메뉴 건너뛰기




Volumn 11, Issue 7, 2013, Pages 2293-2313

Strategies for the development of conotoxins as new therapeutic leads

Author keywords

Cone snail; Ion channel; Pain; Peptide toxin; Peptidomimetic

Indexed keywords

2 AMINOBENZAMIDE; ALPHA CONOTOXIN IMI; ALPHA CONOTOXIN PNIA; ALPHA CONOTOXIN VC1.1; ANALGESIC AGENT; ARGININE; BENZAMIDE; BENZOTHIAZOLE; CALCIUM CHANNEL BLOCKING AGENT; CAV2.1 CHANNEL; CAV2.2 CHANNEL; CONOTOXIN; DIKETOPIPERAZINE CARBOXAMIDE; DIPHENYLMETHYLPIPERAZINE; DISULFIDE; GABAPENTIN; HISTIDINE; LEUCINE; LYSINE; MU CONOTOXIN BUIIIC; MU CONOTOXIN KIIIA; NP 180809; OMEGA CONOTOXIN GVIA; OMEGA CONOTOXIN MVIIA; PEPTIDOMIMETIC AGENT; PIPERAZINE DERIVATIVE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VOLTAGE GATED CALCIUM CHANNEL;

EID: 84880898626     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md11072293     Document Type: Review
Times cited : (26)

References (122)
  • 2
    • 0028864511 scopus 로고
    • Combinatorial peptide libraries in drug design-lessons from venomous cone snails
    • Olivera, B.M.; Hillyard, D.R.; Marsh, M.; Yoshikami, D. Combinatorial peptide libraries in drug design-Lessons from venomous cone snails. Trends Biotechnol. 1995, 13, 422-426.
    • (1995) Trends Biotechnol , vol.13 , pp. 422-426
    • Olivera, B.M.1    Hillyard, D.R.2    Marsh, M.3    Yoshikami, D.4
  • 3
    • 3042631514 scopus 로고    scopus 로고
    • Drugs from the sea: Conopeptides as potential therapeutics
    • Livett, B.G.; Gayler, K.R.; Khalil, Z. Drugs from the sea: Conopeptides as potential therapeutics. Curr. Med. Chem. 2004, 11, 1715-1723.
    • (2004) Curr. Med. Chem , vol.11 , pp. 1715-1723
    • Livett, B.G.1    Gayler, K.R.2    Khalil, Z.3
  • 4
    • 9144242506 scopus 로고    scopus 로고
    • Sodium channel toxins-receptor targeting and therapeutic potential
    • French, R.J.; Terlau, H. Sodium channel toxins-Receptor targeting and therapeutic potential. Curr. Med. Chem. 2004, 11, 3053-3064.
    • (2004) Curr. Med. Chem , vol.11 , pp. 3053-3064
    • French, R.J.1    Terlau, H.2
  • 5
    • 33751049816 scopus 로고    scopus 로고
    • Conotoxins down under
    • Norton, R.S.; Olivera, B.M. Conotoxins down under. Toxicon 2006, 48, 780-798.
    • (2006) Toxicon , vol.48 , pp. 780-798
    • Norton, R.S.1    Olivera, B.M.2
  • 7
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • Terlau, H.; Olivera, B.M. Conus venoms: A rich source of novel ion channel-targeted peptides. Physiol. Rev. 2004, 84, 41-68.
    • (2004) Physiol. Rev , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 8
    • 33646804559 scopus 로고    scopus 로고
    • Conotoxins: Therapeutic potential and application
    • Layer, R.T.; McIntosh, J.M. Conotoxins: Therapeutic potential and application. Mar. Drugs 2006, 4, 119-142.
    • (2006) Mar. Drugs , vol.4 , pp. 119-142
    • Layer, R.T.1    McIntosh, J.M.2
  • 9
    • 0035239229 scopus 로고    scopus 로고
    • Conotoxins, in retrospect
    • Olivera, B.M.; Cruz, L.J. Conotoxins, in retrospect. Toxicon 2001, 39, 7-14.
    • (2001) Toxicon , vol.39 , pp. 7-14
    • Olivera, B.M.1    Cruz, L.J.2
  • 10
    • 77951774753 scopus 로고    scopus 로고
    • Μ-Conotoxins as leads in the development of new analgesics
    • Norton, R.S. μ-Conotoxins as leads in the development of new analgesics. Molecules 2010, 15, 2825-2844.
    • (2010) Molecules , vol.15 , pp. 2825-2844
    • Norton, R.S.1
  • 11
    • 0041513435 scopus 로고    scopus 로고
    • Marine toxins as sources of drug leads
    • Alewood, P.; Hopping, G.; Armishaw, C. Marine toxins as sources of drug leads. Aust. J. Chem. 2003, 56, 769-774.
    • (2003) Aust. J. Chem , vol.56 , pp. 769-774
    • Alewood, P.1    Hopping, G.2    Armishaw, C.3
  • 12
    • 84862180786 scopus 로고    scopus 로고
    • Conoserver: Updated content, knowledge, and discovery tools in the conopeptide database
    • Kaas, Q.; Yu, R.L.; Jin, A.H.; Dutertre, S.; Craik, D.J. Conoserver: Updated content, knowledge, and discovery tools in the conopeptide database. Nucl. Acids. Res. 2012, 40, D325-D330.
    • (2012) Nucl. Acids. Res , vol.40
    • Kaas, Q.1    Yu, R.L.2    Jin, A.H.3    Dutertre, S.4    Craik, D.J.5
  • 13
    • 84865539150 scopus 로고    scopus 로고
    • Large-scale discovery of conopeptides and conoproteins in the injectable venom of a fish-hunting cone snail using a combined proteomic and transcriptomic approach
    • Violette, A.; Biass, D.; Dutertre, S.; Koua, D.; Piquemal, D.; Pierrat, F.; Stocklin, R.; Favreau, P. Large-Scale discovery of conopeptides and conoproteins in the injectable venom of a fish-hunting cone snail using a combined proteomic and transcriptomic approach. J. Proteomics 2012, 75, 5215-5225.
    • (2012) J. Proteomics , vol.75 , pp. 5215-5225
    • Violette, A.1    Biass, D.2    Dutertre, S.3    Koua, D.4    Piquemal, D.5    Pierrat, F.6    Stocklin, R.7    Favreau, P.8
  • 14
    • 84862756408 scopus 로고    scopus 로고
    • Elucidation of the molecular envenomation strategy of the cone snail conus geographus through transcriptome sequencing of its venom duct
    • Hu, H.; Bandyopadhyay, P.K.; Olivera, B.M.; Yandell, M. Elucidation of the molecular envenomation strategy of the cone snail Conus geographus through transcriptome sequencing of its venom duct. BMC Genomics 2012, 13, 284.
    • (2012) BMC Genomics , vol.13 , pp. 284
    • Hu, H.1    Bandyopadhyay, P.K.2    Olivera, B.M.3    Yandell, M.4
  • 17
    • 84952985593 scopus 로고    scopus 로고
    • Conopeptides as novel options for pain management
    • Daly, N.L.; Craik, D.J. Conopeptides as novel options for pain management. Drugs Future 2011, 36, 25-32.
    • (2011) Drugs Future , vol.36 , pp. 25-32
    • Daly, N.L.1    Craik, D.J.2
  • 18
    • 0031796866 scopus 로고    scopus 로고
    • Pharmacotherapeutic potential of ω-conotoxin mviia (snx-111), an n-type neuronal calcium channel blocker found in the venom of conus magus
    • Bowersox, S.S.; Luther, R. Pharmacotherapeutic potential of ω-conotoxin MVIIA (snx-111), an N-type neuronal calcium channel blocker found in the venom of Conus magus. Toxicon 1998, 36, 1651-1658.
    • (1998) Toxicon , vol.36 , pp. 1651-1658
    • Bowersox, S.S.1    Luther, R.2
  • 19
    • 9144272640 scopus 로고    scopus 로고
    • Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain
    • Miljanich, G.P. Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain. Curr. Med. Chem. 2004, 11, 3029-3040.
    • (2004) Curr. Med. Chem , vol.11 , pp. 3029-3040
    • Miljanich, G.P.1
  • 20
    • 33746872198 scopus 로고    scopus 로고
    • Novel delivery technologies for protein and peptide therapeutics
    • Kumar, T.R.S.; Soppimath, K.; Nachaegari, S.K. Novel delivery technologies for protein and peptide therapeutics. Curr. Pharm. Biotechnol. 2006, 7, 261-276.
    • (2006) Curr. Pharm. Biotechnol , vol.7 , pp. 261-276
    • Kumar, T.R.S.1    Soppimath, K.2    Nachaegari, S.K.3
  • 21
    • 22244488749 scopus 로고    scopus 로고
    • Oral delivery of peptide drugs-barriers and developments
    • Hamman, J.H.; Enslin, G.M.; Kotze, A.F. Oral delivery of peptide drugs-Barriers and developments. Biodrugs 2005, 19, 165-177.
    • (2005) Biodrugs , vol.19 , pp. 165-177
    • Hamman, J.H.1    Enslin, G.M.2    Kotze, A.F.3
  • 22
    • 0036257686 scopus 로고    scopus 로고
    • Converting a peptide into a drug: Strategies to improve stability and bioavailability
    • Adessi, C.; Soto, C. Converting a peptide into a drug: Strategies to improve stability and bioavailability. Curr. Med. Chem. 2002, 9, 963-978.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 963-978
    • Adessi, C.1    Soto, C.2
  • 24
    • 79951918591 scopus 로고    scopus 로고
    • Peptidomimetics: Modifying peptides in the pursuit of better vaccines
    • Croft, N.P.; Purcell, A.W. Peptidomimetics: Modifying peptides in the pursuit of better vaccines. Expert Rev. Vaccines 2011, 10, 211-226.
    • (2011) Expert Rev. Vaccines , vol.10 , pp. 211-226
    • Croft, N.P.1    Purcell, A.W.2
  • 25
    • 79952858926 scopus 로고    scopus 로고
    • Pyrrolinone-based peptidomimetics let the enzyme or receptor be the judge
    • Smith, A.B.; Charnley, A.K.; Hirschmann, R. Pyrrolinone-Based peptidomimetics. "Let the enzyme or receptor be the judge". Acc. Chem. Res. 2011, 44, 180-193.
    • (2011) Acc. Chem. Res , vol.44 , pp. 180-193
    • Smith, A.B.1    Charnley, A.K.2    Hirschmann, R.3
  • 26
    • 44949231073 scopus 로고    scopus 로고
    • Peptidomimetics, a synthetic tool of drug discovery
    • Vagner, J.; Qu, H.C.; Hruby, V.J. Peptidomimetics, a synthetic tool of drug discovery. Curr. Opin. Chem. Biol. 2008, 12, 292-296.
    • (2008) Curr. Opin. Chem. Biol , vol.12 , pp. 292-296
    • Vagner, J.1    Qu, H.C.2    Hruby, V.J.3
  • 27
    • 0033038675 scopus 로고    scopus 로고
    • Polypeptide ω-conotoxin gvia as a basis for new analgesic and neuroprotective agents
    • Norton, R.S.; Pallaghy, P.K.; Baell, J.B.; Wright, C.E.; Lew, M.J.; Angus, J.A. Polypeptide ω-conotoxin GVIA as a basis for new analgesic and neuroprotective agents. Drug Dev. Res. 1999, 46, 206-218.
    • (1999) Drug Dev. Res. , vol.46 , pp. 206-218
    • Norton, R.S.1    Pallaghy, P.K.2    Baell, J.B.3    Wright, C.E.4    Lew, M.J.5    Angus, J.A.6
  • 28
    • 52949117550 scopus 로고    scopus 로고
    • Peptides targeting voltage-gated calcium channels
    • Norton, R.S.; McDonough, S.I. Peptides targeting voltage-gated calcium channels. Curr. Pharm. Des. 2008, 14, 2480-2491.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 2480-2491
    • Norton, R.S.1    McDonough, S.I.2
  • 29
  • 32
    • 0034647768 scopus 로고    scopus 로고
    • Dendroid peptide structural mimetics of ω-conotoxin mviia based on a 2(1h)-quinolinone core
    • Guo, Z.X.; Cammidge, A.N.; Horwell, D.C. Dendroid peptide structural mimetics of ω-conotoxin MVIIA based on a 2(1H)-quinolinone core. Tetrahedron 2000, 56, 5169-5175.
    • (2000) Tetrahedron , vol.56 , pp. 5169-5175
    • Guo, Z.X.1    Cammidge, A.N.2    Horwell, D.C.3
  • 33
    • 0032497657 scopus 로고    scopus 로고
    • Synthesis of a non-peptide analogue of ω-conotoxin mviia
    • Menzler, S.; Bikker, J.A.; Horwell, D.C. Synthesis of a non-peptide analogue of ω-conotoxin MVIIA. Tetrahedron Lett. 1998, 39, 7619-7622.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 7619-7622
    • Menzler, S.1    Bikker, J.A.2    Horwell, D.C.3
  • 35
    • 0021749660 scopus 로고
    • Purification and sequence of a presynaptic peptide toxin from conus geographus venom
    • Olivera, B.M.; McIntosh, J.M.; Cruz, L.J.; Luque, F.A.; Gray, W.R. Purification and sequence of A presynaptic peptide toxin from Conus geographus venom. Biochemistry 1948, 23, 5087-5090.
    • (1948) Biochemistry , vol.23 , pp. 5087-5090
    • Olivera, B.M.1    McIntosh, J.M.2    Cruz, L.J.3    Luque, F.A.4    Gray, W.R.5
  • 36
    • 0030973424 scopus 로고    scopus 로고
    • Structure-function relationships of ω-conotoxin gvia-synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues
    • Lew, M.J.; Flinn, J.P.; Pallaghy, P.K.; Murphy, R.; Whorlow, S.L.; Wright, C.E.; Norton, R.S.; Angus, J.A. Structure-function relationships of ω-conotoxin GVIA-Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues. J. Biol. Chem. 1997, 272, 12014-12023.
    • (1997) J. Biol. Chem , vol.272 , pp. 12014-12023
    • Lew, M.J.1    Flinn, J.P.2    Pallaghy, P.K.3    Murphy, R.4    Whorlow, S.L.5    Wright, C.E.6    Norton, R.S.7    Angus, J.A.8
  • 37
    • 0033152766 scopus 로고    scopus 로고
    • Roles of key functional groups in ω-conotoxin gvia-synthesis, structure and functional assay of selected peptide analogues
    • Flinn, J.P.; Pallaghy, P.K.; Lew, M.J.; Murphy, R.; Angus, J.A.; Norton, R.S. Roles of key functional groups in ω-conotoxin GVIA-Synthesis, structure and functional assay of selected peptide analogues. Eur. J. Biochem. 1999, 262, 447-455.
    • (1999) Eur. J. Biochem , vol.262 , pp. 447-455
    • Flinn, J.P.1    Pallaghy, P.K.2    Lew, M.J.3    Murphy, R.4    Angus, J.A.5    Norton, R.S.6
  • 41
    • 33746893865 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of anthranilamide-based non-peptide mimetics of ω-conotoxin gvia
    • Baell, J.B.; Duggan, P.J.; Forsyth, S.A.; Lewis, R.J.; Lok, Y.P.; Schroeder, C.I.; Shepherd, N.E. Synthesis and biological evaluation of anthranilamide-based non-peptide mimetics of ω-conotoxin GVIA. Tetrahedron 2006, 62, 7284-7292.
    • (2006) Tetrahedron , vol.62 , pp. 7284-7292
    • Baell, J.B.1    Duggan, P.J.2    Forsyth, S.A.3    Lewis, R.J.4    Lok, Y.P.5    Schroeder, C.I.6    Shepherd, N.E.7
  • 42
    • 69249177513 scopus 로고    scopus 로고
    • Ω-Conotoxin gvia mimetics based on an anthranilamide core: Effect of variation in ammonium side chain lengths and incorporation of fluorine
    • Andersson, A.; Baell, J.B.; Duggan, P.J.; Graham, J.E.; Lewis, R.J.; Lumsden, N.G.; Tranberg, C.E.; Tuck, K.L.; Yang, A.J. ω-Conotoxin GVIA mimetics based on an anthranilamide core: Effect of variation in ammonium side chain lengths and incorporation of fluorine. Bioorg. Med. Chem. 2009, 17, 6659-6670.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 6659-6670
    • Andersson, A.1    Baell, J.B.2    Duggan, P.J.3    Graham, J.E.4    Lewis, R.J.5    Lumsden, N.G.6    Tranberg, C.E.7    Tuck, K.L.8    Yang, A.J.9
  • 43
    • 38349098208 scopus 로고    scopus 로고
    • Synthesis and ca(v)2.2 binding data for non-peptide mimetics of ω-conotoxin gvia based on a 5-Amino-Anthranilamide core
    • Duggan, P.J.; Faber, J.M.; Graham, J.E.; Lewis, R.J.; Lumsden, N.G.; Tuck, K.L. Synthesis and Ca(v)2.2 binding data for non-peptide mimetics of ω-conotoxin GVIA based on a 5-Amino-Anthranilamide core. Aust. J. Chem. 2008, 61, 11-15.
    • (2008) Aust. J. Chem , vol.61 , pp. 11-15
    • Duggan, P.J.1    Faber, J.M.2    Graham, J.E.3    Lewis, R.J.4    Lumsden, N.G.5    Tuck, K.L.6
  • 47
    • 84455208087 scopus 로고    scopus 로고
    • A-1048400 is a novel, orally active, state-dependent neuronal calcium channel blocker that produces dose-dependent antinociception without altering hemodynamic function in rats
    • Scott, V.E.; Vortherms, T.A.; Niforatos, W.; Swensen, A.M.; Neelands, T.; Milicic, I.; Banfor, P.N.; King, A.; Zhong, C.M.; Simler, G.; et al. A-1048400 is a novel, orally active, state-dependent neuronal calcium channel blocker that produces dose-dependent antinociception without altering hemodynamic function in rats. Biochem. Pharmacol. 2012, 83, 406-418.
    • (2012) Biochem. Pharmacol , vol.83 , pp. 406-418
    • Scott, V.E.1    Vortherms, T.A.2    Niforatos, W.3    Swensen, A.M.4    Neelands, T.5    Milicic, I.6    Banfor, P.N.7    King, A.8    Zhong, C.M.9    Simler, G.10
  • 50
    • 84870567345 scopus 로고    scopus 로고
    • Conotoxins targeting neuronal voltage-gated sodium channel subtypes: Potential analgesics?
    • Basel
    • Knapp, O.; McArthur, J.R.; Adams, D.J. Conotoxins targeting neuronal voltage-gated sodium channel subtypes: Potential analgesics? Toxins (Basel) 2012, 4, 1236-1260.
    • (2012) Toxins , vol.4 , pp. 1236-1260
    • Knapp, O.1    McArthur, J.R.2    Adams, D.J.3
  • 51
    • 35349024767 scopus 로고    scopus 로고
    • Structure/function characterization of μ-conotoxin kiiia, an analgesic, nearly irreversible blocker of mammalian neuronal sodium channels
    • Zhang, M.-M.; Green, B.R.; Catlin, P.; Fiedler, B.; Azam, L.; Chadwick, A.; Terlau, H.; McArthur, J.R.; French, R.J.; Gulyas, J.; et al. Structure/function characterization of μ-conotoxin KIIIA, an analgesic, nearly irreversible blocker of mammalian neuronal sodium channels. J. Biol. Chem. 2007, 282, 30699-30706.
    • (2007) J. Biol. Chem , vol.282 , pp. 30699-30706
    • Zhang, M.-M.1    Green, B.R.2    Catlin, P.3    Fiedler, B.4    Azam, L.5    Chadwick, A.6    Terlau, H.7    McArthur, J.R.8    French, R.J.9    Gulyas, J.10
  • 52
    • 80053200238 scopus 로고    scopus 로고
    • Interactions of key charged residues contributing to selective block of neuronal sodium channels by μ-conotoxin kiiia
    • McArthur, J.R.; Singh, G.; McMaster, D.; Winkfein, R.; Tieleman, D.P.; French, R.J. Interactions of key charged residues contributing to selective block of neuronal sodium channels by μ-conotoxin KIIIA. Mol. Pharmacol. 2011, 80, 573-584.
    • (2011) Mol. Pharmacol , vol.80 , pp. 573-584
    • McArthur, J.R.1    Singh, G.2    McMaster, D.3    Winkfein, R.4    Tieleman, D.P.5    French, R.J.6
  • 53
    • 64349101308 scopus 로고    scopus 로고
    • Structure of the analgesic μ-conotoxin kiiia and effects on the structure and function of disulfide deletion
    • Khoo, K.K.; Feng, Z.-P.; Smith, B.J.; Zhang, M.-M.; Yoshikami, D.; Olivera, B.M.; Bulaj, G.; Norton, R.S. Structure of the analgesic μ-conotoxin KIIIA and effects on the structure and function of disulfide deletion. Biochemistry 2009, 48, 1210-1219.
    • (2009) Biochemistry , vol.48 , pp. 1210-1219
    • Khoo, K.K.1    Feng, Z.-P.2    Smith, B.J.3    Zhang, M.-M.4    Yoshikami, D.5    Olivera, B.M.6    Bulaj, G.7    Norton, R.S.8
  • 56
    • 69549085003 scopus 로고    scopus 로고
    • Characterization of the two fundamental conformations of benzoylureas and elucidation of the factors that facilitate their conformational interchange
    • Lessene, G.; Smith, B.J.; Gable, R.W.; Baell, J.B. Characterization of the two fundamental conformations of benzoylureas and elucidation of the factors that facilitate their conformational interchange. J. Org. Chem. 2009, 74, 6511-6525.
    • (2009) J. Org. Chem , vol.74 , pp. 6511-6525
    • Lessene, G.1    Smith, B.J.2    Gable, R.W.3    Baell, J.B.4
  • 57
    • 0028142443 scopus 로고
    • The solution conformation of 1-(3, 5-dimethylphenyl)methyl-3 (s)-(1h-indol-3-yl)methyl-6(s)-phenylmethyl-2, 5-piperazinedione(1)-An nmr and molecular modeling study
    • Herbert, R.H.; Kelleher, F. The solution conformation of 1-(3, 5-dimethylphenyl)methyl-3 (S)-(1H-indol-3-yl)methyl-6(S)-phenylmethyl-2, 5-piperazinedione(1)-An NMR and molecular modeling study. Tetrahedron Lett. 1994, 35, 5497-5500.
    • (1994) Tetrahedron Lett , vol.35 , pp. 5497-5500
    • Herbert, R.H.1    Kelleher, F.2
  • 58
    • 0014214292 scopus 로고
    • Conformations of cyclic peptides. Folding of cyclic dipeptides containing an aromatic side chain
    • Kopple, K.D.; Marr, D.H. Conformations of cyclic peptides. Folding of cyclic dipeptides containing an aromatic side chain. J. Am. Chem. Soc. 1967, 89, 6193-6200.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 6193-6200
    • Kopple, K.D.1    Marr, D.H.2
  • 59
    • 0031189711 scopus 로고    scopus 로고
    • Molecular recognition of protein-ligand complexes: Applications to drug design
    • Babine, R.E.; Bender, S.L. Molecular recognition of protein-ligand complexes: Applications to drug design. Chem. Rev. 1997, 97, 1359-1472.
    • (1997) Chem. Rev. , vol.97 , pp. 1359-1472
    • Babine, R.E.1    Bender, S.L.2
  • 62
    • 0029085766 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine-receptor- identification of determinants of α-conotoxin m1 selectivity
    • Sine, S.M.; Kreienkamp, H.J.; Bren, N.; Maeda, R.; Taylor, P. Molecular dissection of subunit interfaces in the acetylcholine-receptor-Identification of determinants of α-conotoxin M1 selectivity. Neuron 1995, 15, 205-211.
    • (1995) Neuron , vol.15 , pp. 205-211
    • Sine, S.M.1    Kreienkamp, H.J.2    Bren, N.3    Maeda, R.4    Taylor, P.5
  • 63
    • 0030584684 scopus 로고    scopus 로고
    • The 1.1 angstrom crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin pnia from conus pennaceus
    • Hu, S.H.; Gehrmann, J.; Guddat, L.W.; Alewood, P.F.; Craik, D.J.; Martin, J.L. The 1.1 angstrom crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin PnIA from Conus pennaceus. Structure 1996, 4, 417-423.
    • (1996) Structure , vol.4 , pp. 417-423
    • Hu, S.H.1    Gehrmann, J.2    Guddat, L.W.3    Alewood, P.F.4    Craik, D.J.5    Martin, J.L.6
  • 64
    • 0031013481 scopus 로고    scopus 로고
    • Identification of high-potency neuropeptide y analogues through systematic lactamization
    • Kirby, D.A.; Britton, K.T.; Aubert, M.L.; Rivier, J.E. Identification of high-potency neuropeptide Y analogues through systematic lactamization. J. Med. Chem. 1997, 40, 210-215.
    • (1997) J. Med. Chem , vol.40 , pp. 210-215
    • Kirby, D.A.1    Britton, K.T.2    Aubert, M.L.3    Rivier, J.E.4
  • 65
    • 0037161579 scopus 로고    scopus 로고
    • Norton, r.s. Stabilization of the helical structure of y2-selective analogues of neuropeptide y by lactam bridges
    • Yao, S.G.; Smith-White, M.A.; Potter, E.K.; Norton, R.S. Stabilization of the helical structure of Y2-selective analogues of neuropeptide Y by lactam bridges. J. Med. Chem. 2002, 45, 2310-2318.
    • (2002) J. Med. Chem , vol.45 , pp. 2310-2318
    • Yao, S.G.1    Smith-White, M.A.2    Potter, E.K.3
  • 66
    • 1542285114 scopus 로고    scopus 로고
    • Synthesis and helical structure of lactam bridged bh3 peptides derived from pro-Apoptotic bcl-2 family proteins
    • Yang, B.; Liu, D.X.; Huang, Z.W. Synthesis and helical structure of lactam bridged BH3 peptides derived from pro-Apoptotic Bcl-2 family proteins. Bioorg. Med. Chem. Lett. 2004, 14, 1403-1406.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 1403-1406
    • Yang, B.1    Liu, D.X.2    Huang, Z.W.3
  • 67
    • 4544349166 scopus 로고    scopus 로고
    • Consecutive cyclic pentapeptide modules form short α-helices that are very stable to water and denaturants
    • Shepherd, N.E.; Abbenante, G.; Fairlie, D.P. Consecutive cyclic pentapeptide modules form short α-helices that are very stable to water and denaturants. Angew. Chem. Int. Ed. 2004, 43, 2687-2690.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 2687-2690
    • Shepherd, N.E.1    Abbenante, G.2    Fairlie, D.P.3
  • 68
    • 70350666479 scopus 로고    scopus 로고
    • Left- And right-handed α-helical turns in homo- And hetero-chiral helical scaffolds
    • Shepherd, N.E.; Hoang, H.N.; Abbenante, G.; Fairlie, D.P. Left- And right-handed α-helical turns in homo- And hetero-chiral helical scaffolds. J. Am. Chem. Soc. 2009, 131, 15877-15886.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15877-15886
    • Shepherd, N.E.1    Hoang, H.N.2    Abbenante, G.3    Fairlie, D.P.4
  • 69
  • 71
    • 77953262644 scopus 로고    scopus 로고
    • Μ-Conotoxin kiiia derivatives with divergent affinities versus efficacies in blocking voltage-gated sodium channels
    • Zhang, M.M.; Han, T.S.; Olivera, B.M.; Bulaj, G.; Yoshikami, D. μ-Conotoxin KIIIA derivatives with divergent affinities versus efficacies in blocking voltage-gated sodium channels. Biochemistry 2010, 49, 4804-4812.
    • (2010) Biochemistry , vol.49 , pp. 4804-4812
    • Zhang, M.M.1    Han, T.S.2    Olivera, B.M.3    Bulaj, G.4    Yoshikami, D.5
  • 74
    • 84870878146 scopus 로고    scopus 로고
    • Role of disulfide bonds in peptide and protein conformation
    • Wiley-VCH Verlag: Weinheim, Germany
    • Khoo, K.K.; Norton, R.S. Role of Disulfide Bonds in Peptide and Protein Conformation. In Amino Acids, Peptides and Proteins in Organic Chemistry; Wiley-VCH Verlag: Weinheim, Germany; Volume 5, pp. 395-417.
    • Amino Acids, Peptides and Proteins in Organic Chemistry , vol.5 , pp. 395-417
    • Khoo, K.K.1    Norton, R.S.2
  • 76
    • 33744918558 scopus 로고    scopus 로고
    • Α-Selenoconotoxins, a new class of potent α7 neuronal nicotinic receptor antagonists
    • Armishaw, C.J.; Daly, N.L.; Nevin, S.T.; Adams, D.J.; Craik, D.J.; Alewood, P.F. α-Selenoconotoxins, a new class of potent α7 neuronal nicotinic receptor antagonists. J. Biol. Chem. 2006, 281, 14136-14143.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14136-14143
    • Armishaw, C.J.1    Daly, N.L.2    Nevin, S.T.3    Adams, D.J.4    Craik, D.J.5    Alewood, P.F.6
  • 77
    • 0037900064 scopus 로고    scopus 로고
    • Synthesis of biologically active dicarba analogues of the peptide hormone oxytocin using ring-closing metathesis
    • Stymiest, J.L.; Mitchell, B.F.; Wong, S.; Vederas, J.C. Synthesis of biologically active dicarba analogues of the peptide hormone oxytocin using ring-closing metathesis. Org. Lett. 2003, 5, 47-49.
    • (2003) Org. Lett , vol.5 , pp. 47-49
    • Stymiest, J.L.1    Mitchell, B.F.2    Wong, S.3    Vederas, J.C.4
  • 78
    • 0037416471 scopus 로고    scopus 로고
    • Solid-phase synthesis and biological activity of a thioether analogue of conotoxin g1
    • Bondebjerg, J.; Grunnet, M.; Jespersen, T.; Meldal, M. Solid-Phase synthesis and biological activity of a thioether analogue of conotoxin G1. ChemBioChem 2003, 4, 186-194.
    • (2003) ChemBioChem , vol.4 , pp. 186-194
    • Bondebjerg, J.1    Grunnet, M.2    Jespersen, T.3    Meldal, M.4
  • 79
    • 1942502313 scopus 로고    scopus 로고
    • Thioether side chain cyclization for helical peptide formation: Inhibitors of estrogen receptor-coactivator interactions
    • Galande, A.K.; Bramlett, K.S.; Burris, T.P.; Wittliff, J.L.; Spatola, A.F. Thioether side chain cyclization for helical peptide formation: inhibitors of estrogen receptor-coactivator interactions. J. Peptide Res. 2004, 63, 297-302.
    • (2004) J. Peptide Res , vol.63 , pp. 297-302
    • Galande, A.K.1    Bramlett, K.S.2    Burris, T.P.3    Wittliff, J.L.4    Spatola, A.F.5
  • 81
  • 82
    • 79953211932 scopus 로고    scopus 로고
    • Ring-closing metathesis approaches for the solid-phase synthesis of cyclic peptoids
    • Khan, S.N.; Kim, A.; Grubbs, R.H.; Kwon, Y.U. Ring-Closing metathesis approaches for the solid-phase synthesis of cyclic peptoids. Org. Lett. 2011, 13, 1582-1585.
    • (2011) Org. Lett , vol.13 , pp. 1582-1585
    • Khan, S.N.1    Kim, A.2    Grubbs, R.H.3    Kwon, Y.U.4
  • 83
    • 0029860486 scopus 로고    scopus 로고
    • Application of ring-closing metathesis to the synthesis of rigidified amino acids and peptides
    • Miller, S.J.; Blackwell, H.E.; Grubbs, R.H. Application of ring-closing metathesis to the synthesis of rigidified amino acids and peptides. J. Am. Chem. Soc. 1996, 118, 9606-9614.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 9606-9614
    • Miller, S.J.1    Blackwell, H.E.2    Grubbs, R.H.3
  • 84
    • 0029033474 scopus 로고
    • Synthesis of conformationally restricted amino-Acids and peptides employing olefin metathesis
    • Miller, S.J.; Grubbs, R.H. Synthesis of conformationally restricted amino-Acids and peptides employing olefin metathesis. J. Am. Chem. Soc. 1995, 117, 5855-5856.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 5855-5856
    • Miller, S.J.1    Grubbs, R.H.2
  • 86
    • 67650448251 scopus 로고    scopus 로고
    • Regioselective formation of interlocked dicarba bridges in naturally occurring cyclic peptide toxins using olefin metathesis
    • Robinson, A.J.; van Lierop, B.J.; Garland, R.D.; Teoh, E.; Elaridi, J.; Illesinghe, J.P.; Jackson, W.R. Regioselective formation of interlocked dicarba bridges in naturally occurring cyclic peptide toxins using olefin metathesis. Chem. Commun. 2009, 28, 4293-4295.
    • (2009) Chem. Commun. , vol.28 , pp. 4293-4295
    • Robinson, A.J.1    Van Lierop, B.J.2    Garland, R.D.3    Teoh, E.4    Elaridi, J.5    Illesinghe, J.P.6    Jackson, W.R.7
  • 87
    • 79960087188 scopus 로고    scopus 로고
    • Ring-closing metathesis in peptides-the sting is in the tail! aust
    • Van Lierop, B.J.; Bornschein, C.; Jackson, W.R.; Robinson, A.J. Ring-closing metathesis in peptides-The sting is in the tail! Aust. J. Chem. 2011, 64, 806-811.
    • (2011) J. Chem , vol.64 , pp. 806-811
    • Van Lierop, B.J.1    Bornschein, C.2    Jackson, W.R.3    Robinson, A.J.4
  • 88
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 1981, 34, 167-339.
    • (1981) Adv. Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 89
    • 0014680538 scopus 로고
    • Synthesis of a biologically active analog of deamino-8-Arginine- vasopressin which does not contain a disulfide bond
    • Hase, S.; Morikawa, T.; Sakakiba, S. Synthesis of A biologically active analog of deamino-8-Arginine-vasopressin which does not contain a disulfide bond. Experientia 1969, 25, 1239-1240.
    • (1969) Experientia , vol.25 , pp. 1239-1240
    • Hase, S.1    Morikawa, T.2    Sakakiba, S.3
  • 90
    • 0024536412 scopus 로고
    • A dicarba analog of β-Atrial natriuretic peptide (β-Anp) inhibits guanosine 3′, 5′-cyclic-monophosphate production induced by α-Anp in cultured rat vascular smooth-muscle cells
    • Kambayashi, Y.; Nakajima, S.; Ueda, M.; Inouye, K. A dicarba analog of β-Atrial natriuretic peptide (β-Anp) inhibits guanosine 3′, 5′-cyclic-monophosphate production induced by α-Anp in cultured rat vascular smooth-muscle cells. FEBS Lett. 1989, 248, 28-34.
    • (1989) FEBS Lett. , vol.248 , pp. 28-34
    • Kambayashi, Y.1    Nakajima, S.2    Ueda, M.3    Inouye, K.4
  • 91
    • 0016812494 scopus 로고
    • Studies on pharmacological and biochemical properties of deamino-dicarba-[gly7]-oxytocin (y-5350)
    • Oka, T.; Nakanishi, A.; Okada, T. Studies on pharmacological and biochemical properties of deamino-dicarba-[Gly7]-oxytocin (Y-5350). Jpn. J. Pharmacol. 1975, 25, 15-24.
    • (1975) Jpn. J. Pharmacol , vol.25 , pp. 15-24
    • Oka, T.1    Nakanishi, A.2    Okada, T.3
  • 92
    • 25444514293 scopus 로고    scopus 로고
    • Synthesis of oxytocin analogues with replacement of sulfur by carbon gives potent antagonists with increased stability
    • Stymiest, J.L.; Mitchell, B.F.; Wong, S.; Vederas, J.C. Synthesis of oxytocin analogues with replacement of sulfur by carbon gives potent antagonists with increased stability. J. Org. Chem. 2005, 70, 7799-7809.
    • (2005) J. Org. Chem , vol.70 , pp. 7799-7809
    • Stymiest, J.L.1    Mitchell, B.F.2    Wong, S.3    Vederas, J.C.4
  • 96
    • 84880867759 scopus 로고    scopus 로고
    • Monash University, Clayton 3800, Australia. Personal communication
    • Robinson, A.J. Monash University, Clayton 3800, Australia. Personal communication, 2013.
    • (2013)
    • Robinson, A.J.1
  • 98
    • 80053469174 scopus 로고    scopus 로고
    • Α-Conotoxin imi incorporating stable cystathionine bridges maintains full potency and identical three-dimensional structure
    • Dekan, Z.; Vetter, I.; Daly, N.L.; Craik, D.J.; Lewis, R.J.; Alewood, P.F. α-Conotoxin ImI incorporating stable cystathionine bridges maintains full potency and identical three-dimensional structure. J. Am. Chem. Soc. 2011, 133, 15866-15869.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15866-15869
    • Dekan, Z.1    Vetter, I.2    Daly, N.L.3    Craik, D.J.4    Lewis, R.J.5    Alewood, P.F.6
  • 99
    • 84875138812 scopus 로고    scopus 로고
    • Getting in shape: Controlling peptide bioactivity and bioavailability using conformational constraints
    • Bock, J.E.; Gavenonis, J.; Kritzer, J.A. Getting in shape: Controlling peptide bioactivity and bioavailability using conformational constraints. ACS Chem. Biol. 2013, 8, 488-499.
    • (2013) ACS Chem. Biol , Issue.8 , pp. 488-499
    • Bock, J.E.1    Gavenonis, J.2    Kritzer, J.A.3
  • 100
    • 29744469461 scopus 로고    scopus 로고
    • Strategies to improve stability and bioavailability of peptide drugs
    • Adessi, C.; Soto, C. Strategies to improve stability and bioavailability of peptide drugs. Front. Med. Chem.Online 2004, 1, 513-528.
    • (2004) Front. Med. Chem.Online , vol.1 , pp. 513-528
    • Adessi, C.1    Soto, C.2
  • 101
    • 34548643963 scopus 로고    scopus 로고
    • Chemical modification of conotoxins to improve stability and activity
    • Craik, D.J.; Adams, D.J. Chemical modification of conotoxins to improve stability and activity. ACS Chem. Biol. 2007, 2, 457-468.
    • (2007) ACS Chem. Biol , vol.2 , pp. 457-468
    • Craik, D.J.1    Adams, D.J.2
  • 102
    • 0034885143 scopus 로고    scopus 로고
    • Vancomycin, teicoplanin, and ramoplanin: Synthetic and mechanistic studies
    • Boger, D.L. Vancomycin, teicoplanin, and ramoplanin: Synthetic and mechanistic studies. Med. Res. Rev. 2001, 21, 356-381.
    • (2001) Med. Res. Rev , vol.21 , pp. 356-381
    • Boger, D.L.1
  • 104
    • 0025890947 scopus 로고
    • Mechanism of action of cyclosporine-A and rationale for use in nephrotic syndrome
    • Borel, J.F. Mechanism of action of cyclosporine-A and rationale for use in nephrotic syndrome. Clin. Nephrol. 1991, 35, S23-S30.
    • (1991) Clin. Nephrol , vol.35
    • Borel, J.F.1
  • 105
    • 84859000598 scopus 로고    scopus 로고
    • Basic research: An oral cyclic peptide drug to reverse kidney fibrosis?
    • Allison, S.J. Basic research: An oral cyclic peptide drug to reverse kidney fibrosis? Nat. Rev. Nephrol. 2012, 8, 193-193.
    • (2012) Nat. Rev. Nephrol , vol.8 , pp. 193-193
    • Allison, S.J.1
  • 106
    • 84857048280 scopus 로고    scopus 로고
    • Cyclization of conotoxins to improve their biopharmaceutical properties
    • Clark, R.J.; Akcan, M.; Kaas, Q.; Daly, N.L.; Craik, D.J. Cyclization of conotoxins to improve their biopharmaceutical properties. Toxicon 2012, 59, 446-455.
    • (2012) Toxicon , vol.59 , pp. 446-455
    • Clark, R.J.1    Akcan, M.2    Kaas, Q.3    Daly, N.L.4    Craik, D.J.5
  • 107
    • 77956502216 scopus 로고    scopus 로고
    • The engineering of an orally active conotoxin for the treatment of neuropathic pain. Angew
    • Clark, R.J.; Jensen, J.; Nevin, S.T.; Callaghan, B.P.; Adams, D.J.; Craik, D.J. The engineering of an orally active conotoxin for the treatment of neuropathic pain. Angew. Chem. Int. Ed. 2010, 49, 6545-6548.
    • (2010) Chem. Int. Ed , vol.49 , pp. 6545-6548
    • Clark, R.J.1    Jensen, J.2    Nevin, S.T.3    Callaghan, B.P.4    Adams, D.J.5    Craik, D.J.6
  • 108
    • 33747372837 scopus 로고    scopus 로고
    • The synthesis, structural characterization, and receptor specificity of the α-conotoxin vc1.1
    • Clark, R.J.; Fischer, H.; Nevin, S.T.; Adams, D.J.; Craik, D.J. The synthesis, structural characterization, and receptor specificity of the α-conotoxin Vc1.1. J. Biol. Chem. 2006, 281, 23254-23263.
    • (2006) J. Biol. Chem , vol.281 , pp. 23254-23263
    • Clark, R.J.1    Fischer, H.2    Nevin, S.T.3    Adams, D.J.4    Craik, D.J.5
  • 109
    • 26844476004 scopus 로고    scopus 로고
    • Α-Conotoxin vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones
    • Satkunanathan, N.; Livett, B.; Gayler, K.; Sandall, D.; Down, J.; Khalil, Z. α-Conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones. Brain Res. 2005, 1059, 149-158.
    • (2005) Brain Res. , vol.1059 , pp. 149-158
    • Satkunanathan, N.1    Livett, B.2    Gayler, K.3    Sandall, D.4    Down, J.5    Khalil, Z.6
  • 110
    • 33845212316 scopus 로고    scopus 로고
    • Molecular mechanism for analgesia involving specific antagonism of α9, α10 nicotinic acetylcholine receptors
    • Vincler, M.; Wittenauer, S.; Parker, R.; Ellison, M.; Olivera, B.M.; McIntosh, J.M. Molecular mechanism for analgesia involving specific antagonism of α9, α10 nicotinic acetylcholine receptors. Proc. Natl. Acad. Sci. USA 2006, 103, 17880-17884.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17880-17884
    • Vincler, M.1    Wittenauer, S.2    Parker, R.3    Ellison, M.4    Olivera, B.M.5    McIntosh, J.M.6
  • 111
    • 34447321825 scopus 로고    scopus 로고
    • Targeting the α9, α10 nicotinic acetylcholine receptor to treat severe pain
    • Vincler, M.; McIntosh, J.M. Targeting the α9, α10 nicotinic acetylcholine receptor to treat severe pain. Expert Opin. Ther. 2007, 11, 891-897.
    • (2007) Expert Opin. Ther. , vol.11 , pp. 891-897
    • Vincler, M.1    McIntosh, J.M.2
  • 112
    • 58149172098 scopus 로고    scopus 로고
    • Analgesic α-conotoxins vc1.1 and rgia inhibit n-type calcium channels in rat sensory neurons via gabab receptor activation
    • Callaghan, B.; Haythornthwaite, A.; Berecki, G.; Clark, R.J.; Craik, D.J.; Adams, D.J. Analgesic α-conotoxins Vc1.1 and RgIA inhibit N-type calcium channels in rat sensory neurons via GABAB receptor activation. J. Neurosci. 2008, 28, 10943-10951.
    • (2008) J. Neurosci , vol.28 , pp. 10943-10951
    • Callaghan, B.1    Haythornthwaite, A.2    Berecki, G.3    Clark, R.J.4    Craik, D.J.5    Adams, D.J.6
  • 113
    • 75749113276 scopus 로고    scopus 로고
    • Analgesic α-conotoxins vc1.1 and rgia inhibit n-type calcium channels in sensory neurons of α9 nicotinic receptor knockout mice
    • Austin
    • Callaghan, B.; Adams, D.J. Analgesic α-conotoxins Vc1.1 and RgIA inhibit N-type calcium channels in sensory neurons of α9 nicotinic receptor knockout mice. Channels (Austin) 2010, 4, 51-54.
    • (2010) Channels , vol.4 , pp. 51-54
    • Callaghan, B.1    Adams, D.J.2
  • 114
    • 84863632507 scopus 로고    scopus 로고
    • Γ-Aminobutyric acid type b (gabab) receptor expression is needed for inhibition of n-type (cav2.2) calcium channels by analgesic α-conotoxins
    • Cuny, H.; de Faoite, A.; Huynh, T.G.; Yasuda, T.; Berecki, G.; Adams, D.J. γ-Aminobutyric acid type B (GABAB) receptor expression is needed for inhibition of N-type (Cav2.2) calcium channels by analgesic α-conotoxins. J. Biol. Chem. 2012, 287, 23948-23957.
    • (2012) J. Biol. Chem , vol.287 , pp. 23948-23957
    • Cuny, H.1    De Faoite, A.2    Huynh, T.G.3    Yasuda, T.4    Berecki, G.5    Adams, D.J.6
  • 116
    • 26944452043 scopus 로고    scopus 로고
    • Pegylation, successful approach to drug delivery
    • Veronese, F.M.; Pasut, G. PEGylation, successful approach to drug delivery. Drug Discov. Today 2005, 10, 1451-1458.
    • (2005) Drug Discov. Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 117
    • 0034806376 scopus 로고    scopus 로고
    • Insertion of an n-terminal 6-Aminohexanoic acid after the 7 amino acid position of glucagon-like peptide-1 produces a long-Acting hypoglycemic agent
    • Doyle, M.E.; Greig, N.H.; Holloway, H.W.; Betkey, J.A.; Bernier, M.; Egan, J.M. Insertion of an N-terminal 6-Aminohexanoic acid after the 7 amino acid position of glucagon-like peptide-1 produces a long-Acting hypoglycemic agent. Endocrinology 2001, 142, 4462-4468.
    • (2001) Endocrinology , vol.142 , pp. 4462-4468
    • Doyle, M.E.1    Greig, N.H.2    Holloway, H.W.3    Betkey, J.A.4    Bernier, M.5    Egan, J.M.6
  • 119
    • 0029361837 scopus 로고
    • A rational approach for the development of reduced-size analogues of neuropeptide y with high affinity to the y-1 receptor
    • Rist, B.; Wieland, H.A.; Willim, K.D.; Beck-Sickinger, A.G. A rational approach for the development of reduced-size analogues of neuropeptide Y with high affinity to the Y-1 receptor. J. Peptide Sci. 1995, 1, 341-348.
    • (1995) J. Peptide Sci , vol.1 , pp. 341-348
    • Rist, B.1    Wieland, H.A.2    Willim, K.D.3    Beck-Sickinger, A.G.4
  • 120
    • 29944442294 scopus 로고    scopus 로고
    • A novel conotoxin from conus striatus, μ-siiia, selectively blocking rat tetrodotoxin-resistant sodium channels
    • Wang, C.Z.; Zhang, H.; Jiang, H.; Lu, W.Y.; Zhao, Z.Q.; Chi, C.W. A novel conotoxin from Conus striatus, μ-SIIIA, selectively blocking rat tetrodotoxin-resistant sodium channels. Toxicon 2006, 47, 122-132.
    • (2006) Toxicon , vol.47 , pp. 122-132
    • Wang, C.Z.1    Zhang, H.2    Jiang, H.3    Lu, W.Y.4    Zhao, Z.Q.5    Chi, C.W.6
  • 121
    • 0023223448 scopus 로고
    • The formalin test in mice-dissociation between inflammatory and noninflammatory pain
    • Hunskaar, S.; Hole, K. The formalin test in mice-Dissociation between inflammatory and noninflammatory pain. Pain 1987, 30, 103-114.
    • (1987) Pain , vol.30 , pp. 103-114
    • Hunskaar, S.1    Hole, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.