메뉴 건너뛰기




Volumn 70, Issue 19, 2013, Pages 3665-3693

The insecticidal potential of venom peptides

Author keywords

Cone snail; Insecticidal toxins; Scorpion; Sea anemone; Snake; Spider; Toxin structural folds; Venom peptides; Voltage gated ion channels

Indexed keywords

CONTRYPHAN; CYSTINE STABILIZED ALPHABETA; DEFENSIN LIKE; DISULFIDE DIRECTED BETA HAIRPIN; GLUTAMIC ACID; INHIBITOR CYSTINE KNOT; INSECTICIDAL VENOM PEPTIDE DERIVATIVE; INSECTICIDE; NEUROTOXIN III; THREE FINGER TOXIN; UNCLASSIFIED DRUG; VOLTAGE GATED SODIUM CHANNEL;

EID: 84884356570     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1315-3     Document Type: Review
Times cited : (86)

References (213)
  • 1
    • 33646235855 scopus 로고    scopus 로고
    • Crop losses to pests
    • 10.1017/S0021859605005708
    • Oerke EC (2006) Crop losses to pests. J Agric Sci 144(1):31-43
    • (2006) J Agric Sci , vol.144 , Issue.1 , pp. 31-43
    • Oerke, E.C.1
  • 2
    • 84920115413 scopus 로고    scopus 로고
    • Pesticides and pest control
    • R. Peshin A.K. Dhawan (eds) Springer Dordrecht 10.1007/978-1-4020-8992-3- 3
    • Pimental D (2009) Pesticides and pest control. In: Peshin R, Dhawan AK (eds) Integrated pest management: innovation-development process. Springer, Dordrecht, pp 83-87
    • (2009) Integrated Pest Management: Innovation-development Process , pp. 83-87
    • Pimental, D.1
  • 3
    • 1942534974 scopus 로고    scopus 로고
    • Australian funnel-web spiders: Master insecticide chemists
    • 15066416 1:CAS:528:DC%2BD2cXislGjtro%3D 10.1016/j.toxicon.2004.02.010
    • Tedford HW, Sollod BL, Maggio F, King GF (2004) Australian funnel-web spiders: master insecticide chemists. Toxicon 43(5):601-618
    • (2004) Toxicon , vol.43 , Issue.5 , pp. 601-618
    • Tedford, H.W.1    Sollod, B.L.2    Maggio, F.3    King, G.F.4
  • 5
    • 80054039857 scopus 로고    scopus 로고
    • Assessment of resistance risk in Spodoptera exigua (Hubner) (Lepidoptera: Noctuidae) to chlorantraniliprole
    • 21594963 1:CAS:528:DC%2BC3MXht12rs7vF 10.1002/ps.2201
    • Lai TC, Su JY (2011) Assessment of resistance risk in Spodoptera exigua (Hubner) (Lepidoptera: Noctuidae) to chlorantraniliprole. Pest Manag Sci 67(11):1468-1472
    • (2011) Pest Manag Sci , vol.67 , Issue.11 , pp. 1468-1472
    • Lai, T.C.1    Su, J.Y.2
  • 6
    • 79960171704 scopus 로고    scopus 로고
    • Gene amplification and insecticide resistance
    • 21538802 1:CAS:528:DC%2BC3MXosFamsr0%3D 10.1002/ps.2189
    • Bass C, Field LM (2011) Gene amplification and insecticide resistance. Pest Manag Sci 67(8):886-890
    • (2011) Pest Manag Sci , vol.67 , Issue.8 , pp. 886-890
    • Bass, C.1    Field, L.M.2
  • 7
    • 19644400147 scopus 로고    scopus 로고
    • Insect resistance management in GM crops: Past, present and future
    • 15637622 1:CAS:528:DC%2BD2MXhsFGmtw%3D%3D 10.1038/nbt1056
    • Bates SL, Zhao JZ, Roush RT, Shelton AM (2005) Insect resistance management in GM crops: past, present and future. Nat Biotechnol 23(1):57-62
    • (2005) Nat Biotechnol , vol.23 , Issue.1 , pp. 57-62
    • Bates, S.L.1    Zhao, J.Z.2    Roush, R.T.3    Shelton, A.M.4
  • 8
    • 0031912487 scopus 로고    scopus 로고
    • Golden age of insecticide research: Past, present, or future?
    • 9444749 1:CAS:528:DyaK1cXktlWisg%3D%3D 10.1146/annurev.ento.43.1.1
    • Casida JE, Quistad GB (1998) Golden age of insecticide research: past, present, or future? Annu Rev Entomol 43:1-16
    • (1998) Annu Rev Entomol , vol.43 , pp. 1-16
    • Casida, J.E.1    Quistad, G.B.2
  • 9
    • 84859157566 scopus 로고    scopus 로고
    • Systematic review of biomonitoring studies to determine the association between exposure to organophosphorus and pyrethroid insecticides and human health outcomes
    • 22020228 1:CAS:528:DC%2BC38XkvVKjs7g%3D 10.1016/j.toxlet.2011.10.007
    • Koureas M, Tsakalof A, Tsatsakis A, Hadjichristodoulou C (2012) Systematic review of biomonitoring studies to determine the association between exposure to organophosphorus and pyrethroid insecticides and human health outcomes. Toxicol Lett 210(2):155-168
    • (2012) Toxicol Lett , vol.210 , Issue.2 , pp. 155-168
    • Koureas, M.1    Tsakalof, A.2    Tsatsakis, A.3    Hadjichristodoulou, C.4
  • 10
    • 0036542901 scopus 로고    scopus 로고
    • Alternative insecticides: An urgent need
    • 11998703 10.1016/S1471-4922(01)02220-6
    • Zaim M, Guillet P (2002) Alternative insecticides: an urgent need. Trends Parasitol 18(4):161-163
    • (2002) Trends Parasitol , vol.18 , Issue.4 , pp. 161-163
    • Zaim, M.1    Guillet, P.2
  • 13
    • 79952363866 scopus 로고    scopus 로고
    • On the venom system of centipedes (Chilopoda), a neglected group of venomous animals
    • 21255597 1:CAS:528:DC%2BC3MXjtVCktL8%3D 10.1016/j.toxicon.2011.01.004
    • Undheim EA, King GF (2011) On the venom system of centipedes (Chilopoda), a neglected group of venomous animals. Toxicon 57(4):512-524
    • (2011) Toxicon , vol.57 , Issue.4 , pp. 512-524
    • Undheim, E.A.1    King, G.F.2
  • 14
    • 0034335374 scopus 로고    scopus 로고
    • Neural electrophysiological effect of crude venom of Conus textile from the South China Sea
    • 10775760 1:CAS:528:DC%2BD3cXktF2rt7k%3D 10.1016/S0041-0101(00)00086-6
    • Yang DM, Hu KP, Li CY, Wu CH, Zhou PA (2000) Neural electrophysiological effect of crude venom of Conus textile from the South China Sea. Toxicon 38(11):1607-1612
    • (2000) Toxicon , vol.38 , Issue.11 , pp. 1607-1612
    • Yang, D.M.1    Hu, K.P.2    Li, C.Y.3    Wu, C.H.4    Zhou, P.A.5
  • 15
    • 0035947726 scopus 로고    scopus 로고
    • Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii
    • 11279030 1:CAS:528:DC%2BD3MXktFWnur8%3D 10.1074/jbc.M100216200
    • Orivel J, Redeker V, Le Caer JP, Krier F, Revol-Junelles AM, Longeon A, Chaffotte A, Dejean A, Rossier J (2001) Ponericins, new antibacterial and insecticidal peptides from the venom of the ant Pachycondyla goeldii. J Biol Chem 276(21):17823-17829
    • (2001) J Biol Chem , vol.276 , Issue.21 , pp. 17823-17829
    • Orivel, J.1    Redeker, V.2    Le Caer, J.P.3    Krier, F.4    Revol-Junelles, A.M.5    Longeon, A.6    Chaffotte, A.7    Dejean, A.8    Rossier, J.9
  • 16
    • 0028675596 scopus 로고
    • Purification and characterization of insecticidal toxins from venom glands of the parasitic wasp Bracon hebetor
    • 7703987 1:CAS:528:DyaK2MXjt1Orurc%3D 10.1016/0965-1748(94)90132-5
    • Quistad GB, Nguyen Q, Bernasconi P, Leisy DJ (1994) Purification and characterization of insecticidal toxins from venom glands of the parasitic wasp Bracon hebetor. Insect Biochem Mol Biol 24(10):955-961
    • (1994) Insect Biochem Mol Biol , vol.24 , Issue.10 , pp. 955-961
    • Quistad, G.B.1    Nguyen, Q.2    Bernasconi, P.3    Leisy, D.J.4
  • 17
    • 33847411379 scopus 로고    scopus 로고
    • + channels
    • 17224168 1:CAS:528:DC%2BD2sXis1Cmtrw%3D 10.1016/j.toxicon.2006.11.029
    • + channels. Toxicon 49(4):550-560
    • (2007) Toxicon , vol.49 , Issue.4 , pp. 550-560
    • Bosmans, F.1    Tytgat, J.2
  • 18
    • 25844526403 scopus 로고    scopus 로고
    • Insecticidal activity of proteinous venom from tentacle of jellyfish Rhopilema esculentum Kishinouye
    • 16168648 1:CAS:528:DC%2BD2MXhtVynu7%2FP 10.1016/j.bmcl.2005.08.015
    • Yu HH, Liu XG, Dong XL, Li CP, Xing RE, Liu S, Li PC (2005) Insecticidal activity of proteinous venom from tentacle of jellyfish Rhopilema esculentum Kishinouye. Bioorg Med Chem Lett 15(22):4949-4952
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.22 , pp. 4949-4952
    • Yu, H.H.1    Liu, X.G.2    Dong, X.L.3    Li, C.P.4    Xing, R.E.5    Liu, S.6    Li, P.C.7
  • 19
    • 0018840812 scopus 로고
    • Penetrability of orally toxic protein from cobra venom through the gut of a blowfly
    • 7353052 1:CAS:528:DyaL3cXntVOhsg%3D%3D 10.1016/0304-4165(80)90124-5
    • Primor N, Teitelbaum Z, Zlotkin E (1980) Penetrability of orally toxic protein from cobra venom through the gut of a blowfly. Biochim Biophys Acta 627(1):71-81
    • (1980) Biochim Biophys Acta , vol.627 , Issue.1 , pp. 71-81
    • Primor, N.1    Teitelbaum, Z.2    Zlotkin, E.3
  • 21
    • 79959301228 scopus 로고    scopus 로고
    • + channels isolated from the venom of the theraphosid spider Eucratoscelus constrictus
    • 21447641 1:CAS:528:DC%2BC3MXosFajsLc%3D 10.1124/mol.110.070540
    • + channels isolated from the venom of the theraphosid spider Eucratoscelus constrictus. Mol Pharmacol 80(1):1-13
    • (2011) Mol Pharmacol , vol.80 , Issue.1 , pp. 1-13
    • Windley, M.J.1    Escoubas, P.2    Valenzuela, S.M.3    Nicholson, G.M.4
  • 22
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • Pallaghy PK, Nielsen KJ, Craik DJ, Norton RS (1994) A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci 31:833-1839
    • (1994) Protein Sci , vol.31 , pp. 833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 24
    • 84872130087 scopus 로고    scopus 로고
    • Spider-venom peptides: Structure, pharmacology, and potential for control of insect pests
    • 23020618 1:CAS:528:DC%2BC3sXivVWjtLs%3D 10.1146/annurev-ento-120811- 153650
    • King GF, Hardy MC (2013) Spider-venom peptides: structure, pharmacology, and potential for control of insect pests. Annu Rev Entomol 58:475-496
    • (2013) Annu Rev Entomol , vol.58 , pp. 475-496
    • King, G.F.1    Hardy, M.C.2
  • 25
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • 10936622 1:CAS:528:DC%2BD3cXmsFKisrw%3D 10.1016/S0041-0101(00)00160-4
    • Craik DJ, Daly NL, Waine C (2001) The cystine knot motif in toxins and implications for drug design. Toxicon 39(1):43-60
    • (2001) Toxicon , vol.39 , Issue.1 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 26
    • 0036447597 scopus 로고    scopus 로고
    • Structure and function of insecticidal neurotoxins from Australian funnel-web spiders
    • 1:CAS:528:DC%2BD3sXpvVSh
    • King GF, Tedford HW, Maggio F (2002) Structure and function of insecticidal neurotoxins from Australian funnel-web spiders. J Toxicol-Toxin Rev 21(4):359-389
    • (2002) J Toxicol-Toxin Rev , vol.21 , Issue.4 , pp. 359-389
    • King, G.F.1    Tedford, H.W.2    Maggio, F.3
  • 27
    • 11144319833 scopus 로고    scopus 로고
    • Were arachnids the first to use combinatorial peptide libraries?
    • 15626513 1:CAS:528:DC%2BD2MXjsVOh 10.1016/j.peptides.2004.07.016
    • Sollod BL, Wilson D, Zhaxybayeva O, Gogarten JP, Drinkwater R, King GF (2005) Were arachnids the first to use combinatorial peptide libraries? Peptides 26:131-139
    • (2005) Peptides , vol.26 , pp. 131-139
    • Sollod, B.L.1    Wilson, D.2    Zhaxybayeva, O.3    Gogarten, J.P.4    Drinkwater, R.5    King, G.F.6
  • 29
    • 29844438166 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels
    • 16382098 1:CAS:528:DC%2BD28XhtFWgu74%3D 10.1124/pr.57.4.4
    • Catterall WA, Goldin AL, Waxman SG (2005) International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels. Pharmacol Rev 57(4):397-409
    • (2005) Pharmacol Rev , vol.57 , Issue.4 , pp. 397-409
    • Catterall, W.A.1    Goldin, A.L.2    Waxman, S.G.3
  • 30
    • 52949131528 scopus 로고    scopus 로고
    • Animal peptides targeting voltage-activated sodium channels
    • 18781997 1:CAS:528:DC%2BD1cXhtlehsbzP 10.2174/138161208785777423
    • Billen B, Bosmans F, Tytgat J (2008) Animal peptides targeting voltage-activated sodium channels. Curr Pharm Des 14(24):2492-2502
    • (2008) Curr Pharm des , vol.14 , Issue.24 , pp. 2492-2502
    • Billen, B.1    Bosmans, F.2    Tytgat, J.3
  • 34
    • 0346996705 scopus 로고    scopus 로고
    • Function and solution structure of hainantoxin-I, a novel insect sodium channel inhibitor from the Chinese bird spider Selenocosmia hainana
    • 14675784 1:CAS:528:DC%2BD3sXpvVentbg%3D 10.1016/S0014-5793(03)01303-6
    • Li D, Xiao Y, Hu W, Xie J, Bosmans F, Tytgat J, Liang S (2003) Function and solution structure of hainantoxin-I, a novel insect sodium channel inhibitor from the Chinese bird spider Selenocosmia hainana. FEBS Lett 555(3):616-622
    • (2003) FEBS Lett , vol.555 , Issue.3 , pp. 616-622
    • Li, D.1    Xiao, Y.2    Hu, W.3    Xie, J.4    Bosmans, F.5    Tytgat, J.6    Liang, S.7
  • 35
    • 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
    • 18628201 1:CAS:528:DC%2BD1cXhtFKgsrrE 10.1074/jbc.M708447200
    • Xiao Y, Bingham JP, Zhu W, Moczydlowski E, Liang S, Cummins TR (2008) 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(40):27300-27313
    • (2008) J Biol Chem , vol.283 , Issue.40 , pp. 27300-27313
    • Xiao, Y.1    Bingham, J.P.2    Zhu, W.3    Moczydlowski, E.4    Liang, S.5    Cummins, T.R.6
  • 36
    • 78649959796 scopus 로고    scopus 로고
    • The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation
    • 20855463 1:CAS:528:DC%2BC3cXhsFGgu7bN 10.1124/mol.110.066332
    • Xiao Y, Blumenthal K, Jackson JO 2nd, Liang S, Cummins TR (2010) The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation. Mol Pharmacol 78(6):1124-1134
    • (2010) Mol Pharmacol , vol.78 , Issue.6 , pp. 1124-1134
    • Xiao, Y.1    Blumenthal, K.2    Jackson II, J.O.3    Liang, S.4    Cummins, T.R.5
  • 37
    • 84858336620 scopus 로고    scopus 로고
    • The effects of huwentoxin-I on the voltage-gated sodium channels of rat hippocampal and cockroach dorsal unpaired median neurons
    • 22094230 10.1016/j.peptides.2011.10.029 1:CAS:528:DC%2BC38XjvVWrtL8%3D
    • Wang M, Rong M, Xiao Y, Liang S (2012) The effects of huwentoxin-I on the voltage-gated sodium channels of rat hippocampal and cockroach dorsal unpaired median neurons. Peptides 34(1):19-25
    • (2012) Peptides , vol.34 , Issue.1 , pp. 19-25
    • Wang, M.1    Rong, M.2    Xiao, Y.3    Liang, S.4
  • 38
    • 0142042688 scopus 로고    scopus 로고
    • 2+ channels in differentiated NG108-15 cells, a patch-clamp study
    • 11024489 1:CAS:528:DC%2BD3cXnvVGjurc%3D 10.1016/S0041-0101(00)00150-1
    • 2+ channels in differentiated NG108-15 cells, a patch-clamp study. Toxicon 39(4):491-498
    • (2001) Toxicon , vol.39 , Issue.4 , pp. 491-498
    • Peng, K.1    Chen, X.D.2    Liang, S.P.3
  • 39
    • 0028920782 scopus 로고
    • Purification and amino acid sequence of the insecticidal neurotoxin Tx4(6-1) from the venom of the 'armed' spider Phoneutria nigriventer (Keys)
    • 7778132 1:CAS:528:DyaK2MXksFSjtb0%3D 10.1016/0041-0101(94)00130-Z
    • Figueiredo SG, Garcia ME, Valentim AC, Cordeiro MN, Diniz CR, Richardson M (1995) Purification and amino acid sequence of the insecticidal neurotoxin Tx4(6-1) from the venom of the 'armed' spider Phoneutria nigriventer (Keys). Toxicon 33(1):83-93
    • (1995) Toxicon , vol.33 , Issue.1 , pp. 83-93
    • Figueiredo, S.G.1    Garcia, M.E.2    Valentim, A.C.3    Cordeiro, M.N.4    Diniz, C.R.5    Richardson, M.6
  • 40
    • 0036138970 scopus 로고    scopus 로고
    • The toxin Tx4(6-1) from the spider Phoneutria nigriventer slows down Na+ current inactivation in insect CNS via binding to receptor site 3
    • 12770132 10.1016/S0022-1910(01)00143-3
    • de Lima ME, Stankiewicz M, Hamon A, de Figueiredo SG, Cordeiro MN, Diniz CR, Martin-Eauclaire M, Pelhate M (2002) The toxin Tx4(6-1) from the spider Phoneutria nigriventer slows down Na+ current inactivation in insect CNS via binding to receptor site 3. J Insect Physiol 48(1):53-61
    • (2002) J Insect Physiol , vol.48 , Issue.1 , pp. 53-61
    • De Lima, M.E.1    Stankiewicz, M.2    Hamon, A.3    De Figueiredo, S.G.4    Cordeiro, M.N.5    Diniz, C.R.6    Martin-Eauclaire, M.7    Pelhate, M.8
  • 41
    • 0034598649 scopus 로고    scopus 로고
    • Purification and amino acid sequence of a highly insecticidal toxin from the venom of the Brazilian spider Phoneutria nigriventer which inhibits NMDA-evoked currents in rat hippocampal neurones
    • 10978749 10.1016/S0041-0101(00)00129-X
    • de Figueiredo SG, de Lima ME, Nascimento Cordeiro M, Diniz CR, Patten D, Halliwell RF, Gilroy J, Richardson M (2001) Purification and amino acid sequence of a highly insecticidal toxin from the venom of the Brazilian spider Phoneutria nigriventer which inhibits NMDA-evoked currents in rat hippocampal neurones. Toxicon 39(2-3):309-317
    • (2001) Toxicon , vol.39 , Issue.2-3 , pp. 309-317
    • De Figueiredo, S.G.1    De Lima, M.E.2    Nascimento Cordeiro, M.3    Diniz, C.R.4    Patten, D.5    Halliwell, R.F.6    Gilroy, J.7    Richardson, M.8
  • 42
    • 1642452826 scopus 로고    scopus 로고
    • PnT4-3, a new insect toxin from Phoneutria nigriventer venom elicits the glutamate uptake inhibition exhibited by PhTx4 toxic fraction
    • 14757211 10.1016/j.toxicon.2003.10.009 1:CAS:528:DC%2BD2cXmtFaktw%3D%3D
    • Oliveira LC, De Lima ME, Pimenta AM, Mansuelle P, Rochat H, Cordeiro MN, Richardson M, Figueiredo SG (2003) PnT4-3, a new insect toxin from Phoneutria nigriventer venom elicits the glutamate uptake inhibition exhibited by PhTx4 toxic fraction. Toxicon 42(7):793-800
    • (2003) Toxicon , vol.42 , Issue.7 , pp. 793-800
    • Oliveira, L.C.1    De Lima, M.E.2    Pimenta, A.M.3    Mansuelle, P.4    Rochat, H.5    Cordeiro, M.N.6    Richardson, M.7    Figueiredo, S.G.8
  • 43
    • 0038304846 scopus 로고    scopus 로고
    • Distinct primary structures of the major peptide toxins from the venom of the spider Macrothele gigas that bind to sites 3 and 4 in the sodium channel
    • 12860384 1:CAS:528:DC%2BD3sXlsVaitbc%3D 10.1016/S0014-5793(03)00666-5
    • Corzo G, Gilles N, Satake H, Villegas E, Dai L, Nakajima T, Haupt J (2003) Distinct primary structures of the major peptide toxins from the venom of the spider Macrothele gigas that bind to sites 3 and 4 in the sodium channel. FEBS Lett 547(1-3):43-50
    • (2003) FEBS Lett , vol.547 , Issue.1-3 , pp. 43-50
    • Corzo, G.1    Gilles, N.2    Satake, H.3    Villegas, E.4    Dai, L.5    Nakajima, T.6    Haupt, J.7
  • 44
    • 84863777217 scopus 로고    scopus 로고
    • Spider-venom peptides that target voltage-gated sodium channels: Pharmacological tools and potential therapeutic leads
    • 22543187 1:CAS:528:DC%2BC38XmvVyqu7Y%3D 10.1016/j.toxicon.2012.04.337
    • Klint JK, Senff S, Rupasinghe DB, Er SY, Herzig V, Nicholson GM, King GF (2012) Spider-venom peptides that target voltage-gated sodium channels: pharmacological tools and potential therapeutic leads. Toxicon 60(4):478-491
    • (2012) Toxicon , vol.60 , Issue.4 , pp. 478-491
    • Klint, J.K.1    Senff, S.2    Rupasinghe, D.B.3    Er, S.Y.4    Herzig, V.5    Nicholson, G.M.6    King, G.F.7
  • 45
    • 13444283566 scopus 로고    scopus 로고
    • A spider toxin that induces a typical effect of scorpion α-toxins but competes with β-toxins on binding to insect sodium channels
    • 15683238 1:CAS:528:DC%2BD2MXis12juw%3D%3D 10.1021/bi048434k
    • Corzo G, Escoubas P, Villegas E, Karbat I, Gordon D, Gurevitz M, Nakajima T, Gilles N (2005) A spider toxin that induces a typical effect of scorpion α-toxins but competes with β-toxins on binding to insect sodium channels. Biochemistry 44(5):1542-1549
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1542-1549
    • Corzo, G.1    Escoubas, P.2    Villegas, E.3    Karbat, I.4    Gordon, D.5    Gurevitz, M.6    Nakajima, T.7    Gilles, N.8
  • 46
    • 0033833498 scopus 로고    scopus 로고
    • Isolation, synthesis and pharmacological characterization of δ-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae)
    • 10971590 1:CAS:528:DC%2BD3cXmslGrtLg%3D 10.1046/j.1432-1327.2000.01653.x
    • Corzo G, Escoubas P, Stankiewicz M, Pelhate M, Kristensen CP, Nakajima T (2000) Isolation, synthesis and pharmacological characterization of δ-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae). Eur J Biochem 267(18):5783-5795
    • (2000) Eur J Biochem , vol.267 , Issue.18 , pp. 5783-5795
    • Corzo, G.1    Escoubas, P.2    Stankiewicz, M.3    Pelhate, M.4    Kristensen, C.P.5    Nakajima, T.6
  • 49
    • 77953306009 scopus 로고    scopus 로고
    • + channel gating by novel insect-selective toxins from the spider Agelena orientalis
    • 20385552 1:CAS:528:DC%2BC3cXmvFaqsL8%3D 10.1074/jbc.M110.125211
    • + channel gating by novel insect-selective toxins from the spider Agelena orientalis. J Biol Chem 285(24):18545-18554
    • (2010) J Biol Chem , vol.285 , Issue.24 , pp. 18545-18554
    • Billen, B.1    Vassilevski, A.2    Nikolsky, A.3    Debaveye, S.4    Tytgat, J.5    Grishin, E.6
  • 50
    • 1942438979 scopus 로고    scopus 로고
    • Agatoxins: Ion channel specific toxins from the American funnel web spider, Agelenopsis aperta
    • 15066410 1:CAS:528:DC%2BD2cXislGjsbY%3D 10.1016/j.toxicon.2004.02.004
    • Adams ME (2004) Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta. Toxicon 43(5):509-525
    • (2004) Toxicon , vol.43 , Issue.5 , pp. 509-525
    • Adams, M.E.1
  • 51
    • 33847403885 scopus 로고    scopus 로고
    • V channels by peptidic spider toxins
    • 17197008 1:CAS:528:DC%2BD2sXis1Cmtr4%3D 10.1016/j.toxicon.2006.11.012
    • V channels by peptidic spider toxins. Toxicon 49(4):513-530
    • (2007) Toxicon , vol.49 , Issue.4 , pp. 513-530
    • King, G.F.1
  • 53
    • 0030614894 scopus 로고    scopus 로고
    • 2+ currents in central insect neurons: Electrophysiological and pharmacological properties
    • 9120560 1:CAS:528:DyaK2sXhtlWltrk%3D
    • 2+ currents in central insect neurons: electrophysiological and pharmacological properties. J Neurophysiol 77(1):186-199
    • (1997) J Neurophysiol , vol.77 , Issue.1 , pp. 186-199
    • Wicher, D.1    Penzlin, H.2
  • 54
    • 0030981657 scopus 로고    scopus 로고
    • The structure of a novel insecticidal neurotoxin, ω-atracotoxin- HV1, from the venom of an Australian funnel web spider
    • 9228949 1:CAS:528:DyaK2sXksVeksrk%3D 10.1038/nsb0797-559
    • Fletcher JI, Smith R, O'Donoghue SI, Nilges M, Connor M, Howden ME, Christie MJ, King GF (1997) The structure of a novel insecticidal neurotoxin, ω-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol 4(7):559-566
    • (1997) Nat Struct Biol , vol.4 , Issue.7 , pp. 559-566
    • Fletcher, J.I.1    Smith, R.2    O'Donoghue, S.I.3    Nilges, M.4    Connor, M.5    Howden, M.E.6    Christie, M.J.7    King, G.F.8
  • 56
    • 0033199282 scopus 로고    scopus 로고
    • Structure-function studies of ω-atracotoxin, a potent antagonist of insect voltage-gated calcium channels
    • 10491095 1:CAS:528:DyaK1MXlvFWrsLs%3D 10.1046/j.1432-1327.1999.00646.x
    • Wang X, Smith R, Fletcher JI, Wilson H, Wood CJ, Howden ME, King GF (1999) Structure-function studies of ω-atracotoxin, a potent antagonist of insect voltage-gated calcium channels. Eur J Biochem 264(2):488-494
    • (1999) Eur J Biochem , vol.264 , Issue.2 , pp. 488-494
    • Wang, X.1    Smith, R.2    Fletcher, J.I.3    Wilson, H.4    Wood, C.J.5    Howden, M.E.6    King, G.F.7
  • 57
    • 0035854663 scopus 로고    scopus 로고
    • Functional significance of the β-hairpin in the insecticidal neurotoxin ω-atracotoxin-Hv1a
    • 11313356 1:CAS:528:DC%2BD3MXlsVKntLY%3D 10.1074/jbc.M102199200
    • Tedford HW, Fletcher JI, King GF (2001) Functional significance of the β-hairpin in the insecticidal neurotoxin ω-atracotoxin-Hv1a. J Biol Chem 276:26568-26576
    • (2001) J Biol Chem , vol.276 , pp. 26568-26576
    • Tedford, H.W.1    Fletcher, J.I.2    King, G.F.3
  • 58
    • 6344287807 scopus 로고    scopus 로고
    • Scanning mutagenesis of ω-atracotoxin-Hv1a reveals a spatially restricted epitope that confers selective activity against insect calcium channels
    • 15308644 1:CAS:528:DC%2BD2cXot1yns7w%3D 10.1074/jbc.M404006200
    • Tedford HW, Gilles N, Menez A, Doering CJ, Zamponi GW, King GF (2004) Scanning mutagenesis of ω-atracotoxin-Hv1a reveals a spatially restricted epitope that confers selective activity against insect calcium channels. J Biol Chem 279(42):44133-44140
    • (2004) J Biol Chem , vol.279 , Issue.42 , pp. 44133-44140
    • Tedford, H.W.1    Gilles, N.2    Menez, A.3    Doering, C.J.4    Zamponi, G.W.5    King, G.F.6
  • 61
    • 0029084407 scopus 로고
    • Three-dimensional solution structure of the calcium channel antagonist ω-agatoxin IVA: Consensus molecular folding of calcium channel blockers
    • 7623383 1:CAS:528:DyaK2MXnt1agtrg%3D 10.1006/jmbi.1995.0406
    • Kim JI, Konishi S, Iwai H, Kohno T, Gouda H, Shimada I, Sato K, Arata Y (1995) Three-dimensional solution structure of the calcium channel antagonist ω-agatoxin IVA: consensus molecular folding of calcium channel blockers. J Mol Biol 250(5):659-671
    • (1995) J Mol Biol , vol.250 , Issue.5 , pp. 659-671
    • Kim, J.I.1    Konishi, S.2    Iwai, H.3    Kohno, T.4    Gouda, H.5    Shimada, I.6    Sato, K.7    Arata, Y.8
  • 62
    • 0141767105 scopus 로고    scopus 로고
    • Huwentoxin-V, a novel insecticidal peptide toxin from the spider Selenocosmia huwena, and a natural mutant of the toxin: Indicates the key amino acid residues related to the biological activity
    • 12893056 1:CAS:528:DC%2BD3sXlslers78%3D 10.1016/S0041-0101(03)00095-3
    • Zhang PF, Chen P, Hu WJ, Liang SP (2003) Huwentoxin-V, a novel insecticidal peptide toxin from the spider Selenocosmia huwena, and a natural mutant of the toxin: indicates the key amino acid residues related to the biological activity. Toxicon 42(1):15-20
    • (2003) Toxicon , vol.42 , Issue.1 , pp. 15-20
    • Zhang, P.F.1    Chen, P.2    Hu, W.J.3    Liang, S.P.4
  • 63
    • 0029328421 scopus 로고
    • Synthesis of an O-palmitoylated 44-residue peptide amide (PLTX-II) blocking presynaptic calcium channels in Drosophila
    • 8527876 1:CAS:528:DyaK2MXotlKlurY%3D
    • Bodi J, Nishio H, Zhou Y, Branton WD, Kimura T, Sakakibara S (1995) Synthesis of an O-palmitoylated 44-residue peptide amide (PLTX-II) blocking presynaptic calcium channels in Drosophila. Pept Res 8(4):228-235
    • (1995) Pept Res , vol.8 , Issue.4 , pp. 228-235
    • Bodi, J.1    Nishio, H.2    Zhou, Y.3    Branton, W.D.4    Kimura, T.5    Sakakibara, S.6
  • 64
    • 49649104531 scopus 로고    scopus 로고
    • Biochemical characterization of cysteine-rich peptides from Oxyopes sp. Venom that block calcium ion channels
    • 18606178 1:CAS:528:DC%2BD1cXhtVaisrjI 10.1016/j.toxicon.2008.05.019
    • Villegas E, Adachi-Akahane S, Bosmans F, Tytgat J, Nakajima T, Corzo G (2008) Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels. Toxicon 52(2):228-236
    • (2008) Toxicon , vol.52 , Issue.2 , pp. 228-236
    • Villegas, E.1    Adachi-Akahane, S.2    Bosmans, F.3    Tytgat, J.4    Nakajima, T.5    Corzo, G.6
  • 65
    • 0034043512 scopus 로고    scopus 로고
    • Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge
    • 10881200 1:CAS:528:DC%2BD3cXktFantLc%3D 10.1038/75921
    • Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF (2000) Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol 7(6):505-513
    • (2000) Nat Struct Biol , vol.7 , Issue.6 , pp. 505-513
    • Wang, X.1    Connor, M.2    Smith, R.3    Maciejewski, M.W.4    Howden, M.E.5    Nicholson, G.M.6    Christie, M.J.7    King, G.F.8
  • 66
    • 0037151037 scopus 로고    scopus 로고
    • Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function
    • 11937509 1:CAS:528:DC%2BD38XltVGku70%3D 10.1074/jbc.M202297200
    • Maggio F, King GF (2002) Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function. J Biol Chem 277(25):22806-22813
    • (2002) J Biol Chem , vol.277 , Issue.25 , pp. 22806-22813
    • Maggio, F.1    King, G.F.2
  • 69
    • 58149241373 scopus 로고    scopus 로고
    • Novel α-KTx sites in the BK channel and comparative sequence analysis reveal distinguishing features of the BK and KV channel outer pore
    • 18815746 1:CAS:528:DC%2BD1cXhtF2gs7nI 10.1007/s12013-008-9026-3
    • Giangiacomo KM, Becker J, Garsky C, Schmalhofer W, Garcia ML, Mullmann TJ (2008) Novel α-KTx sites in the BK channel and comparative sequence analysis reveal distinguishing features of the BK and KV channel outer pore. Cell Biochem Biophys 52(1):47-58
    • (2008) Cell Biochem Biophys , vol.52 , Issue.1 , pp. 47-58
    • Giangiacomo, K.M.1    Becker, J.2    Garsky, C.3    Schmalhofer, W.4    Garcia, M.L.5    Mullmann, T.J.6
  • 70
    • 0033991583 scopus 로고    scopus 로고
    • A point mutation in the maxi-K clone dSlo forms a high affinity site for charybdotoxin
    • 1:CAS:528:DyaK1MXnvFejurs%3D 10.1016/S0028-3908(99)00074-X
    • Myers MP, Stampe P (2000) A point mutation in the maxi-K clone dSlo forms a high affinity site for charybdotoxin. Neuropharmacol 39(1):11-20
    • (2000) Neuropharmacol , vol.39 , Issue.1 , pp. 11-20
    • Myers, M.P.1    Stampe, P.2
  • 71
    • 6544276937 scopus 로고    scopus 로고
    • On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
    • 9020148 1:CAS:528:DyaK2sXht1Oqsbs%3D 10.1074/jbc.272.7.4302
    • Dauplais M, Lecoq A, Song J, Cotton J, Jamin N, Gilquin B, Roumestand C, Vita C, de Medeiros CL, Rowan EG, Harvey AL, Menez A (1997) On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J Biol Chem 272(7):4302-4309
    • (1997) J Biol Chem , vol.272 , Issue.7 , pp. 4302-4309
    • Dauplais, M.1    Lecoq, A.2    Song, J.3    Cotton, J.4    Jamin, N.5    Gilquin, B.6    Roumestand, C.7    Vita, C.8    De Medeiros, C.L.9    Rowan, E.G.10    Harvey, A.L.11    Menez, A.12
  • 72
    • 0034663625 scopus 로고    scopus 로고
    • A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel
    • 10861934 1:CAS:528:DC%2BD3cXlsFCrtb0%3D 10.1002/1097-0134(20000815)40: 3<436: AID-PROT90>3.0.CO;2-9
    • Mosbah A, Kharrat R, Fajloun Z, Renisio JG, Blanc E, Sabatier JM, El Ayeb M, Darbon H (2000) A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel. Proteins 40(3):436-442
    • (2000) Proteins , vol.40 , Issue.3 , pp. 436-442
    • Mosbah, A.1    Kharrat, R.2    Fajloun, Z.3    Renisio, J.G.4    Blanc, E.5    Sabatier, J.M.6    El Ayeb, M.7    Darbon, H.8
  • 73
    • 3042727965 scopus 로고    scopus 로고
    • Isolation and characterization of a novel lepidopteran-selective toxin from the venom of South Indian red scorpion, Mesobuthus tamulus
    • 10.1186/1471-2091-2-16
    • Wudayagiri R, Inceoglu B, Herrmann R, Derbel M, Choudary PV, Hammock BD (2001) Isolation and characterization of a novel lepidopteran-selective toxin from the venom of South Indian red scorpion, Mesobuthus tamulus. BMC Biochem 216(2):16
    • (2001) BMC Biochem , vol.216 , Issue.2 , pp. 16
    • Wudayagiri, R.1    Inceoglu, B.2    Herrmann, R.3    Derbel, M.4    Choudary, P.V.5    Hammock, B.D.6
  • 74
    • 0027466723 scopus 로고
    • Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion
    • 8383429 1:CAS:528:DyaK3sXmtF2nsLg%3D
    • DeBin JA, Maggio JE, Strichartz GR (1993) Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am J Physiol 264(2 Pt 1):C361-C369
    • (1993) Am J Physiol , vol.264 , Issue.2 PART 1
    • Debin, J.A.1    Maggio, J.E.2    Strichartz, G.R.3
  • 75
    • 0032423609 scopus 로고    scopus 로고
    • Purification and partial characterization of a 'short' insectotoxin-like peptide from the venom of the scorpion Parabuthus schlechteri
    • 9891977 1:CAS:528:DyaK1MXhslWksQ%3D%3D 10.1016/S0014-5793(98)01589-0
    • Tytgat J, Debont T, Rostoll K, Muller GJ, Verdonck F, Daenens P, van der Walt JJ, Possani LD (1998) Purification and partial characterization of a 'short' insectotoxin-like peptide from the venom of the scorpion Parabuthus schlechteri. FEBS Lett 441(3):387-391
    • (1998) FEBS Lett , vol.441 , Issue.3 , pp. 387-391
    • Tytgat, J.1    Debont, T.2    Rostoll, K.3    Muller, G.J.4    Verdonck, F.5    Daenens, P.6    Van Der Walt, J.J.7    Possani, L.D.8
  • 76
    • 0037423212 scopus 로고    scopus 로고
    • Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2
    • 12454020 1:CAS:528:DC%2BD3sXot1ynsA%3D%3D 10.1074/jbc.M205662200
    • Deshane J, Garner CC, Sontheimer H (2003) Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2. J Biol Chem 278(6):4135-4144
    • (2003) J Biol Chem , vol.278 , Issue.6 , pp. 4135-4144
    • Deshane, J.1    Garner, C.C.2    Sontheimer, H.3
  • 77
    • 77951151896 scopus 로고    scopus 로고
    • Annexin A2 is a molecular target for TM601, a peptide with tumor-targeting and anti-angiogenic effects
    • 20018898 1:CAS:528:DC%2BC3cXhs1altbY%3D 10.1074/jbc.M109.066092
    • Kesavan K, Ratliff J, Johnson EW, Dahlberg W, Asara JM, Misra P, Frangioni JV, Jacoby DB (2010) Annexin A2 is a molecular target for TM601, a peptide with tumor-targeting and anti-angiogenic effects. J Biol Chem 285(7):4366-4374
    • (2010) J Biol Chem , vol.285 , Issue.7 , pp. 4366-4374
    • Kesavan, K.1    Ratliff, J.2    Johnson, E.W.3    Dahlberg, W.4    Asara, J.M.5    Misra, P.6    Frangioni, J.V.7    Jacoby, D.B.8
  • 78
    • 84884353929 scopus 로고
    • The nature of the membrane-receptors for scorpion-venom neurotoxin
    • 1:CAS:528:DyaL3cXlt1Kksbs%3D
    • Grishin EV, Soldatov NM, Ovchinnikov YA (1980) The nature of the membrane-receptors for scorpion-venom neurotoxin. Bioorg Khim 6(6):914-922
    • (1980) Bioorg Khim , vol.6 , Issue.6 , pp. 914-922
    • Grishin, E.V.1    Soldatov, N.M.2    Ovchinnikov, Y.A.3
  • 79
    • 72249106546 scopus 로고    scopus 로고
    • Insecticidal activity of scorpion toxin (ButaIT) and snowdrop lectin (GNA) containing fusion proteins towards pest species of different orders
    • 19728320 1:CAS:528:DC%2BD1MXhsFGrsbrM 10.1002/ps.1833
    • Fitches EC, Bell HA, Powell ME, Back E, Sargiotti C, Weaver RJ, Gatehouse JA (2010) Insecticidal activity of scorpion toxin (ButaIT) and snowdrop lectin (GNA) containing fusion proteins towards pest species of different orders. Pest Manag Sci 66(1):74-83
    • (2010) Pest Manag Sci , vol.66 , Issue.1 , pp. 74-83
    • Fitches, E.C.1    Bell, H.A.2    Powell, M.E.3    Back, E.4    Sargiotti, C.5    Weaver, R.J.6    Gatehouse, J.A.7
  • 80
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt Consortium 10.1093/nar/gkr981 1:CAS:528:DC%2BC3MXhs12htbjF
    • UniProt Consortium (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucl Acids Res 40:D71-D75
    • (2012) Nucl Acids Res , vol.40
  • 81
    • 77954415694 scopus 로고    scopus 로고
    • Conotoxin venom peptide therapeutics
    • 20047034 1:CAS:528:DC%2BC3cXhtlSgsL7N 10.1007/978-1-4419-1132-2-5
    • Lewis RJ (2009) Conotoxin venom peptide therapeutics. Adv Exp Med Biol 655:44-48
    • (2009) Adv Exp Med Biol , vol.655 , pp. 44-48
    • Lewis, R.J.1
  • 82
    • 77951774753 scopus 로고    scopus 로고
    • μ-Conotoxins as leads in the development of new analgesics
    • 20428082 1:CAS:528:DC%2BC3cXlsFelurw%3D 10.3390/molecules15042825
    • Norton RS (2010) μ-Conotoxins as leads in the development of new analgesics. Molecules 15(4):2825-2844
    • (2010) Molecules , vol.15 , Issue.4 , pp. 2825-2844
    • Norton, R.S.1
  • 83
    • 84858178207 scopus 로고    scopus 로고
    • Conus venom peptide pharmacology
    • 22407615 1:CAS:528:DC%2BC38XmslKksbc%3D 10.1124/pr.111.005322
    • Lewis RJ, Dutertre S, Vetter I, Christie MJ (2012) Conus venom peptide pharmacology. Pharmacol Rev 64(2):259-298
    • (2012) Pharmacol Rev , vol.64 , Issue.2 , pp. 259-298
    • Lewis, R.J.1    Dutertre, S.2    Vetter, I.3    Christie, M.J.4
  • 84
    • 0031791992 scopus 로고    scopus 로고
    • + currents in neurosecretory insect neurons
    • 9826912 1:CAS:528:DyaK1cXmtFygsrs%3D
    • + currents in neurosecretory insect neurons. Receptors Channels 5(6):355-366
    • (1998) Receptors Channels , vol.5 , Issue.6 , pp. 355-366
    • Wicher, D.1    Penzlin, H.2
  • 86
    • 0006637980 scopus 로고
    • ω-Conotoxin: Direct and persistent blockade of specific types of calcium channels in neurons but not muscle
    • 2438698 1:CAS:528:DyaL2sXktlCkt7Y%3D 10.1073/pnas.84.12.4327
    • McCleskey EW, Fox AP, Feldman DH, Cruz LJ, Olivera BM, Tsien RW, Yoshikami D (1987) ω-Conotoxin: direct and persistent blockade of specific types of calcium channels in neurons but not muscle. Proc Natl Acad Sci USA 84(12):4327-4331
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.12 , pp. 4327-4331
    • McCleskey, E.W.1    Fox, A.P.2    Feldman, D.H.3    Cruz, L.J.4    Olivera, B.M.5    Tsien, R.W.6    Yoshikami, D.7
  • 88
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • 12074021 1:CAS:528:DyaK28XivVyksrg%3D 10.1038/381148a0
    • Terlau H, Shon KJ, Grilley M, Stocker M, Stuhmer W, Olivera BM (1996) Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature 381(6578):148-151
    • (1996) Nature , vol.381 , Issue.6578 , pp. 148-151
    • Terlau, H.1    Shon, K.J.2    Grilley, M.3    Stocker, M.4    Stuhmer, W.5    Olivera, B.M.6
  • 90
    • 0025932018 scopus 로고
    • Mollusc-specific toxins from the venom of Conus textile neovicarius
    • 1761058 1:CAS:528:DyaK38Xltlarsg%3D%3D 10.1111/j.1432-1033.1991.tb16412.x
    • Fainzilber M, Gordon D, Hasson A, Spira ME, Zlotkin E (1991) Mollusc-specific toxins from the venom of Conus textile neovicarius. Eur J Biochem 202(2):589-595
    • (1991) Eur J Biochem , vol.202 , Issue.2 , pp. 589-595
    • Fainzilber, M.1    Gordon, D.2    Hasson, A.3    Spira, M.E.4    Zlotkin, E.5
  • 91
    • 79959373747 scopus 로고    scopus 로고
    • Recombinant conotoxin, TxVIA, produced in yeast has insecticidal activity
    • 21640131 1:CAS:528:DC%2BC3MXnvFOhsLk%3D 10.1016/j.toxicon.2011.05.009
    • Bruce C, Fitches EC, Chougule N, Bell HA, Gatehouse JA (2011) Recombinant conotoxin, TxVIA, produced in yeast has insecticidal activity. Toxicon 58(1):93-100
    • (2011) Toxicon , vol.58 , Issue.1 , pp. 93-100
    • Bruce, C.1    Fitches, E.C.2    Chougule, N.3    Bell, H.A.4    Gatehouse, J.A.5
  • 92
    • 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
    • 8300586 1:CAS:528:DyaK2cXhvVGjtLo%3D
    • Fainzilber M, Kofman O, Zlotkin E, Gordon D (1994) 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(4):2574-2580
    • (1994) J Biol Chem , vol.269 , Issue.4 , pp. 2574-2580
    • Fainzilber, M.1    Kofman, O.2    Zlotkin, E.3    Gordon, D.4
  • 93
    • 0028855708 scopus 로고
    • A new conotoxin affecting sodium current inactivation interacts with the δ-conotoxin receptor site
    • 7836370 1:CAS:528:DyaK2MXjtFOksLk%3D 10.1074/jbc.270.3.1123
    • Fainzilber M, Lodder JC, Kits KS, Kofman O, Vinnitsky I, Van Rietschoten J, Zlotkin E, Gordon D (1995) A new conotoxin affecting sodium current inactivation interacts with the δ-conotoxin receptor site. J Biol Chem 270(3):1123-1129
    • (1995) J Biol Chem , vol.270 , Issue.3 , pp. 1123-1129
    • Fainzilber, M.1    Lodder, J.C.2    Kits, K.S.3    Kofman, O.4    Vinnitsky, I.5    Van Rietschoten, J.6    Zlotkin, E.7    Gordon, D.8
  • 94
    • 21844466444 scopus 로고    scopus 로고
    • Molecular interaction of δ-conotoxins with voltage-gated sodium channels
    • 15990094 1:CAS:528:DC%2BD2MXmt1ejur8%3D 10.1016/j.febslet.2005.05.077
    • Leipold E, Hansel A, Olivera BM, Terlau H, Heinemann SH (2005) Molecular interaction of δ-conotoxins with voltage-gated sodium channels. FEBS Lett 579(18):3881-3884
    • (2005) FEBS Lett , vol.579 , Issue.18 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 95
    • 34250017052 scopus 로고    scopus 로고
    • Conotoxins of the O-superfamily affecting voltage-gated sodium channels
    • 17385074 1:CAS:528:DC%2BD2sXntVOgsro%3D 10.1007/s00018-007-6565-5
    • Heinemann SH, Leipold E (2007) Conotoxins of the O-superfamily affecting voltage-gated sodium channels. Cell Mol Life Sci 64(11):1329-1340
    • (2007) Cell Mol Life Sci , vol.64 , Issue.11 , pp. 1329-1340
    • Heinemann, S.H.1    Leipold, E.2
  • 96
    • 0037184042 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the sodium channel agonist/antagonist δ-conotoxin TxVIA
    • 12145313 1:CAS:528:DC%2BD38XnsVCjtL8%3D 10.1074/jbc.M206833200
    • Kohno T, Sasaki T, Kobayashi K, Fainzilber M, Sato K (2002) Three-dimensional solution structure of the sodium channel agonist/antagonist δ-conotoxin TxVIA. J Biol Chem 277(39):36387-36391
    • (2002) J Biol Chem , vol.277 , Issue.39 , pp. 36387-36391
    • Kohno, T.1    Sasaki, T.2    Kobayashi, K.3    Fainzilber, M.4    Sato, K.5
  • 97
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • 1720574 1:CAS:528:DyaK38Xltlakuw%3D%3D 10.1126/science.1720574
    • Bontems F, Roumestand C, Gilquin B, Menez A, Toma F (1991) Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science 254(5037):1521-1523
    • (1991) Science , vol.254 , Issue.5037 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 98
    • 0029644729 scopus 로고
    • Refined three-dimensional solution structure of insect defensin A
    • 7663941 1:CAS:528:DyaK2MXlvFyhsLo%3D 10.1016/S0969-2126(01)00177-0
    • Cornet B, Bonmatin JM, Hetru C, Hoffmann JA, Ptak M, Vovelle F (1995) Refined three-dimensional solution structure of insect defensin A. Structure 3(5):435-448
    • (1995) Structure , vol.3 , Issue.5 , pp. 435-448
    • Cornet, B.1    Bonmatin, J.M.2    Hetru, C.3    Hoffmann, J.A.4    Ptak, M.5    Vovelle, F.6
  • 99
    • 36248957133 scopus 로고    scopus 로고
    • A review of defensins of diverse origins
    • 1:CAS:528:DC%2BD2sXhtlSisbzO 10.2174/138920307782411446
    • Wong JH, Xia L, Ng TB (2007) A review of defensins of diverse origins. Curr Prot Pept Sci 8(5):446-459
    • (2007) Curr Prot Pept Sci , vol.8 , Issue.5 , pp. 446-459
    • Wong, J.H.1    Xia, L.2    Ng, T.B.3
  • 100
    • 27144432006 scopus 로고    scopus 로고
    • Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily
    • 16143827 1:CAS:528:DC%2BD2MXht1ShsbrP 10.1007/s00018-005-5200-6
    • Zhu S, Gao B, Tytgat J (2005) Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily. Cell Mol Life Sci 62(19-20):2257-2269
    • (2005) Cell Mol Life Sci , vol.62 , Issue.19-20 , pp. 2257-2269
    • Zhu, S.1    Gao, B.2    Tytgat, J.3
  • 102
    • 0015197045 scopus 로고
    • Purification and properties of the insect toxin from the venom of the scorpion Androctonus australis Hector
    • 5150738 1:CAS:528:DyaE38XktFGhur4%3D 10.1016/S0300-9084(71)80195-5
    • Zlotkin E, Rochat H, Miranda F, Kopeyan C, Lissitzky S (1971) Purification and properties of the insect toxin from the venom of the scorpion Androctonus australis Hector. Biochimie 53(10):1073-1078
    • (1971) Biochimie , vol.53 , Issue.10 , pp. 1073-1078
    • Zlotkin, E.1    Rochat, H.2    Miranda, F.3    Kopeyan, C.4    Lissitzky, S.5
  • 104
    • 0029738506 scopus 로고    scopus 로고
    • Functional expression and genetic alteration of an alpha scorpion neurotoxin
    • 8756487 1:CAS:528:DyaK28Xkt1yltbY%3D 10.1021/bi9528309
    • Zilberberg N, Gordon D, Pelhate M, Adams ME, Norris TM, Zlotkin E, Gurevitz M (1996) Functional expression and genetic alteration of an alpha scorpion neurotoxin. Biochemistry 35(31):10215-10222
    • (1996) Biochemistry , vol.35 , Issue.31 , pp. 10215-10222
    • Zilberberg, N.1    Gordon, D.2    Pelhate, M.3    Adams, M.E.4    Norris, T.M.5    Zlotkin, E.6    Gurevitz, M.7
  • 105
    • 0030611173 scopus 로고    scopus 로고
    • Bot IT2: A new scorpion toxin to study receptor site on insect sodium channels
    • 9094428 1:CAS:528:DyaK2sXhvFWhtbg%3D 10.1016/S0014-5793(97)00160-9
    • Cestele S, Borchani L, El Ayeb M, Rochat H (1997) Bot IT2: a new scorpion toxin to study receptor site on insect sodium channels. FEBS Lett 405(1):77-80
    • (1997) FEBS Lett , vol.405 , Issue.1 , pp. 77-80
    • Cestele, S.1    Borchani, L.2    El Ayeb, M.3    Rochat, H.4
  • 106
    • 0025303099 scopus 로고
    • A scorpion venom neurotoxin paralytic to insects that affects sodium current inactivation: Purification, primary structure, and mode of action
    • 2383565 1:CAS:528:DyaK3cXktF2hsL8%3D 10.1021/bi00477a009
    • Eitan M, Fowler E, Herrmann R, Duval A, Pelhate M, Zlotkin E (1990) A scorpion venom neurotoxin paralytic to insects that affects sodium current inactivation: purification, primary structure, and mode of action. Biochemistry 29(25):5941-5947
    • (1990) Biochemistry , vol.29 , Issue.25 , pp. 5941-5947
    • Eitan, M.1    Fowler, E.2    Herrmann, R.3    Duval, A.4    Pelhate, M.5    Zlotkin, E.6
  • 107
    • 0025111065 scopus 로고
    • Characterization of the transcript for a depressant insect selective neurotoxin gene with an isolated cDNA clone from the scorpion Buthotus judaicus
    • 2387406 1:CAS:528:DyaK3cXlsVKmtbk%3D 10.1016/0014-5793(90)81161-G
    • Gurevitz M, Zlotkin E, Zilberberg N (1990) Characterization of the transcript for a depressant insect selective neurotoxin gene with an isolated cDNA clone from the scorpion Buthotus judaicus. FEBS Lett 269(1):229-232
    • (1990) FEBS Lett , vol.269 , Issue.1 , pp. 229-232
    • Gurevitz, M.1    Zlotkin, E.2    Zilberberg, N.3
  • 108
    • 0029851928 scopus 로고    scopus 로고
    • An insect-specific toxin from Centruroides noxius Hoffmann. CDNA, primary structure, three-dimensional model and electrostatic surface potentials in comparison with other toxin variants
    • 8973638 1:CAS:528:DyaK2sXjvFOk 10.1111/j.1432-1033.1996.0235r.x
    • Selisko B, Garcia C, Becerril B, Delepierre M, Possani LD (1996) An insect-specific toxin from Centruroides noxius Hoffmann. cDNA, primary structure, three-dimensional model and electrostatic surface potentials in comparison with other toxin variants. Eur J Biochem 242(2):235-242
    • (1996) Eur J Biochem , vol.242 , Issue.2 , pp. 235-242
    • Selisko, B.1    Garcia, C.2    Becerril, B.3    Delepierre, M.4    Possani, L.D.5
  • 109
    • 33846513431 scopus 로고    scopus 로고
    • Voltage-gated ion channels and gating modifier toxins
    • 17239913 1:CAS:528:DC%2BD2sXps1emuw%3D%3D 10.1016/j.toxicon.2006.09.022
    • Catterall WA, Cestele S, Yarov-Yarovoy V, Yu FH, Konoki K, Scheuer T (2007) Voltage-gated ion channels and gating modifier toxins. Toxicon 49(2):124-141
    • (2007) Toxicon , vol.49 , Issue.2 , pp. 124-141
    • Catterall, W.A.1    Cestele, S.2    Yarov-Yarovoy, V.3    Yu, F.H.4    Konoki, K.5    Scheuer, T.6
  • 110
    • 33846474874 scopus 로고    scopus 로고
    • Voltage-gated sodium channel modulation by scorpion α-toxins
    • 17087986 1:CAS:528:DC%2BD2sXps1elsg%3D%3D 10.1016/j.toxicon.2006.09.023
    • Bosmans F, Tytgat J (2007) Voltage-gated sodium channel modulation by scorpion α-toxins. Toxicon 49(2):142-158
    • (2007) Toxicon , vol.49 , Issue.2 , pp. 142-158
    • Bosmans, F.1    Tytgat, J.2
  • 111
    • 3843138450 scopus 로고    scopus 로고
    • Molecular basis of the high insecticidal potency of scorpion α-toxins
    • 15133045 1:CAS:528:DC%2BD2cXlslOrt7w%3D 10.1074/jbc.M402048200
    • Karbat I, Frolow F, Froy O, Gilles N, Cohen L, Turkov M, Gordon D, Gurevitz M (2004) Molecular basis of the high insecticidal potency of scorpion α-toxins. J Biol Chem 279(30):31679-31686
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31679-31686
    • Karbat, I.1    Frolow, F.2    Froy, O.3    Gilles, N.4    Cohen, L.5    Turkov, M.6    Gordon, D.7    Gurevitz, M.8
  • 113
    • 0033543581 scopus 로고    scopus 로고
    • Crystal structures of two α-like scorpion toxins: Non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel
    • 10493862 1:CAS:528:DyaK1MXlvFyksr8%3D 10.1006/jmbi.1999.3036
    • He XL, Li HM, Zeng ZH, Liu XQ, Wang M, Wang DC (1999) Crystal structures of two α-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel. J Mol Biol 292(1):125-135
    • (1999) J Mol Biol , vol.292 , Issue.1 , pp. 125-135
    • He, X.L.1    Li, H.M.2    Zeng, Z.H.3    Liu, X.Q.4    Wang, M.5    Wang, D.C.6
  • 114
    • 4143091852 scopus 로고    scopus 로고
    • Structural mechanism governing cis and trans isomeric states and an intramolecular switch for cis/trans isomerization of a non-proline peptide bond observed in crystal structures of scorpion toxins
    • 15321715 1:CAS:528:DC%2BD2cXmsVCrtL8%3D 10.1016/j.jmb.2004.06.067
    • Guan RJ, Xiang Y, He XL, Wang CG, Wang M, Zhang Y, Sundberg EJ, Wang DC (2004) Structural mechanism governing cis and trans isomeric states and an intramolecular switch for cis/trans isomerization of a non-proline peptide bond observed in crystal structures of scorpion toxins. J Mol Biol 341(5):1189-1204
    • (2004) J Mol Biol , vol.341 , Issue.5 , pp. 1189-1204
    • Guan, R.J.1    Xiang, Y.2    He, X.L.3    Wang, C.G.4    Wang, M.5    Zhang, Y.6    Sundberg, E.J.7    Wang, D.C.8
  • 115
    • 26844484788 scopus 로고    scopus 로고
    • + channel selectivity of the scorpion α-like toxin BmK M1
    • 16209876 1:CAS:528:DC%2BD2MXhtFCjsLfI 10.1016/j.jmb.2005.08.068
    • + channel selectivity of the scorpion α-like toxin BmK M1. J Mol Biol 353(4):788-803
    • (2005) J Mol Biol , vol.353 , Issue.4 , pp. 788-803
    • Ye, X.1    Bosmans, F.2    Li, C.3    Zhang, Y.4    Wang, D.C.5    Tytgat, J.6
  • 116
    • 72949110796 scopus 로고    scopus 로고
    • Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese scorpion Buthus martensii Karsch
    • 19932686 1:CAS:528:DC%2BC3cXpsVGr 10.1016/j.bbrc.2009.11.110
    • Zhu J, Tong X, Cao C, Wu G, Zhang N, Wu H (2010) Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese scorpion Buthus martensii Karsch. Biochem Biophys Res Commun 391(1):627-633
    • (2010) Biochem Biophys Res Commun , vol.391 , Issue.1 , pp. 627-633
    • Zhu, J.1    Tong, X.2    Cao, C.3    Wu, G.4    Zhang, N.5    Wu, H.6
  • 117
    • 0030598925 scopus 로고    scopus 로고
    • Crystal structure of an acidic neurotoxin from scorpion Buthus martensii Karsch at 1.85 Å resolution
    • 8780783 1:CAS:528:DyaK28XltlKisL4%3D 10.1006/jmbi.1996.0473
    • Li HM, Wang DC, Zeng ZH, Jin L, Hu RQ (1996) Crystal structure of an acidic neurotoxin from scorpion Buthus martensii Karsch at 1.85 Å resolution. J Mol Biol 261(3):415-431
    • (1996) J Mol Biol , vol.261 , Issue.3 , pp. 415-431
    • Li, H.M.1    Wang, D.C.2    Zeng, Z.H.3    Jin, L.4    Hu, R.Q.5
  • 118
    • 0033613920 scopus 로고    scopus 로고
    • NMR structures and activity of a novel α-like toxin from the scorpion Leiurus quinquestriatus hebraeus
    • 9917409 1:CAS:528:DyaK1MXhtV2htbw%3D 10.1006/jmbi.1998.2418
    • Krimm I, Gilles N, Sautiere P, Stankiewicz M, Pelhate M, Gordon D, Lancelin JM (1999) NMR structures and activity of a novel α-like toxin from the scorpion Leiurus quinquestriatus hebraeus. J Mol Biol 285(4):1749-1763
    • (1999) J Mol Biol , vol.285 , Issue.4 , pp. 1749-1763
    • Krimm, I.1    Gilles, N.2    Sautiere, P.3    Stankiewicz, M.4    Pelhate, M.5    Gordon, D.6    Lancelin, J.M.7
  • 119
    • 84856073147 scopus 로고    scopus 로고
    • Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels
    • 1:CAS:528:DC%2BC38XmvFart7k%3D
    • Zhu S, Peigneur S, Gao B, Lu X, Cao C, Tytgat J (2012) Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels. Mol Cell Proteomics 11(1):1-18
    • (2012) Mol Cell Proteomics , vol.11 , Issue.1 , pp. 1-18
    • Zhu, S.1    Peigneur, S.2    Gao, B.3    Lu, X.4    Cao, C.5    Tytgat, J.6
  • 120
    • 80053416574 scopus 로고    scopus 로고
    • Elucidation of the molecular basis of selective recognition uncovers the interaction site for the core domain of scorpion α-toxins on sodium channels
    • 21832067 1:CAS:528:DC%2BC3MXht1Cqtb%2FE 10.1074/jbc.M111.259507
    • Gur M, Kahn R, Karbat I, Regev N, Wang J, Catterall WA, Gordon D, Gurevitz M (2011) Elucidation of the molecular basis of selective recognition uncovers the interaction site for the core domain of scorpion α-toxins on sodium channels. J Biol Chem 286(40):35209-35217
    • (2011) J Biol Chem , vol.286 , Issue.40 , pp. 35209-35217
    • Gur, M.1    Kahn, R.2    Karbat, I.3    Regev, N.4    Wang, J.5    Catterall, W.A.6    Gordon, D.7    Gurevitz, M.8
  • 121
    • 14244265321 scopus 로고    scopus 로고
    • Common features in the functional surface of scorpion β-toxins and elements that confer specificity for insect and mammalian voltage-gated sodium channels
    • 15569679 1:CAS:528:DC%2BD2MXhtVymur0%3D 10.1074/jbc.M408427200
    • Cohen L, Karbat I, Gilles N, Ilan N, Benveniste M, Gordon D, Gurevitz M (2005) Common features in the functional surface of scorpion β-toxins and elements that confer specificity for insect and mammalian voltage-gated sodium channels. J Biol Chem 280(6):5045-5053
    • (2005) J Biol Chem , vol.280 , Issue.6 , pp. 5045-5053
    • Cohen, L.1    Karbat, I.2    Gilles, N.3    Ilan, N.4    Benveniste, M.5    Gordon, D.6    Gurevitz, M.7
  • 122
    • 33846396124 scopus 로고    scopus 로고
    • X-ray structure and mutagenesis of the scorpion depressant toxin LqhIT2 reveals key determinants crucial for activity and anti-insect selectivity
    • 17166514 1:CAS:528:DC%2BD2sXhtVejt7s%3D 10.1016/j.jmb.2006.10.085
    • Karbat I, Turkov M, Cohen L, Kahn R, Gordon D, Gurevitz M, Frolow F (2007) X-ray structure and mutagenesis of the scorpion depressant toxin LqhIT2 reveals key determinants crucial for activity and anti-insect selectivity. J Mol Biol 366(2):586-601
    • (2007) J Mol Biol , vol.366 , Issue.2 , pp. 586-601
    • Karbat, I.1    Turkov, M.2    Cohen, L.3    Kahn, R.4    Gordon, D.5    Gurevitz, M.6    Frolow, F.7
  • 125
    • 0033605851 scopus 로고    scopus 로고
    • Solution structure of toxin 2 from Centruroides noxius Hoffmann, a β-scorpion neurotoxin acting on sodium channels
    • 10080898 1:CAS:528:DyaK1MXhvVaht74%3D 10.1006/jmbi.1999.2611
    • Pintar A, Possani LD, Delepierre M (1999) Solution structure of toxin 2 from Centruroides noxius Hoffmann, a β-scorpion neurotoxin acting on sodium channels. J Mol Biol 287(2):359-367
    • (1999) J Mol Biol , vol.287 , Issue.2 , pp. 359-367
    • Pintar, A.1    Possani, L.D.2    Delepierre, M.3
  • 126
    • 0033735270 scopus 로고    scopus 로고
    • The binding of BmK IT2, a depressant insect-selective scorpion toxin on mammal and insect sodium channels
    • 11070192 1:CAS:528:DC%2BD3cXosFOqs74%3D 10.1016/S0168-0102(00)00164-4
    • Li YJ, Tan ZY, Ji YH (2000) The binding of BmK IT2, a depressant insect-selective scorpion toxin on mammal and insect sodium channels. Neurosci Res 38(3):257-264
    • (2000) Neurosci Res , vol.38 , Issue.3 , pp. 257-264
    • Li, Y.J.1    Tan, Z.Y.2    Ji, Y.H.3
  • 127
    • 0026801059 scopus 로고
    • Localization of receptor sites for insect-selective toxins on sodium channels by site-directed antibodies
    • 1324719 1:CAS:528:DyaK38XltVKjs7s%3D 10.1021/bi00148a025
    • Gordon D, Moskowitz H, Eitan M, Warner C, Catterall WA, Zlotkin E (1992) Localization of receptor sites for insect-selective toxins on sodium channels by site-directed antibodies. Biochemistry 31(33):7622-7628
    • (1992) Biochemistry , vol.31 , Issue.33 , pp. 7622-7628
    • Gordon, D.1    Moskowitz, H.2    Eitan, M.3    Warner, C.4    Catterall, W.A.5    Zlotkin, E.6
  • 128
    • 0021682684 scopus 로고
    • The binding of the insect-selective neurotoxin (AaIT) from scorpion-venom to locust synaptosomal membranes
    • 1:CAS:528:DyaL2MXhvFaktQ%3D%3D 10.1016/0005-2736(84)90379-1
    • Gordon D, Jover E, Couraud F, Zlotkin E (1984) The binding of the insect-selective neurotoxin (AaIT) from scorpion-venom to locust synaptosomal membranes. Biochim Biophys Acta 778(2):349-358
    • (1984) Biochim Biophys Acta , vol.778 , Issue.2 , pp. 349-358
    • Gordon, D.1    Jover, E.2    Couraud, F.3    Zlotkin, E.4
  • 129
    • 0031020104 scopus 로고    scopus 로고
    • Biochemical and pharmacological characterization of a depressant insect toxin from the venom of the scorpion Buthacus arenicola
    • 9030726 1:CAS:528:DyaK2sXhtVWitr8%3D 10.1111/j.1432-1033.1997.93-1a.x
    • Cestele S, Kopeyan C, Oughideni R, Mansuelle P, Granier C, Rochat H (1997) Biochemical and pharmacological characterization of a depressant insect toxin from the venom of the scorpion Buthacus arenicola. Eur J Biochem 243(1-2):93-99
    • (1997) Eur J Biochem , vol.243 , Issue.1-2 , pp. 93-99
    • Cestele, S.1    Kopeyan, C.2    Oughideni, R.3    Mansuelle, P.4    Granier, C.5    Rochat, H.6
  • 130
    • 0036618134 scopus 로고    scopus 로고
    • Domain 2 of Drosophila para voltage-gated sodium channel confers insect properties to a rat brain channel
    • 12040042 1:CAS:528:DC%2BD38XksFWgtb0%3D
    • Shichor I, Zlotkin E, Ilan N, Chikashvili D, Stuhmer W, Gordon D, Lotan I (2002) Domain 2 of Drosophila para voltage-gated sodium channel confers insect properties to a rat brain channel. J Neurosci 22(11):4364-4371
    • (2002) J Neurosci , vol.22 , Issue.11 , pp. 4364-4371
    • Shichor, I.1    Zlotkin, E.2    Ilan, N.3    Chikashvili, D.4    Stuhmer, W.5    Gordon, D.6    Lotan, I.7
  • 131
    • 79251581335 scopus 로고    scopus 로고
    • Localization of receptor site on insect sodium channel for depressant β-toxin BmK IT2
    • 21264295 1:CAS:528:DC%2BC3MXhtFWnt7g%3D 10.1371/journal.pone.0014510
    • He H, Liu Z, Dong B, Zhang J, Shu X, Zhou J, Ji Y (2011) Localization of receptor site on insect sodium channel for depressant β-toxin BmK IT2. PLoS ONE 6(1):e14510
    • (2011) PLoS ONE , vol.6 , Issue.1 , pp. 14510
    • He, H.1    Liu, Z.2    Dong, B.3    Zhang, J.4    Shu, X.5    Zhou, J.6    Ji, Y.7
  • 133
    • 84865733660 scopus 로고    scopus 로고
    • Mapping the interaction site for a β-scorpion toxin in the pore module of domain III of voltage-gated Na+ channels
    • 22761417 1:CAS:528:DC%2BC38Xht1yqtLrN 10.1074/jbc.M112.370742
    • Zhang JZ, Yarov-Yarovoy V, Scheuer T, Karbat I, Cohen L, Gordon D, Gurevitz M, Catterall WA (2012) Mapping the interaction site for a β-scorpion toxin in the pore module of domain III of voltage-gated Na+ channels. J Biol Chem 287(36):30719-30728
    • (2012) J Biol Chem , vol.287 , Issue.36 , pp. 30719-30728
    • Zhang, J.Z.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Karbat, I.4    Cohen, L.5    Gordon, D.6    Gurevitz, M.7    Catterall, W.A.8
  • 134
    • 0001302972 scopus 로고
    • The tolerance of lepidopterous larvae to an insect selective neurotoxin
    • 1:CAS:528:DyaK3MXhvFaiug%3D%3D 10.1016/0020-1790(90)90075-6
    • Herrmann R, Fishman L, Zlotkin E (1990) The tolerance of lepidopterous larvae to an insect selective neurotoxin. Insect Biochemistry 20(6):625-637
    • (1990) Insect Biochemistry , vol.20 , Issue.6 , pp. 625-637
    • Herrmann, R.1    Fishman, L.2    Zlotkin, E.3
  • 135
    • 0026621019 scopus 로고
    • Oral toxicity to flesh flies of a neurotoxic polypeptide
    • 1421443 1:CAS:528:DyaK38XmtVKrsb0%3D 10.1002/arch.940210105
    • Zlotkin E, Fishman L, Shapiro JP (1992) Oral toxicity to flesh flies of a neurotoxic polypeptide. Arch Insect Biochem Physiol 21(1):41-52
    • (1992) Arch Insect Biochem Physiol , vol.21 , Issue.1 , pp. 41-52124
    • Zlotkin, E.1    Fishman, L.2    Shapiro, J.P.3
  • 136
    • 0031001258 scopus 로고    scopus 로고
    • Insect tolerance to a neurotoxic polypeptide: Pharmacokinetic and pharmacodynamic aspects
    • 9318940 1:CAS:528:DyaK2sXlt1WmsbY%3D
    • Fishman L, Herrmann R, Gordon D, Zlotkin E (1997) Insect tolerance to a neurotoxic polypeptide: pharmacokinetic and pharmacodynamic aspects. J Exp Biol 200(Pt 7):1115-1123
    • (1997) J Exp Biol , vol.200 , Issue.PART 7 , pp. 1115-1123
    • Fishman, L.1    Herrmann, R.2    Gordon, D.3    Zlotkin, E.4
  • 137
    • 34248583581 scopus 로고    scopus 로고
    • Isolation of the first toxin from the scorpion Buthus occitanus israelis showing preference for shaker potassium channels
    • 17490656 1:CAS:528:DC%2BD2sXlvFamsLg%3D 10.1016/j.febslet.2007.04.065
    • Kozminsky-Atias A, Somech E, Zilberberg N (2007) Isolation of the first toxin from the scorpion Buthus occitanus israelis showing preference for shaker potassium channels. FEBS Lett 581(13):2478-2484
    • (2007) FEBS Lett , vol.581 , Issue.13 , pp. 2478-2484
    • Kozminsky-Atias, A.1    Somech, E.2    Zilberberg, N.3
  • 138
    • 0023270432 scopus 로고
    • Sequence of a probable potassium channel component encoded at shaker locus of Drosophila
    • 2441471 1:CAS:528:DyaL1cXhvVWisbg%3D 10.1126/science.2441471
    • Tempel BL, Papazian DM, Schwarz TL, Jan YN, Jan LY (1987) Sequence of a probable potassium channel component encoded at shaker locus of Drosophila. Science 237(4816):770-775
    • (1987) Science , vol.237 , Issue.4816 , pp. 770-775
    • Tempel, B.L.1    Papazian, D.M.2    Schwarz, T.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 140
    • 0032753963 scopus 로고    scopus 로고
    • A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies
    • 10542442 1:CAS:528:DyaK1MXns1ylsbk%3D 10.1016/S0165-6147(99)01398-X
    • Tytgat J, Chandy KG, Garcia ML, Gutman GA, Martin-Eauclaire MF, van der Walt JJ, Possani LD (1999) A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies. Trends Pharmacol Sci 20(11):444-447
    • (1999) Trends Pharmacol Sci , vol.20 , Issue.11 , pp. 444-447
    • Tytgat, J.1    Chandy, K.G.2    Garcia, M.L.3    Gutman, G.A.4    Martin-Eauclaire, M.F.5    Van Der Walt, J.J.6    Possani, L.D.7
  • 141
    • 0030064382 scopus 로고    scopus 로고
    • + channel selectivity filter by mutant cycle-based structure analysis
    • 8562077 1:CAS:528:DyaK28XosFCrug%3D%3D 10.1016/S0896-6273(00)80030-6
    • + channel selectivity filter by mutant cycle-based structure analysis. Neuron 16(1):131-139
    • (1996) Neuron , vol.16 , Issue.1 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    Mackinnon, R.3
  • 142
    • 0036840108 scopus 로고    scopus 로고
    • + channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • 12414693 1:CAS:528:DC%2BD38Xos1Crsbo%3D 10.1016/S0006-3495(02)75270-3
    • + channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles. Biophys J 83(5):2595-2609
    • (2002) Biophys J , vol.83 , Issue.5 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 143
    • 79960586218 scopus 로고    scopus 로고
    • Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif
    • 21670253 1:CAS:528:DC%2BC3MXovFent7c%3D 10.1073/pnas.1103501108
    • Smith JJ, Hill JM, Little MJ, Nicholson GM, King GF, Alewood PF (2011) Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif. Proc Natl Acad Sci USA 108(26):10478-10483
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.26 , pp. 10478-10483
    • Smith, J.J.1    Hill, J.M.2    Little, M.J.3    Nicholson, G.M.4    King, G.F.5    Alewood, P.F.6
  • 144
    • 67349224086 scopus 로고    scopus 로고
    • Insecticidal peptides from the theraposid spider Brachypelma albiceps: An NMR-based model of Ba2
    • 19374957 1:CAS:528:DC%2BD1MXnt1yisL0%3D 10.1016/j.bbapap.2009.04.004
    • Corzo G, Bernard C, Clement H, Villegas E, Bosmans F, Tytgat J, Possani LD, Darbon H, Alagon A (2009) Insecticidal peptides from the theraposid spider Brachypelma albiceps: an NMR-based model of Ba2. Biochim Biophys Acta 1794(8):1190-1196
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.8 , pp. 1190-1196
    • Corzo, G.1    Bernard, C.2    Clement, H.3    Villegas, E.4    Bosmans, F.5    Tytgat, J.6    Possani, L.D.7    Darbon, H.8    Alagon, A.9
  • 146
    • 34548817288 scopus 로고    scopus 로고
    • Purification and characterization of a novel short-chain insecticidal toxin with two disulfide bridges from the venom of the scorpion Liocheles australasiae
    • 17681581 1:CAS:528:DC%2BD2sXhtV2qsbzN 10.1016/j.toxicon.2007.06.014
    • Matsushita N, Miyashita M, Sakai A, Nakagawa Y, Miyagawa H (2007) Purification and characterization of a novel short-chain insecticidal toxin with two disulfide bridges from the venom of the scorpion Liocheles australasiae. Toxicon 50(6):861-867
    • (2007) Toxicon , vol.50 , Issue.6 , pp. 861-867
    • Matsushita, N.1    Miyashita, M.2    Sakai, A.3    Nakagawa, Y.4    Miyagawa, H.5
  • 147
    • 67649414216 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum
    • 19379768 1:CAS:528:DC%2BD1MXotVKjsbc%3D 10.1016/j.toxicon.2009.04.010
    • Silva EC, Camargos TS, Maranhao AQ, Silva-Pereira I, Silva LP, Possani LD, Schwartz EF (2009) Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum. Toxicon 54(3):252-261
    • (2009) Toxicon , vol.54 , Issue.3 , pp. 252-261
    • Silva, E.C.1    Camargos, T.S.2    Maranhao, A.Q.3    Silva-Pereira, I.4    Silva, L.P.5    Possani, L.D.6    Schwartz, E.F.7
  • 148
    • 0028277938 scopus 로고
    • Neuropeptide y effector systems: Perspectives for drug development
    • 7754533 1:CAS:528:DyaK2cXksFSitrg%3D 10.1016/0165-6147(94)90076-0
    • Grundemar L, Hakanson R (1994) Neuropeptide Y effector systems: perspectives for drug development. Trends Pharmacol Sci 15(5):153-159
    • (1994) Trends Pharmacol Sci , vol.15 , Issue.5 , pp. 153-159
    • Grundemar, L.1    Hakanson, R.2
  • 149
    • 0013980779 scopus 로고
    • Hypotensive peptides: Bradykinin, kallidin, and eledoisin
    • 5333768 1:CAS:528:DyaF2sXptF2mug%3D%3D 10.1016/S1054-3589(08)60097-6
    • Erdos EG (1966) Hypotensive peptides: bradykinin, kallidin, and eledoisin. Adv Pharmacol 4:1-90
    • (1966) Adv Pharmacol , vol.4 , pp. 1-90
    • Erdos, E.G.1
  • 150
    • 0025008260 scopus 로고
    • Structure of a protein superfiber: Spider dragline silk
    • 2402494 1:CAS:528:DyaK3MXitlGq 10.1073/pnas.87.18.7120
    • Xu M, Lewis RV (1990) Structure of a protein superfiber: spider dragline silk. Proc Natl Acad Sci USA 87(18):7120-7124
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.18 , pp. 7120-7124
    • Xu, M.1    Lewis, R.V.2
  • 151
    • 36148983045 scopus 로고    scopus 로고
    • Inducible antibacterial response of scorpion venom gland
    • 18023929 1:CAS:528:DC%2BD2sXhtlCqsrrP 10.1016/j.peptides.2007.10.004
    • Gao B, Tian C, Zhu S (2007) Inducible antibacterial response of scorpion venom gland. Peptides 28(12):2299-2305
    • (2007) Peptides , vol.28 , Issue.12 , pp. 2299-2305
    • Gao, B.1    Tian, C.2    Zhu, S.3
  • 153
    • 0026532161 scopus 로고
    • Antimicrobial properties of secretions from the metapleural glands of Myrmecia gulosa (the Australian bull ant)
    • 1568945 1:STN:280:DyaK383jsVyntg%3D%3D 10.1111/j.1365-2672.1992.tb01822.x
    • Veal DA, Trimble JE, Beattie AJ (1992) Antimicrobial properties of secretions from the metapleural glands of Myrmecia gulosa (the Australian bull ant). J Appl Bacteriol 72(3):188-194
    • (1992) J Appl Bacteriol , vol.72 , Issue.3 , pp. 188-194
    • Veal, D.A.1    Trimble, J.E.2    Beattie, A.J.3
  • 154
    • 0025311318 scopus 로고
    • A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin
    • 2358464 1:CAS:528:DyaK3cXkvFemsLo%3D
    • Fujiwara S, Imai J, Fujiwara M, Yaeshima T, Kawashima T, Kobayashi K (1990) A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. J Biol Chem 265(19):11333-11337
    • (1990) J Biol Chem , vol.265 , Issue.19 , pp. 11333-11337
    • Fujiwara, S.1    Imai, J.2    Fujiwara, M.3    Yaeshima, T.4    Kawashima, T.5    Kobayashi, K.6
  • 155
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • 10590307 1:CAS:528:DyaK1MXnslylsr4%3D
    • Bechinger B (1999) The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim Biophys Acta 1462(1-2):157-183
    • (1999) Biochim Biophys Acta , vol.1462 , Issue.1-2 , pp. 157-183
    • Bechinger, B.1
  • 156
    • 18344373480 scopus 로고    scopus 로고
    • Scorpion venom peptides without disulfide bridges
    • 16036557 1:CAS:528:DC%2BD2MXjvFaisbk%3D 10.1080/15216540500058899
    • Zeng XC, Corzo G, Hahin R (2005) Scorpion venom peptides without disulfide bridges. IUBMB Life 57(1):13-21
    • (2005) IUBMB Life , vol.57 , Issue.1 , pp. 13-21
    • Zeng, X.C.1    Corzo, G.2    Hahin, R.3
  • 157
    • 0347991711 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic peptides of venomous arthropods
    • 14685689 1:CAS:528:DC%2BD2cXivFCktLY%3D 10.1007/s00018-003-3106-8
    • Kuhn-Nentwig L (2003) Antimicrobial and cytolytic peptides of venomous arthropods. Cell Mol Life Sci 60(12):2651-2668
    • (2003) Cell Mol Life Sci , vol.60 , Issue.12 , pp. 2651-2668
    • Kuhn-Nentwig, L.1
  • 159
    • 77249126426 scopus 로고    scopus 로고
    • A novel amphipathic linear peptide with both insect toxicity and antimicrobial activity from the venom of the scorpion Isometrus maculatus
    • 20139620 1:CAS:528:DC%2BC3cXjtVajsrc%3D 10.1271/bbb.90723
    • Miyashita M, Sakai A, Matsushita N, Hanai Y, Nakagawa Y, Miyagawa H (2010) A novel amphipathic linear peptide with both insect toxicity and antimicrobial activity from the venom of the scorpion Isometrus maculatus. Biosci Biotechnol Biochem 74(2):364-369
    • (2010) Biosci Biotechnol Biochem , vol.74 , Issue.2 , pp. 364-369
    • Miyashita, M.1    Sakai, A.2    Matsushita, N.3    Hanai, Y.4    Nakagawa, Y.5    Miyagawa, H.6
  • 160
    • 0037189567 scopus 로고    scopus 로고
    • Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins
    • 11976325 1:CAS:528:DC%2BD38XltF2ntLg%3D 10.1074/jbc.M200511200
    • Corzo G, Villegas E, Gomez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T (2002) Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. J Biol Chem 277(26):23627-23637
    • (2002) J Biol Chem , vol.277 , Issue.26 , pp. 23627-23637
    • Corzo, G.1    Villegas, E.2    Gomez-Lagunas, F.3    Possani, L.D.4    Belokoneva, O.S.5    Nakajima, T.6
  • 161
    • 33745347364 scopus 로고    scopus 로고
    • Isolation and characterisation of conomap-Vt, a D-amino acid containing excitatory peptide from the venom of a vermivorous cone snail
    • 16797543 1:CAS:528:DC%2BD28Xms1ahuro%3D 10.1016/j.febslet.2006.06.011
    • Dutertre S, Lumsden NG, Alewood PF, Lewis RJ (2006) Isolation and characterisation of conomap-Vt, a D-amino acid containing excitatory peptide from the venom of a vermivorous cone snail. FEBS Lett 580(16):3860-3866
    • (2006) FEBS Lett , vol.580 , Issue.16 , pp. 3860-3866
    • Dutertre, S.1    Lumsden, N.G.2    Alewood, P.F.3    Lewis, R.J.4
  • 162
    • 0026034945 scopus 로고
    • Lom-AG-myotropin: A novel myotropic peptide from the male accessory glands of Locusta migratoria
    • 2052501 1:CAS:528:DyaK3MXhvVansL8%3D 10.1016/0196-9781(91)90158-L
    • Paemen L, Tips A, Schoofs L, Proost P, Van Damme J, De Loof A (1991) Lom-AG-myotropin: a novel myotropic peptide from the male accessory glands of Locusta migratoria. Peptides 12(1):7-10
    • (1991) Peptides , vol.12 , Issue.1 , pp. 7-10
    • Paemen, L.1    Tips, A.2    Schoofs, L.3    Proost, P.4    Van Damme, J.5    De Loof, A.6
  • 163
    • 0027583961 scopus 로고
    • Structure and function of the molluscan myoactive tetradecapeptides
    • 7763794 1:CAS:528:DyaK2cXltlSntb0%3D
    • Harada A, Yoshida M, Minakata H, Nomoto K, Muneoka Y, Kobayashi M (1993) Structure and function of the molluscan myoactive tetradecapeptides. Zool Sci 10(2):257-265
    • (1993) Zool Sci , vol.10 , Issue.2 , pp. 257-265
    • Harada, A.1    Yoshida, M.2    Minakata, H.3    Nomoto, K.4    Muneoka, Y.5    Kobayashi, M.6
  • 164
    • 77953812194 scopus 로고    scopus 로고
    • Human β-defensin 1: A restless warrior against allergies, infections and cancer
    • 20100591 1:CAS:528:DC%2BC3cXlsFKms7s%3D 10.1016/j.biocel.2010.01.021
    • Prado-Montes de Oca E (2010) Human β-defensin 1: a restless warrior against allergies, infections and cancer. Int J Biochem Cell Biol 42(6):800-804
    • (2010) Int J Biochem Cell Biol , vol.42 , Issue.6 , pp. 800-804
    • Prado-Montes De Oca, E.1
  • 168
    • 70350379630 scopus 로고    scopus 로고
    • Structures of sea anemone toxins
    • 19285996 1:CAS:528:DC%2BD1MXhtlekt7rJ 10.1016/j.toxicon.2009.02.035
    • Norton RS (2009) Structures of sea anemone toxins. Toxicon 54(8):1075-1088
    • (2009) Toxicon , vol.54 , Issue.8 , pp. 1075-1088
    • Norton, R.S.1
  • 169
    • 51749125812 scopus 로고    scopus 로고
    • Intron retention as a posttranscriptional regulatory mechanism of neurotoxin expression at early life stages of the starlet anemone Nematostella vectensis
    • 18538344 1:CAS:528:DC%2BD1cXns1eitrc%3D 10.1016/j.jmb.2008.05.011
    • Moran Y, Weinberger H, Reitzel AM, Sullivan JC, Kahn R, Gordon D, Finnerty JR, Gurevitz M (2008) Intron retention as a posttranscriptional regulatory mechanism of neurotoxin expression at early life stages of the starlet anemone Nematostella vectensis. J Mol Biol 380(3):437-443
    • (2008) J Mol Biol , vol.380 , Issue.3 , pp. 437-443
    • Moran, Y.1    Weinberger, H.2    Reitzel, A.M.3    Sullivan, J.C.4    Kahn, R.5    Gordon, D.6    Finnerty, J.R.7    Gurevitz, M.8
  • 170
    • 84870325152 scopus 로고    scopus 로고
    • A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins
    • 22972919 1:CAS:528:DC%2BC38XhvVCgtrbE 10.1096/fj.12-218479
    • Peigneur S, Beress L, Moller C, Mari F, Forssmann WG, Tytgat J (2012) A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. Faseb J 26(12):5141-5151
    • (2012) Faseb J , vol.26 , Issue.12 , pp. 5141-5151
    • Peigneur, S.1    Beress, L.2    Moller, C.3    Mari, F.4    Forssmann, W.G.5    Tytgat, J.6
  • 171
    • 0037021470 scopus 로고    scopus 로고
    • The sea anemone Bunodosoma granulifera contains surprisingly efficacious and potent insect-selective toxins
    • 12459477 1:CAS:528:DC%2BD38XovFGks7k%3D 10.1016/S0014-5793(02)03653-0
    • Bosmans F, Aneiros A, Tytgat J (2002) The sea anemone Bunodosoma granulifera contains surprisingly efficacious and potent insect-selective toxins. FEBS Lett 532(1-2):131-134
    • (2002) FEBS Lett , vol.532 , Issue.1-2 , pp. 131-134
    • Bosmans, F.1    Aneiros, A.2    Tytgat, J.3
  • 173
    • 0028245287 scopus 로고
    • Positively charged amino acid residues located similarly in sea anemone and scorpion toxins
    • 7911468 1:CAS:528:DyaK2cXltVWmuro%3D
    • Loret EP, del Valle RM, Mansuelle P, Sampieri F, Rochat H (1994) Positively charged amino acid residues located similarly in sea anemone and scorpion toxins. J Biol Chem 269(24):16785-16788
    • (1994) J Biol Chem , vol.269 , Issue.24 , pp. 16785-16788
    • Loret, E.P.1    Del Valle, R.M.2    Mansuelle, P.3    Sampieri, F.4    Rochat, H.5
  • 174
    • 0027981495 scopus 로고
    • Three-dimensional structure in solution of neurotoxin III from the sea anemone Anemonia sulcata
    • 7727358 1:CAS:528:DyaK2cXlslaltrw%3D 10.1021/bi00203a001
    • Manoleras N, Norton RS (1994) Three-dimensional structure in solution of neurotoxin III from the sea anemone Anemonia sulcata. Biochemistry 33(37):11051-11061
    • (1994) Biochemistry , vol.33 , Issue.37 , pp. 11051-11061
    • Manoleras, N.1    Norton, R.S.2
  • 175
    • 0343240064 scopus 로고
    • Asexual reproduction, diet, and anomalies of anemone Nematostella vectensis in Nova Scotia
    • Frank PG, Bleakney JS (1978) Asexual reproduction, diet, and anomalies of anemone Nematostella vectensis in Nova Scotia. Can Field Nat 92(3):259-263
    • (1978) Can Field Nat , vol.92 , Issue.3 , pp. 259-263
    • Frank, P.G.1    Bleakney, J.S.2
  • 176
    • 33746220061 scopus 로고    scopus 로고
    • Expression and mutagenesis of the sea anemone toxin Av2 reveals key amino acid residues important for activity on voltage-gated sodium channels
    • 16846229 1:CAS:528:DC%2BD28XmtlOmsLw%3D 10.1021/bi060386b
    • Moran Y, Cohen L, Kahn R, Karbat I, Gordon D, Gurevitz M (2006) Expression and mutagenesis of the sea anemone toxin Av2 reveals key amino acid residues important for activity on voltage-gated sodium channels. Biochemistry 45(29):8864-8873
    • (2006) Biochemistry , vol.45 , Issue.29 , pp. 8864-8873
    • Moran, Y.1    Cohen, L.2    Kahn, R.3    Karbat, I.4    Gordon, D.5    Gurevitz, M.6
  • 178
    • 0030010219 scopus 로고    scopus 로고
    • Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel
    • 8621610 1:CAS:528:DyaK28XisFSmur8%3D 10.1074/jbc.271.16.9422
    • Dias-Kadambi BL, Drum CL, Hanck DA, Blumenthal KM (1996) Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel. J Biol Chem 271(16):9422-9428
    • (1996) J Biol Chem , vol.271 , Issue.16 , pp. 9422-9428
    • Dias-Kadambi, B.L.1    Drum, C.L.2    Hanck, D.A.3    Blumenthal, K.M.4
  • 179
    • 0029911653 scopus 로고    scopus 로고
    • Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurin B
    • 8639500 1:CAS:528:DyaK28XhtlWit7o%3D 10.1021/bi9528457
    • Khera PK, Blumenthal KM (1996) Importance of highly conserved anionic residues and electrostatic interactions in the activity and structure of the cardiotonic polypeptide anthopleurin B. Biochemistry 35(11):3503-3507
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3503-3507
    • Khera, P.K.1    Blumenthal, K.M.2
  • 180
    • 0035184582 scopus 로고    scopus 로고
    • Contryphans from Conus textile venom ducts
    • 11137539 1:CAS:528:DC%2BD3MXmsVyluw%3D%3D 10.1016/S0041-0101(00)00210-5
    • Jimenez EC, Watkins M, Juszczak LJ, Cruz LJ, Olivera BM (2001) Contryphans from Conus textile venom ducts. Toxicon 39(6):803-808
    • (2001) Toxicon , vol.39 , Issue.6 , pp. 803-808
    • Jimenez, E.C.1    Watkins, M.2    Juszczak, L.J.3    Cruz, L.J.4    Olivera, B.M.5
  • 181
    • 84862180786 scopus 로고    scopus 로고
    • ConoServer: Updated content, knowledge, and discovery tools in the conopeptide database
    • 22058133 1:CAS:528:DC%2BC3MXhs12hurrJ 10.1093/nar/gkr886
    • Kaas Q, Yu R, Jin AH, Dutertre S, Craik DJ (2012) ConoServer: updated content, knowledge, and discovery tools in the conopeptide database. Nucl Acids Res 40:D325-D330
    • (2012) Nucl Acids Res , vol.40
    • Kaas, Q.1    Yu, R.2    Jin, A.H.3    Dutertre, S.4    Craik, D.J.5
  • 183
    • 77956063164 scopus 로고    scopus 로고
    • Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets
    • 20670641 1:CAS:528:DC%2BC3cXhtVyjtL3N 10.1016/j.toxicon.2010.07.010
    • Kini RM, Doley R (2010) Structure, function and evolution of three-finger toxins: mini proteins with multiple targets. Toxicon 56(6):855-867
    • (2010) Toxicon , vol.56 , Issue.6 , pp. 855-867
    • Kini, R.M.1    Doley, R.2
  • 184
    • 0026451624 scopus 로고
    • Nuclear magnetic resonance solution structure of the α-neurotoxin from the black mamba (Dendroaspis polylepis polylepis)
    • 1433289 1:CAS:528:DyaK3sXjsVWrsA%3D%3D 10.1016/0022-2836(92)90525-O
    • Brown LR, Wuthrich K (1992) Nuclear magnetic resonance solution structure of the α-neurotoxin from the black mamba (Dendroaspis polylepis polylepis). J Mol Biol 227(4):1118-1135
    • (1992) J Mol Biol , vol.227 , Issue.4 , pp. 1118-1135
    • Brown, L.R.1    Wuthrich, K.2
  • 185
    • 34548348973 scopus 로고    scopus 로고
    • Actions of snake neurotoxins on an insect nicotinic cholinergic synapse
    • 1:CAS:528:DC%2BD2sXpsF2lu74%3D 10.1007/s10158-007-0053-3
    • Hue B, Buckingham SD, Buckingham D, Sattelle DB (2007) Actions of snake neurotoxins on an insect nicotinic cholinergic synapse. Invertebr Neurosci 7(3):173-178
    • (2007) Invertebr Neurosci , vol.7 , Issue.3 , pp. 173-178
    • Hue, B.1    Buckingham, S.D.2    Buckingham, D.3    Sattelle, D.B.4
  • 186
    • 33847415775 scopus 로고    scopus 로고
    • Insecticidal toxins from black widow spider venom
    • 17210168 1:CAS:528:DC%2BD2sXis1Cmtr8%3D 10.1016/j.toxicon.2006.11.021
    • Rohou A, Nield J, Ushkaryov YA (2007) Insecticidal toxins from black widow spider venom. Toxicon 49(4):531-549
    • (2007) Toxicon , vol.49 , Issue.4 , pp. 531-549
    • Rohou, A.1    Nield, J.2    Ushkaryov, Y.A.3
  • 188
    • 84861719028 scopus 로고    scopus 로고
    • Sphingomyelinase D in sicariid spider venom is a potent insecticidal toxin
    • 22561243 1:CAS:528:DC%2BC38XptVKktLo%3D 10.1016/j.toxicon.2012.04.350
    • Zobel-Thropp PA, Kerins AE, Binford GJ (2012) Sphingomyelinase D in sicariid spider venom is a potent insecticidal toxin. Toxicon 60(3):265-271
    • (2012) Toxicon , vol.60 , Issue.3 , pp. 265-271
    • Zobel-Thropp, P.A.1    Kerins, A.E.2    Binford, G.J.3
  • 189
    • 33646563390 scopus 로고    scopus 로고
    • Loxoscelism
    • 16714202 10.1016/j.clindermatol.2005.11.006
    • Swanson DL, Vetter RS (2006) Loxoscelism. Clin Dermatol 24(3):213-221
    • (2006) Clin Dermatol , vol.24 , Issue.3 , pp. 213-221
    • Swanson, D.L.1    Vetter, R.S.2
  • 190
    • 31344451320 scopus 로고    scopus 로고
    • Orally active acaricidal peptide toxins from spider venom
    • 16330063 1:CAS:528:DC%2BD28Xnsl2isg%3D%3D 10.1016/j.toxicon.2005.10.011
    • Mukherjee AK, Sollod BL, Wikel SK, King GF (2006) Orally active acaricidal peptide toxins from spider venom. Toxicon 47:182-187
    • (2006) Toxicon , vol.47 , pp. 182-187
    • Mukherjee, A.K.1    Sollod, B.L.2    Wikel, S.K.3    King, G.F.4
  • 192
    • 0035013453 scopus 로고    scopus 로고
    • In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; Mechanisms of insecticidal action
    • 11356425 1:CAS:528:DC%2BD3MXjsFWgtr0%3D 10.1016/S0022-1910(01)00068-3
    • Fitches E, Woodhouse SD, Edwards JP, Gatehouse JA (2001) In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal action. J Insect Physiol 47:777-787
    • (2001) J Insect Physiol , vol.47 , pp. 777-787
    • Fitches, E.1    Woodhouse, S.D.2    Edwards, J.P.3    Gatehouse, J.A.4
  • 193
    • 84862659177 scopus 로고    scopus 로고
    • Fusion to snowdrop lectin magnifies the oral activity of insecticidal ω-hexatoxin-Hv1a peptide by enabling its delivery to the central nervous system
    • 22761779 1:CAS:528:DC%2BC38XpvVWltr8%3D 10.1371/journal.pone.0039389
    • Fitches EC, Pyati P, King GF, Gatehouse JA (2012) Fusion to snowdrop lectin magnifies the oral activity of insecticidal ω-hexatoxin-Hv1a peptide by enabling its delivery to the central nervous system. PLoS ONE 7(6):e39389
    • (2012) PLoS ONE , vol.7 , Issue.6 , pp. 39389
    • Fitches, E.C.1    Pyati, P.2    King, G.F.3    Gatehouse, J.A.4
  • 194
    • 32044468332 scopus 로고    scopus 로고
    • Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae)
    • 16206236 1:CAS:528:DC%2BD28Xht12qur8%3D 10.1002/ps.1119
    • Down RE, Fitches EC, Wiles DP, Corti P, Bell HA, Gatehouse JA, Edwards JP (2006) Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae). Pest Manag Sci 62(1):77-85
    • (2006) Pest Manag Sci , vol.62 , Issue.1 , pp. 77-85
    • Down, R.E.1    Fitches, E.C.2    Wiles, D.P.3    Corti, P.4    Bell, H.A.5    Gatehouse, J.A.6    Edwards, J.P.7
  • 195
    • 1642568734 scopus 로고    scopus 로고
    • Fusion proteins containing insect-specific toxins as pest control agents: Snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion
    • 15037094 1:CAS:528:DC%2BD2cXltVCrsg%3D%3D 10.1016/j.jinsphys.2003.09.010
    • Fitches E, Edwards M, Mee C, Grishin E, Gatehouse A, Edwards J, Gatehouse J (2004) Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion. J Insect Physiol 50:61-71
    • (2004) J Insect Physiol , vol.50 , pp. 61-71
    • Fitches, E.1    Edwards, M.2    Mee, C.3    Grishin, E.4    Gatehouse, A.5    Edwards, J.6    Gatehouse, J.7
  • 196
    • 0030018959 scopus 로고    scopus 로고
    • Development of recombinant baculoviruses for insect control
    • 8546446 1:CAS:528:DyaK28XksVyrtg%3D%3D 10.1146/annurev.en.41.010196. 001203
    • Bonning BC, Hammock BD (1996) Development of recombinant baculoviruses for insect control. Annu Rev Entomol 41:191-210
    • (1996) Annu Rev Entomol , vol.41 , pp. 191-210
    • Bonning, B.C.1    Hammock, B.D.2
  • 197
    • 36849024454 scopus 로고    scopus 로고
    • A scorpion neurotoxin increases the potency of a fungal insecticide
    • 17994009 1:CAS:528:DC%2BD2sXhsVSjurjP 10.1038/nbt1357
    • Wang C, St Leger RJ (2007) A scorpion neurotoxin increases the potency of a fungal insecticide. Nat Biotechnol 25(12):1455-1456
    • (2007) Nat Biotechnol , vol.25 , Issue.12 , pp. 1455-1456
    • Wang, C.1    St Leger, R.J.2
  • 198
    • 67349277601 scopus 로고    scopus 로고
    • Entomopathogenic fungi and their role in pest control
    • C. Kubicek I.S. Druzhinina (eds) 2 4 Springer Berlin
    • Charnley AK, Collins SA (2007) Entomopathogenic fungi and their role in pest control. In: Kubicek CP, Druzhinina IS (eds) The Mycota IV: environmental and microbial relationships, vol 4, 2nd edn. Springer, Berlin, pp 159-187
    • (2007) The Mycota IV: Environmental and Microbial Relationships , pp. 159-187
    • Charnley, A.K.1    Collins, S.A.2
  • 199
    • 79953737423 scopus 로고    scopus 로고
    • Insect-resistant biotech crops and their impacts on beneficial arthropods
    • 21444317 1:STN:280:DC%2BC3MzktFWmsg%3D%3D 10.1098/rstb.2010.0330
    • Gatehouse AM, Ferry N, Edwards MG, Bell HA (2011) Insect-resistant biotech crops and their impacts on beneficial arthropods. Philos Trans R Soc Lond B Biol Sci 366(1569):1438-1452
    • (2011) Philos Trans R Soc Lond B Biol Sci , vol.366 , Issue.1569 , pp. 1438-1452
    • Gatehouse, A.M.1    Ferry, N.2    Edwards, M.G.3    Bell, H.A.4
  • 200
    • 0030482539 scopus 로고    scopus 로고
    • Insect resistance of transformed tobacco plants with the gene of the spider insecticidal peptide
    • 1:CAS:528:DyaK28Xjtl2murw%3D
    • Jiang H, Zhu YX, Che ZL (1996) Insect resistance of transformed tobacco plants with the gene of the spider insecticidal peptide. J Integr Plant Biol (Acta Botan Sin) 38(2):95-99
    • (1996) J Integr Plant Biol (Acta Botan Sin) , vol.38 , Issue.2 , pp. 95-99
    • Jiang, H.1    Zhu, Y.X.2    Che, Z.L.3
  • 201
    • 84856823029 scopus 로고    scopus 로고
    • National Institute for Biotechnology and Genetic Engineering (NIBGE): Genetically modified spider cotton
    • 10.1177/097282011100900105
    • Omar A, Ali Chatha K (2012) National Institute for Biotechnology and Genetic Engineering (NIBGE): genetically modified spider cotton. Asian J Manag Cases 9:33-58
    • (2012) Asian J Manag Cases , vol.9 , pp. 33-58
    • Omar, A.1    Ali Chatha, K.2
  • 202
    • 33745122972 scopus 로고    scopus 로고
    • Spider venom toxin protects plants from insect attack
    • 16779650 1:CAS:528:DC%2BD28XlvVGrt70%3D 10.1007/s11248-006-0007-2
    • Khan SA, Zafar Y, Briddon RW, Malik KA, Mukhtar Z (2006) Spider venom toxin protects plants from insect attack. Transgenic Res 15(3):349-357
    • (2006) Transgenic Res , vol.15 , Issue.3 , pp. 349-357
    • Khan, S.A.1    Zafar, Y.2    Briddon, R.W.3    Malik, K.A.4    Mukhtar, Z.5
  • 203
    • 79551632702 scopus 로고    scopus 로고
    • Response of the gypsy moth, Lymantria dispar to transgenic poplar, Populus simonii × P. Nigra, expressing fusion protein gene of the spider insecticidal peptide and Bt-toxin C-peptide
    • 10.1673/031.010.20001
    • Cao C-W, Liu G-F, Wang Z-Y, Yan S-C, Ma L, Yang C-P (2010) Response of the gypsy moth, Lymantria dispar to transgenic poplar, Populus simonii × P. nigra, expressing fusion protein gene of the spider insecticidal peptide and Bt-toxin C-peptide. J Insect Sci 10(200):1-13
    • (2010) J Insect Sci , vol.10 , Issue.200 , pp. 1-13
    • Cao, C.-W.1    Liu, G.-F.2    Wang, Z.-Y.3    Yan, S.-C.4    Ma, L.5    Yang, C.-P.6
  • 204
    • 57849091267 scopus 로고    scopus 로고
    • Expression of a spider venom peptide in transgenic tobacco confers insect resistance
    • 19000914 10.1016/j.toxicon.2008.10.020 1:CAS:528:DC%2BD1cXhsFCjs7fE
    • Hernández-Campuzano B, Suárez R, Lina L, Hernández V, Villegas E, Corzo G, Iturriaga G (2009) Expression of a spider venom peptide in transgenic tobacco confers insect resistance. Toxicon 53(1):122-128
    • (2009) Toxicon , vol.53 , Issue.1 , pp. 122-128
    • Hernández-Campuzano, B.1    Suárez, R.2    Lina, L.3    Hernández, V.4    Villegas, E.5    Corzo, G.6    Iturriaga, G.7
  • 205
    • 33947390038 scopus 로고    scopus 로고
    • Mode of action of mosquitocidal Bacillus thuringiensis toxins
    • 17145072 1:CAS:528:DC%2BD2sXjtlyrurY%3D 10.1016/j.toxicon.2006.11.008
    • Soberon M, Fernandez LE, Perez C, Gill SS, Bravo A (2007) Mode of action of mosquitocidal Bacillus thuringiensis toxins. Toxicon 49:597-600
    • (2007) Toxicon , vol.49 , pp. 597-600
    • Soberon, M.1    Fernandez, L.E.2    Perez, C.3    Gill, S.S.4    Bravo, A.5
  • 206
    • 84866519244 scopus 로고    scopus 로고
    • Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes
    • 22842900 1:CAS:528:DC%2BC38XhtFWms73P 10.1038/nature11375
    • Baconguis I, Gouaux E (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature 489(7416):400-405
    • (2012) Nature , vol.489 , Issue.7416 , pp. 400-405
    • Baconguis, I.1    Gouaux, E.2
  • 208
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • 16612389 1:CAS:528:DC%2BD28XjsVWktbk%3D 10.1038/nature04649
    • Lange A, Giller K, Hornig S, Martin-Eauclaire MF, Pongs O, Becker S, Baldus M (2006) Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR. Nature 440(7086):959-962
    • (2006) Nature , vol.440 , Issue.7086 , pp. 959-962
    • Lange, A.1    Giller, K.2    Hornig, S.3    Martin-Eauclaire, M.F.4    Pongs, O.5    Becker, S.6    Baldus, M.7
  • 209
    • 18444411922 scopus 로고    scopus 로고
    • Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha- neurotoxins and nicotinic receptors
    • 15791209 1:CAS:528:DC%2BD2MXktFequro%3D 10.1038/sj.emboj.7600620
    • Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P (2005) Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha- neurotoxins and nicotinic receptors. EMBO J 24(8):1512-1522
    • (2005) EMBO J , vol.24 , Issue.8 , pp. 1512-1522
    • Bourne, Y.1    Talley, T.T.2    Hansen, S.B.3    Taylor, P.4    Marchot, P.5
  • 211
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution
    • 17643119 1:CAS:528:DC%2BD2sXotFykurc%3D 10.1038/nn1942
    • Dellisanti CD, Yao Y, Stroud JC, Wang ZZ, Chen L (2007) Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution. Nat Neurosci 10(8):953-962
    • (2007) Nat Neurosci , vol.10 , Issue.8 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.Z.4    Chen, L.5
  • 212
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • 11086218 1:CAS:528:DC%2BD3cXovFahtr0%3D 10.1016/S0300-9084(00)01174-3
    • Cestele S, Catterall WA (2000) Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie 82(9-10):883-892
    • (2000) Biochimie , vol.82 , Issue.9-10 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 213
    • 33847366129 scopus 로고    scopus 로고
    • The differential preference of scorpion α-toxins for insect or mammalian sodium channels: Implications for improved insect control
    • 17215013 1:CAS:528:DC%2BD2sXis1Cmsbk%3D 10.1016/j.toxicon.2006.11.016
    • Gordon D, Karbat I, Ilan N, Cohen L, Kahn R, Gilles N, Dong K, Stuhmer W, Tytgat J, Gurevitz M (2007) The differential preference of scorpion α-toxins for insect or mammalian sodium channels: implications for improved insect control. Toxicon 49(4):452-472
    • (2007) Toxicon , vol.49 , Issue.4 , pp. 452-472
    • Gordon, D.1    Karbat, I.2    Ilan, N.3    Cohen, L.4    Kahn, R.5    Gilles, N.6    Dong, K.7    Stuhmer, W.8    Tytgat, J.9    Gurevitz, M.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.