels upon spinal mechanisms of pain, hyperalgesia and allodynia
    • Vanegas H and Schaible H (2000) Effects of antagonists to high-threshold calcium channels upon spinal mechanisms of pain, hyperalgesia and allodynia. Pain 85: 9-18.
    • (2000) Pain , vol.85 , pp. 9-18
    • Vanegas, H.1    Schaible, H.2
  • 376
    • 34447321825 scopus 로고    scopus 로고
    • Targeting the α9α10 nicotinic acetylcholine receptor to treat severe pain
    • Vincler M and McIntosh JM (2007) Targeting the α9α10 nicotinic acetylcholine receptor to treat severe pain. Expert Opin Ther Targets 11:891-897.
    • (2007) Expert Opin Ther Targets , vol.11 , pp. 891-897
    • Vincler, M.1    McIntosh, J.M.2
  • 377
    • 33845212316 scopus 로고    scopus 로고
    • Molecular mechanism for analgesia involving specific antagonism of α9α10 nicotinic acetylcholine receptors
    • Vincler M, Wittenauer S, Parker R, Ellison M, Olivera BM, and McIntosh JM (2006) Molecular mechanism for analgesia involving specific antagonism of α9α10 nicotinic acetylcholine receptors. Proc Natl Acad Sci USA 103:17880-17884.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17880-17884
    • Vincler, M.1    Wittenauer, S.2    Parker, R.3    Ellison, M.4    Olivera, B.M.5    McIntosh, J.M.6
  • 382
    • 70349623944 scopus 로고    scopus 로고
    • Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents
    • Wang L, Liu J, Pi C, Zeng X, Zhou M, Jiang X, Chen S, Ren Z, and Xu A (2009) Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents. Arch Toxicol 83:925-932.
    • (2009) Arch Toxicol , vol.83 , pp. 925-932
    • Wang, L.1    Liu, J.2    Pi, C.3    Zeng, X.4    Zhou, M.5    Jiang, X.6    Chen, S.7    Ren, Z.8    Xu, A.9
  • 383
    • 57849140606 scopus 로고    scopus 로고
    • Identification and characterization of a novel O-superfamily conotoxin from Conus litteratus
    • Wang L, Pi C, Liu J, Chen S, Peng C, Sun D, Zhou M, Xiang H, Ren Z, and Xu A (2008) Identification and characterization of a novel O-superfamily conotoxin from Conus litteratus. J Pept Sci 14:1077-1083.
    • (2008) J Pept Sci , vol.14 , pp. 1077-1083
    • Wang, L.1    Pi, C.2    Liu, J.3    Chen, S.4    Peng, C.5    Sun, D.6    Zhou, M.7    Xiang, H.8    Ren, Z.9    Xu, A.10
  • 388
    • 23044455421 scopus 로고    scopus 로고
    • SO-3, a new O-superfamily conopeptide derived from Conus striatus, selectively inhibits N-type calcium currents in cultured hippocampal neurons
    • Wen L, Yang S, Qiao H, Liu Z, Zhou W, Zhang Y, and Huang P (2005) SO-3, a new O-superfamily conopeptide derived from Conus striatus, selectively inhibits N-type calcium currents in cultured hippocampal neurons. Br J Pharmacol 145:728-739.
    • (2005) Br J Pharmacol , vol.145 , pp. 728-739
    • Wen, L.1    Yang, S.2    Qiao, H.3    Liu, Z.4    Zhou, W.5    Zhang, Y.6    Huang, P.7
  • 390
    • 0037168454 scopus 로고    scopus 로고
    • μ-Conotoxin SmIIIA, a potent inhibitor of tetrodotoxin-resistant sodium channels in amphibian sympathetic and sensory neurons
    • West PJ, Bulaj G, Garrett JE, Olivera BM, and Yoshikami D (2002) μ-Conotoxin SmIIIA, a potent inhibitor of tetrodotoxin-resistant sodium channels in amphibian sympathetic and sensory neurons. Biochemistry 41:15388-15393.
    • (2002) Biochemistry , vol.41 , pp. 15388-15393
    • West, P.J.1    Bulaj, G.2    Garrett, J.E.3    Olivera, B.M.4    Yoshikami, D.5
  • 391
    • 0032528631 scopus 로고    scopus 로고
    • + channel subtypes on rat spinal motor neurons, interneurons, and nerve terminals
    • + channel subtypes on rat spinal motor neurons, interneurons, and nerve terminals. J Neurosci 18:6319-6330.
    • (1998) J Neurosci , vol.18 , pp. 6319-6330
    • Westenbroek, R.E.1    Hoskins, L.2    Catterall, W.A.3
  • 394
    • 44249110008 scopus 로고    scopus 로고
    • Synthesis and characterization of 125I-α-conotoxin ArIB[V11L;V16A], a selective α7 nicotinic acetylcholine receptor antagonist
    • Whiteaker P, Marks MJ, Christensen S, Dowell C, Collins AC, and McIntosh JM (2008) Synthesis and characterization of 125I-α-conotoxin ArIB[V11L;V16A], a selective α7 nicotinic acetylcholine receptor antagonist. J Pharmacol Exp Ther 325:910-919.
    • (2008) J Pharmacol Exp Ther , vol.325 , pp. 910-919
    • Whiteaker, P.1    Marks, M.J.2    Christensen, S.3    Dowell, C.4    Collins, A.C.5    McIntosh, J.M.6
  • 396
    • 79960025671 scopus 로고    scopus 로고
    • v1.1 through 1.8 identify those responsible for action potentials in sciatic nerve
    • Wilson MJ, Yoshikami D, Azam L, Gajewiak J, Olivera BM, Bulaj G, and Zhang MM (2011a) μ-Conotoxins that differentially block sodium channels Nav1.1 through 1.8 identify those responsible for action potentials in sciatic nerve. Proc Natl Acad Sci USA 108:10302-10307.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10302-10307
    • Wilson, M.J.1    Yoshikami, D.2    Azam, L.3    Gajewiak, J.4    Olivera, B.M.5    Bulaj, G.6    Zhang, M.M.7
  • 398
    • 22144442830 scopus 로고    scopus 로고
    • v2.2 voltage-gated calcium channels for neuropathic pain
    • Winquist RJ, Pan JQ, and Gribkoff VK (2005) Use-dependent blockade of Cav2.2 voltage-gated calcium channels for neuropathic pain. Biochem Pharmacol 70:489-499.
    • (2005) Biochem Pharmacol , vol.70 , pp. 489-499
    • Winquist, R.J.1    Pan, J.Q.2    Gribkoff, V.K.3
  • 399
    • 0034798601 scopus 로고    scopus 로고
    • Point mutations identify the glutamate binding pocket of the N-methyl-daspartate receptor as major site of conantokin-G inhibition
    • Wittekindt B, Malany S, Schemm R, Otvos L, Maccecchini ML, Laube B, and Betz H (2001) Point mutations identify the glutamate binding pocket of the N-methyl-daspartate receptor as major site of conantokin-G inhibition. Neuropharmacology 41:753-761.
    • (2001) Neuropharmacology , vol.41 , pp. 753-761
    • Wittekindt, B.1    Malany, S.2    Schemm, R.3    Otvos, L.4    Maccecchini, M.L.5    Laube, B.6    Betz, H.7
  • 400
    • 0028059514 scopus 로고
    • Calcium channel subtypes in rat brain: Biochemical characterization of the high-affinity receptors for ω-conopeptides SNX-230 (synthetic MVIIC), SNX-183 (SVIB), and SNX-111 (MVIIA)
    • Woppmann A, Ramachandran J, and Miljanich GP (1994) Calcium channel subtypes in rat brain: biochemical characterization of the high-affinity receptors for ω-conopeptides SNX-230 (synthetic MVIIC), SNX-183 (SVIB), and SNX-111 (MVIIA). Mol Cell Neurosci 5:350-357.
    • (1994) Mol Cell Neurosci , vol.5 , pp. 350-357
    • Woppmann, A.1    Ramachandran, J.2    Miljanich, G.P.3
  • 401
  • 402
    • 55249117019 scopus 로고    scopus 로고
    • Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain ii voltage sensor in the closed configuration
    • Xiao Y, Bingham JP, Zhu W, Moczydlowski E, Liang S, and Cummins TR (2008a) Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain ii voltage sensor in the closed configuration. J Biol Chem 283:27300-27313.
    • (2008) J Biol Chem , vol.283 , pp. 27300-27313
    • Xiao, Y.1    Bingham, J.P.2    Zhu, W.3    Moczydlowski, E.4    Liang, S.5    Cummins, T.R.6
  • 403
    • 38149035935 scopus 로고    scopus 로고
    • Synthesis and characterization of huwentoxin-IV, a neurotoxin inhibiting central neuronal sodium channels
    • Xiao Y, Luo X, Kuang F, Deng M, Wang M, Zeng X, and Liang S (2008b) Synthesis and characterization of huwentoxin-IV, a neurotoxin inhibiting central neuronal sodium channels. Toxicon 51:230-239.
    • (2008) Toxicon , vol.51 , pp. 230-239
    • Xiao, Y.1    Luo, X.2    Kuang, F.3    Deng, M.4    Wang, M.5    Zeng, X.6    Liang, S.7
  • 404
    • 30844473761 scopus 로고    scopus 로고
    • Calcium channels as therapeutic targets in neuropathic pain
    • Yaksh TL (2006) Calcium channels as therapeutic targets in neuropathic pain. J Pain 7:S13-30.
    • (2006) J Pain , vol.7
    • Yaksh, T.L.1
  • 405
    • 0023711980 scopus 로고
    • A novel sodium channel inhibitor from Conus geographus: Purification, structure, and pharmacological properties
    • Yanagawa Y, Abe T, Satake M, Odani S, Suzuki J, and Ishikawa K (1988) A novel sodium channel inhibitor from Conus geographus: purification, structure, and pharmacological properties. Biochemistry 27:6256-6262.
    • (1988) Biochemistry , vol.27 , pp. 6256-6262
    • Yanagawa, Y.1    Abe, T.2    Satake, M.3    Odani, S.4    Suzuki, J.5    Ishikawa, K.6
  • 409
    • 33646698386 scopus 로고    scopus 로고
    • v1.3 neuronal L-type calcium channels: Differential targeting and signaling to pCREB
    • Zhang H, Fu Y, Altier C, Platzer J, Surmeier DJ, and Bezprozvanny I (2006a) Cav1.2 and Cav1.3 neuronal L-type calcium channels: differential targeting and signaling to pCREB. Eur J Neurosci 23:2297-2310.
    • (2006) Eur J Neurosci , vol.23 , pp. 2297-2310
    • Zhang, H.1    Fu, Y.2    Altier, C.3    Platzer, J.4    Surmeier, D.J.5    Bezprozvanny, I.6
  • 411
    • 35349024767 scopus 로고    scopus 로고
    • Structure/function characterization of μ-conotoxin KIIIA, an analgesic, nearly irreversible blocker of mammalian neuronal sodium channels
    • Zhang MM, Green BR, Catlin P, Fiedler B, Azam L, Chadwick A, Terlau H, McArthur JR, French RJ, Gulyas J, et al. (2007) Structure/function characterization of μ-conotoxin KIIIA, an analgesic, nearly irreversible blocker of mammalian neuronal sodium channels. J Biol Chem 282:30699-30706.
    • (2007) J Biol Chem , vol.282 , pp. 30699-30706
    • Zhang, M.M.1    Green, B.R.2    Catlin, P.3    Fiedler, B.4    Azam, L.5    Chadwick, A.6    Terlau, H.7    McArthur, J.R.8    French, R.J.9    Gulyas, J.10
  • 412
    • 77953262644 scopus 로고    scopus 로고
    • μ-Conotoxin KIIIA derivatives with divergent affinities versus efficacies in blocking voltagegated sodium channels
    • Zhang MM, Han TS, Olivera BM, Bulaj G, and Yoshikami D (2010) μ-Conotoxin KIIIA derivatives with divergent affinities versus efficacies in blocking voltagegated sodium channels. Biochemistry 49:4804-4812.
    • (2010) Biochemistry , vol.49 , pp. 4804-4812
    • Zhang, M.M.1    Han, T.S.2    Olivera, B.M.3    Bulaj, G.4    Yoshikami, D.5
  • 413
    • 21244490871 scopus 로고    scopus 로고
    • Cloning of novel conotoxin precursor sequences from Conus litteratus
    • Zhao D and Huang P (2000) Cloning of novel conotoxin precursor sequences from Conus pulicarius. Prog Nat Sci 10:33-36.
    • (2000) Prog Nat Sci , vol.10 , pp. 33-36
    • Zhao, D.1    Huang, P.2
  • 414
    • 79953288241 scopus 로고    scopus 로고
    • Discovery of non-peptide, small molecule antagonists of α9α10 nicotinic acetylcholine receptors as novel analgesics for the treatment of neuropathic and tonic inflammatory pain
    • Zheng G, Zhang Z, Dowell C, Wala E, Dwoskin LP, Holtman JR, McIntosh JM, and Crooks PA (2011) Discovery of non-peptide, small molecule antagonists of α9α10 nicotinic acetylcholine receptors as novel analgesics for the treatment of neuropathic and tonic inflammatory pain. Bioorg Med Chem Lett 21:2476-2479.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 2476-2479
    • Zheng, G.1    Zhang, Z.2    Dowell, C.3    Wala, E.4    Dwoskin, L.P.5    Holtman, J.R.6    McIntosh, J.M.7    Crooks, P.A.8
  • 416
    • 32344433189 scopus 로고    scopus 로고
    • The μO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3
    • Zorn S, Leipold E, Hansel A, Bulaj G, Olivera BM, Terlau H, and Heinemann SH (2006) The μO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3. FEBS Lett 580:1360-1364.
    • (2006) FEBS Lett , vol.580 , pp. 1360-1364
    • Zorn, S.1    Leipold, E.2    Hansel, A.3    Bulaj, G.4    Olivera, B.M.5    Terlau, H.6    Heinemann, S.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.