메뉴 건너뛰기




Volumn 2, Issue 7, 2007, Pages 457-468

Chemical modification of conotoxins to improve stability and activity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CONOTOXIN AULB; ALPHA CONOTOXIN GID; ALPHA CONOTOXIN LML; ALPHA CONOTOXIN MII; ALPHA CONOTOXIN SI; ALPHA CONOTOXIN VC1.1; AM 336; CALCIUM CHANNEL N TYPE; CGX 1160; CONANTOKIN G; CONOTOXIN; CONTULAKIN G; CYCLOSPORIN; MARINE TOXIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; NEUROTENSIN RECEPTOR; NICOTINIC RECEPTOR; NORADRENALIN TRANSPORTER; OMEGA CONOTOXIN; OMEGA CONOTOXIN CVID; OMEGA CONOTOXIN MVIIA; POTASSIUM CHANNEL; SEROTONIN 3 RECEPTOR; SODIUM CHANNEL; UNCLASSIFIED DRUG; VASOPRESSIN RECEPTOR; X CONOTOXIN MRLA; XEN 2174; DISULFIDE;

EID: 34548643963     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb700091j     Document Type: Review
Times cited : (95)

References (100)
  • 1
    • 0001021863 scopus 로고
    • Conus peptides as chemical probes for receptors and ion channels
    • Myers, R. A., Cruz, L. J., and Olivera, B. M. (1993) Conus peptides as chemical probes for receptors and ion channels, Chem. Rev. 93, 1923-1936.
    • (1993) Chem. Rev , vol.93 , pp. 1923-1936
    • Myers, R.A.1    Cruz, L.J.2    Olivera, B.M.3
  • 3
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis, R. J., and Garcia, M. L. (2003) Therapeutic potential of venom peptides, Nat. Rev. Drug Discovery 2, 790-802.
    • (2003) Nat. Rev. Drug Discovery , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 4
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • Terlau, H., and Olivera, B. M. (2004) Conus venoms: a rich source of novel ion channel-targeted peptides, Physiol. Rev. 84, 41-68.
    • (2004) Physiol. Rev , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 5
    • 9144272640 scopus 로고    scopus 로고
    • Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain
    • Miljanich, G. P. (2004) Ziconotide: neuronal calcium channel blocker for treating severe chronic pain, Curr. Med. Chem. 11, 3029-3040.
    • (2004) Curr. Med. Chem , vol.11 , pp. 3029-3040
    • Miljanich, G.P.1
  • 6
    • 33749645832 scopus 로고    scopus 로고
    • Ziconotide - a novel neuron-specific calcium channel blocker for the intrathecal treatment of severe chronic pain - a short review
    • Klotz, U. (2006) Ziconotide - a novel neuron-specific calcium channel blocker for the intrathecal treatment of severe chronic pain - a short review, Int. J. Clin. Pharmocol. Ther. 44, 478-483.
    • (2006) Int. J. Clin. Pharmocol. Ther , vol.44 , pp. 478-483
    • Klotz, U.1
  • 7
    • 0042230657 scopus 로고    scopus 로고
    • Conopeptides: Unique pharmacological agents that challenge current peptide methodologies
    • Mari, F., and Fields, G. B. (2003) Conopeptides: unique pharmacological agents that challenge current peptide methodologies, Chim. Oggi 43-48.
    • (2003) Chim. Oggi , pp. 43-48
    • Mari, F.1    Fields, G.B.2
  • 8
    • 29344443859 scopus 로고    scopus 로고
    • Conotoxins and the posttranslational modification of secreted gene products
    • Buczek, O., Bulaj, G., and Olivera, B. M. (2005) Conotoxins and the posttranslational modification of secreted gene products, Cell. Mol. Life Sci. 62, 3067-3079.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 3067-3079
    • Buczek, O.1    Bulaj, G.2    Olivera, B.M.3
  • 9
    • 0034013024 scopus 로고    scopus 로고
    • Bioavailability of ziconotide in brain: Influx from blood, stability, and diffusion
    • Newcomb, R., Abbruscato, T. J. Singh, T., Nadasdi, L., Davis, T. P., and Miljanich, G. (2000) Bioavailability of ziconotide in brain: influx from blood, stability, and diffusion, Peptides 21, 491-501.
    • (2000) Peptides , vol.21 , pp. 491-501
    • Newcomb, R.1    Abbruscato, T.J.2    Singh, T.3    Nadasdi, L.4    Davis, T.P.5    Miljanich, G.6
  • 11
    • 0035033785 scopus 로고    scopus 로고
    • α-Conotoxins: Nicotinic acetylcholine receptor antagonists as pharmacological tools and potential drug leads
    • Dutton, J. L., and Craik, D. J. (2001) α-Conotoxins: nicotinic acetylcholine receptor antagonists as pharmacological tools and potential drug leads, Curr. Med. Chem. 8, 327-344.
    • (2001) Curr. Med. Chem , vol.8 , pp. 327-344
    • Dutton, J.L.1    Craik, D.J.2
  • 12
    • 3042631514 scopus 로고    scopus 로고
    • Drugs from the sea: Conopeptides as potential therapeutics
    • Livett, B. G., Gayler, K. R., and Khalil, Z. (2004) Drugs from the sea: conopeptides as potential therapeutics, Curr. Med. Chem. 11, 1715-1723.
    • (2004) Curr. Med. Chem , vol.11 , pp. 1715-1723
    • Livett, B.G.1    Gayler, K.R.2    Khalil, Z.3
  • 13
    • 3442894756 scopus 로고    scopus 로고
    • Conotoxins and structural biology: A prospective paradigm for drug discovery
    • Grant, M. A., Morelli, X. J., and Rigby, A. C. (2004) Conotoxins and structural biology: a prospective paradigm for drug discovery, Curr. Protein Pept. Sci. 5, 235-248.
    • (2004) Curr. Protein Pept. Sci , vol.5 , pp. 235-248
    • Grant, M.A.1    Morelli, X.J.2    Rigby, A.C.3
  • 14
    • 33750957742 scopus 로고    scopus 로고
    • Therapeutic applications of conotoxins that target the neuronal nicotinic acetylcholine receptor
    • Livett, B. G., Sandall, D. W., Keays, D., Down, J., Gayler, K. R., Satkunanathan, N., and Khalil, Z. (2006) Therapeutic applications of conotoxins that target the neuronal nicotinic acetylcholine receptor, Toxicon 48, 810-829.
    • (2006) Toxicon , vol.48 , pp. 810-829
    • Livett, B.G.1    Sandall, D.W.2    Keays, D.3    Down, J.4    Gayler, K.R.5    Satkunanathan, N.6    Khalil, Z.7
  • 15
    • 33751049816 scopus 로고    scopus 로고
    • Conotoxins down under
    • Norton, R. S., and Olivera, B. M. (2006) Conotoxins down under, Toxicon 48, 780-798.
    • (2006) Toxicon , vol.48 , pp. 780-798
    • Norton, R.S.1    Olivera, B.M.2
  • 16
    • 34250017052 scopus 로고    scopus 로고
    • Conotoxins of the O-superfamily affecting voltage-gated sodium channels
    • Heinemann, S. H., and Leipold, E. (2007) Conotoxins of the O-superfamily affecting voltage-gated sodium channels, Cell. Mol. Life Sci. 64, 1329-1340.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 1329-1340
    • Heinemann, S.H.1    Leipold, E.2
  • 18
    • 0042290798 scopus 로고    scopus 로고
    • Applications of NMR in drug design: Structure-activity relationships in disulfide-rich peptides
    • Craik, D. J. (1999) Applications of NMR in drug design: structure-activity relationships in disulfide-rich peptides, Protein Pept. Lett. 6, 341-350.
    • (1999) Protein Pept. Lett , vol.6 , pp. 341-350
    • Craik, D.J.1
  • 19
    • 0028984720 scopus 로고
    • Solution structure of omega-conotoxin MVIIA using 2D NMR spectroscopy
    • Basus, V. J., Nadasdi, L., Ramachandran, J., and Miljanich, G. P. (1995) Solution structure of omega-conotoxin MVIIA using 2D NMR spectroscopy, FEBS Lett. 370, 163-169.
    • (1995) FEBS Lett , vol.370 , pp. 163-169
    • Basus, V.J.1    Nadasdi, L.2    Ramachandran, J.3    Miljanich, G.P.4
  • 20
    • 0030601856 scopus 로고    scopus 로고
    • A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: Comparison of MVIIA, SVIB and SNX-202
    • Nielsen, K. J., Thomas, L., Lewis, R. J., Alewood, P. F., and Craik, D. J. (1996) A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202, J. Mol. Biol. 263, 297-310.
    • (1996) J. Mol. Biol , vol.263 , pp. 297-310
    • Nielsen, K.J.1    Thomas, L.2    Lewis, R.J.3    Alewood, P.F.4    Craik, D.J.5
  • 21
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik, D. J., Daly, N. L., and Waine, C. (2001) The cystine knot motif in toxins and implications for drug design, Toxicon 39, 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 22
    • 0033198875 scopus 로고    scopus 로고
    • Post-translationally modified neuropeptides from Conus venoms
    • Craig, A. G., Bandyopadhyay, P., and Olivera, B. M. (1999) Post-translationally modified neuropeptides from Conus venoms, Eur. J. Biochem. 264, 271-275.
    • (1999) Eur. J. Biochem , vol.264 , pp. 271-275
    • Craig, A.G.1    Bandyopadhyay, P.2    Olivera, B.M.3
  • 23
    • 33746256601 scopus 로고    scopus 로고
    • NMR of conotoxins: Structural features and an analysis of chemical shifts of post-translationally modified amino acids
    • Marx, U. C., Daly, N. L., and Craik, D. J. (2006) NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids, Magn. Reson. Chem. 44, S41-550.
    • (2006) Magn. Reson. Chem , vol.44
    • Marx, U.C.1    Daly, N.L.2    Craik, D.J.3
  • 24
    • 29844433234 scopus 로고    scopus 로고
    • Overview of molecular relationships in the voltage-gated ion channel superfamily
    • Yu, F. H., Yarov-Yarovoy, V., Gutman, G. A., and Catterall, W. A. (2005) Overview of molecular relationships in the voltage-gated ion channel superfamily, Pharmacol. Rev. 57, 387-395.
    • (2005) Pharmacol. Rev , vol.57 , pp. 387-395
    • Yu, F.H.1    Yarov-Yarovoy, V.2    Gutman, G.A.3    Catterall, W.A.4
  • 25
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA
    • Scanlon, M. J., Naranjo, D., Thomas, L., Alewood, P. F., Lewis, R. J., and Craik, D. J. (1997) Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA, Structure 5, 1585-1597.
    • (1997) Structure , vol.5 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5    Craik, D.J.6
  • 31
    • 3042607961 scopus 로고    scopus 로고
    • The Cys-loop superfamily of ligand-gated ion channels: The impact of receptor structure on function
    • Connolly, C. N., and Wafford, K. A. (2004) The Cys-loop superfamily of ligand-gated ion channels: the impact of receptor structure on function, Biochem. Soc. Trans. 32, 529-534.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 529-534
    • Connolly, C.N.1    Wafford, K.A.2
  • 32
    • 3042786368 scopus 로고    scopus 로고
    • Molecular biology and ontogeny of glutamate receptors in the mammalian central nervous system
    • Simeone, T. A., Sanchez, R. M., and Rho, J. M. (2004) Molecular biology and ontogeny of glutamate receptors in the mammalian central nervous system, J. Child Neurol. 19, 343-360.
    • (2004) J. Child Neurol , vol.19 , pp. 343-360
    • Simeone, T.A.1    Sanchez, R.M.2    Rho, J.M.3
  • 33
    • 33645106684 scopus 로고    scopus 로고
    • Historical review: ATP as a neurotransmitter
    • Burnstock, G. (2006) Historical review: ATP as a neurotransmitter, Trends Pharmacol. Sci. 27, 166-176.
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 166-176
    • Burnstock, G.1
  • 35
    • 0038010721 scopus 로고    scopus 로고
    • Characterization and three-dimensional structure determination of psi-conotoxin Piiif, a novel noncompetitive antagonist of nicotinic acetylcholine receptors
    • Van Wagoner, R. M., Jacobsen, R. B., Olivera, B. M., and Ireland, C. M. (2003) Characterization and three-dimensional structure determination of psi-conotoxin Piiif, a novel noncompetitive antagonist of nicotinic acetylcholine receptors, Biochemistry 42, 6353-6362.
    • (2003) Biochemistry , vol.42 , pp. 6353-6362
    • Van Wagoner, R.M.1    Jacobsen, R.B.2    Olivera, B.M.3    Ireland, C.M.4
  • 36
    • 33747188678 scopus 로고    scopus 로고
    • Toxin insights into nicotinic acetylcholine receptors
    • Dutertre, S., and Lewis, R. J. (2006) Toxin insights into nicotinic acetylcholine receptors, Biochem. Pharmacol. 72, 661-670.
    • (2006) Biochem. Pharmacol , vol.72 , pp. 661-670
    • Dutertre, S.1    Lewis, R.J.2
  • 37
    • 0037072765 scopus 로고    scopus 로고
    • Alpha-conotoxin GIC from Conus geographus, a novel peptide antagonist of nicotinic acetylcholine receptors
    • McIntosh, J. M., Dowell, C., Watkins, M., Garrett, J. E., Yoshikami, D., and Olivera, B. M. (2002) Alpha-conotoxin GIC from Conus geographus, a novel peptide antagonist of nicotinic acetylcholine receptors, J. Biol. Chem. 277, 33610-33615.
    • (2002) J. Biol. Chem , vol.277 , pp. 33610-33615
    • McIntosh, J.M.1    Dowell, C.2    Watkins, M.3    Garrett, J.E.4    Yoshikami, D.5    Olivera, B.M.6
  • 38
    • 9144236304 scopus 로고    scopus 로고
    • Conantokins: Peptide antagonists of NMDA receptors
    • Layer, R. T., Wagstaff, J. D., and White, H. S. (2004) Conantokins: peptide antagonists of NMDA receptors, Curr. Med. Chem. 11, 3073-3084.
    • (2004) Curr. Med. Chem , vol.11 , pp. 3073-3084
    • Layer, R.T.1    Wagstaff, J.D.2    White, H.S.3
  • 40
    • 0036930324 scopus 로고    scopus 로고
    • Conus venom peptides: Reflections from the biology of clades and specie
    • Olivera, B. M. (2002) Conus venom peptides: reflections from the biology of clades and specie, Annu. Rev. Ecol. Syst. 33, 25-47.
    • (2002) Annu. Rev. Ecol. Syst , vol.33 , pp. 25-47
    • Olivera, B.M.1
  • 41
    • 0030691875 scopus 로고    scopus 로고
    • Rapid in situ neutralization protocols for Boc and Fmoc solid-phase chemistries
    • Alewood, P., Alewood, D., Miranda, L., Love, S., Meutermans, W., and Wilson, D. (1997) Rapid in situ neutralization protocols for Boc and Fmoc solid-phase chemistries, Methods Enzymol. 289, 14-29.
    • (1997) Methods Enzymol , vol.289 , pp. 14-29
    • Alewood, P.1    Alewood, D.2    Miranda, L.3    Love, S.4    Meutermans, W.5    Wilson, D.6
  • 42
    • 32344433189 scopus 로고    scopus 로고
    • The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3
    • Zorn, S., Leipold, E., Hansel, A., Bulaj, G., Olivera, B. M., Terlau, H., and Heinemann, S. H. (2006) The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3, FEBS Lett. 580, 1360-1364.
    • (2006) FEBS Lett , vol.580 , pp. 1360-1364
    • Zorn, S.1    Leipold, E.2    Hansel, A.3    Bulaj, G.4    Olivera, B.M.5    Terlau, H.6    Heinemann, S.H.7
  • 44
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • Wakankar, A. A., and Borchardt, R. T. (2006) Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization, J. Pharm. Sci. 95, 2321-2336.
    • (2006) J. Pharm. Sci , vol.95 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 45
    • 0029854154 scopus 로고    scopus 로고
    • Contryphan is a D-tryptophan-containing Conus peptide
    • Jimenez, E. C., Olivera, B. M., Gray, W. R., and Cruz, L. J. (1996) Contryphan is a D-tryptophan-containing Conus peptide, J. Biol. Chem. 271, 28002-28005.
    • (1996) J. Biol. Chem , vol.271 , pp. 28002-28005
    • Jimenez, E.C.1    Olivera, B.M.2    Gray, W.R.3    Cruz, L.J.4
  • 46
    • 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
    • Dutertre, S., Lumsden, N. G., Alewood, P. F., and Lewis, R. J. (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, 3860-3866.
    • (2006) FEBS Lett , vol.580 , pp. 3860-3866
    • Dutertre, S.1    Lumsden, N.G.2    Alewood, P.F.3    Lewis, R.J.4
  • 47
    • 0033602916 scopus 로고    scopus 로고
    • Effects of chirality at Tyr13 on the structure-activity relationships of omega-conotoxins from Conus magus
    • Nielsen, K. J., Adams, D. A., Alewood, P. F., Lewis, R. J., Thomas, L., Schroeder, T., and Craik, D. J. (1999) Effects of chirality at Tyr13 on the structure-activity relationships of omega-conotoxins from Conus magus, Biochemistry 38, 6741-6751.
    • (1999) Biochemistry , vol.38 , pp. 6741-6751
    • Nielsen, K.J.1    Adams, D.A.2    Alewood, P.F.3    Lewis, R.J.4    Thomas, L.5    Schroeder, T.6    Craik, D.J.7
  • 48
    • 3543031622 scopus 로고    scopus 로고
    • Development of small molecules that mimic the binding of omega-conotoxins at the N-type voltage-gated calcium channel
    • Schroeder, C. I., Smythe, M. L., and Lewis, R. J. (2004) Development of small molecules that mimic the binding of omega-conotoxins at the N-type voltage-gated calcium channel, Mol. Diversity 8, 127-134.
    • (2004) Mol. Diversity , vol.8 , pp. 127-134
    • Schroeder, C.I.1    Smythe, M.L.2    Lewis, R.J.3
  • 51
    • 1242273820 scopus 로고    scopus 로고
    • Chemical and functional identification and characterization of novel sulfated α-conotoxins from the cone snail Conus anemone
    • Loughnan, M. L., Nicke, A., Jones, A., Adams, D. J., Alewood, P. F., and Lewis, R. J. (2004) Chemical and functional identification and characterization of novel sulfated α-conotoxins from the cone snail Conus anemone, J. Med. Chem. 47, 1234-1241.
    • (2004) J. Med. Chem , vol.47 , pp. 1234-1241
    • Loughnan, M.L.1    Nicke, A.2    Jones, A.3    Adams, D.J.4    Alewood, P.F.5    Lewis, R.J.6
  • 52
    • 0030584684 scopus 로고    scopus 로고
    • The 1.1 Å 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., and Martin, J. L. (1996) The 1.1 Å crystal structure of the neuronal acetylcholine receptor antagonist, α-conotoxin PnIA from Conus pennaceus, Structure 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
  • 53
    • 0038661000 scopus 로고    scopus 로고
    • A novel alpha-conotoxin identified by gene sequencing is active in suppressing the vascular response to selective stimulation of sensory nerves in vivo
    • Sandall, D. W., Satkunanathan, N., Keays, D. A., Polidano, M. A., Liping, X., Pham, V., Down, J. G., Khalil, Z., Livett, B. G., and Gayler, K. R. (2003) A novel alpha-conotoxin identified by gene sequencing is active in suppressing the vascular response to selective stimulation of sensory nerves in vivo, Biochemistry 42, 6904-6911.
    • (2003) Biochemistry , vol.42 , pp. 6904-6911
    • Sandall, D.W.1    Satkunanathan, N.2    Keays, D.A.3    Polidano, M.A.4    Liping, X.5    Pham, V.6    Down, J.G.7    Khalil, Z.8    Livett, B.G.9    Gayler, K.R.10
  • 54
    • 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., and Craik, D. J. (2006) The synthesis, structural characterization, and receptor specificity of the α-conotoxin Vc1.1 J. Biol. Chem. 281, 23254-23263.
    • (2006) J. Biol. Chem , vol.281 , pp. 23254-23263
    • Clark, R.J.1    Fischer, H.2    Nevin, S.T.3    Adams, D.J.4    Craik, D.J.5
  • 55
    • 26844476004 scopus 로고    scopus 로고
    • α-Conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones
    • Satkunanathan, N., Livett, B., Gayler, K., Sandall, D., Down, J., and Khalil, Z. (2005) α-Conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones, Brain Res. 1059, 149-158.
    • (2005) Brain Res , vol.1059 , pp. 149-158
    • Satkunanathan, N.1    Livett, B.2    Gayler, K.3    Sandall, D.4    Down, J.5    Khalil, Z.6
  • 56
    • 0344406263 scopus 로고    scopus 로고
    • Synthesis, structure elucidation, in vitro biological activity, toxicity, and Caco-2 cell permeability of lipophilic analogues of α-conotoxin MII
    • Blanchfield, J. T., Dutton, J. L., Hogg, R. C., Gallagher, O. P., Craik, D. J., Jones, A., Adams, D. J., Lewis, R. J., Alewood, P. F., and Toth, I. (2003) Synthesis, structure elucidation, in vitro biological activity, toxicity, and Caco-2 cell permeability of lipophilic analogues of α-conotoxin MII, J. Med. Chem. 46, 1266-1272.
    • (2003) J. Med. Chem , vol.46 , pp. 1266-1272
    • Blanchfield, J.T.1    Dutton, J.L.2    Hogg, R.C.3    Gallagher, O.P.4    Craik, D.J.5    Jones, A.6    Adams, D.J.7    Lewis, R.J.8    Alewood, P.F.9    Toth, I.10
  • 58
    • 33947424873 scopus 로고    scopus 로고
    • Protein folding determinants: Structural features determining alternative disulfide pairing in α- and χ /λ-conotoxins
    • Kang, T. S., Radic, Z., Talley, T. T., Jois, S. D., Taylor, P., and Kini, R. M. (2007) Protein folding determinants: structural features determining alternative disulfide pairing in α- and χ /λ-conotoxins, Biochemistry 46, 3338-3355.
    • (2007) Biochemistry , vol.46 , pp. 3338-3355
    • Kang, T.S.1    Radic, Z.2    Talley, T.T.3    Jois, S.D.4    Taylor, P.5    Kini, R.M.6
  • 59
    • 0029856411 scopus 로고    scopus 로고
    • Folding of omega-conotoxins. 2. Influence of precursor sequences and protein disulfide isomerase
    • Price-Carter, M., Gray, W. R., and Goldenberg, D. P. (1996) Folding of omega-conotoxins. 2. Influence of precursor sequences and protein disulfide isomerase, Biochemistry 35, 15547-15557.
    • (1996) Biochemistry , vol.35 , pp. 15547-15557
    • Price-Carter, M.1    Gray, W.R.2    Goldenberg, D.P.3
  • 60
    • 0034671899 scopus 로고    scopus 로고
    • λ-Conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus
    • Balaji, R. A., Ohtake, A., Sato, K., Gopalakrishnakone, P., Kini, R. M., Seow, K. T., and Bay, B. H. (2000) λ-Conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus, J. Biol. Chem. 275, 39516-39522.
    • (2000) J. Biol. Chem , vol.275 , pp. 39516-39522
    • Balaji, R.A.1    Ohtake, A.2    Sato, K.3    Gopalakrishnakone, P.4    Kini, R.M.5    Seow, K.T.6    Bay, B.H.7
  • 64
    • 3142739323 scopus 로고    scopus 로고
    • Adrenergic targets for the treatment of cognitive deficits in schizophrenia
    • Arnsten, A. F. (2004) Adrenergic targets for the treatment of cognitive deficits in schizophrenia, Psychopharmacology (Berlin) 174, 25-31.
    • (2004) Psychopharmacology (Berlin) , vol.174 , pp. 25-31
    • Arnsten, A.F.1
  • 65
    • 0034730440 scopus 로고    scopus 로고
    • Noradrenaline systems in the hypothalamus, amygdala and locus coeruleus are involved in the provocation of anxiety: Basic studies
    • Tanaka, M., Yoshida, M., Emoto, H., and Ishii, H. (2000) Noradrenaline systems in the hypothalamus, amygdala and locus coeruleus are involved in the provocation of anxiety: basic studies, Eur. J. Pharmacol. 405, 397-406.
    • (2000) Eur. J. Pharmacol , vol.405 , pp. 397-406
    • Tanaka, M.1    Yoshida, M.2    Emoto, H.3    Ishii, H.4
  • 66
    • 0033555286 scopus 로고    scopus 로고
    • Transmitters involved in antinociception in the spinal cord
    • Furst, S. (1999) Transmitters involved in antinociception in the spinal cord, Brain Res. Bull. 48, 129-141.
    • (1999) Brain Res. Bull , vol.48 , pp. 129-141
    • Furst, S.1
  • 68
    • 15444344863 scopus 로고    scopus 로고
    • A novel post-translational modification involving bromination of tryptophan. Identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom
    • Craig, A. G., Jimenez, E. C., Dykert, J., Nielsen, D. B., Gulyas, J., Abogadie, F. C., Porter, J., Rivier, J. E., Cruz, L. J., Olivera, B. M., and McIntosh, J. M. (1997) A novel post-translational modification involving bromination of tryptophan. Identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom, J. Biol. Chem. 272, 4689-4698.
    • (1997) J. Biol. Chem , vol.272 , pp. 4689-4698
    • Craig, A.G.1    Jimenez, E.C.2    Dykert, J.3    Nielsen, D.B.4    Gulyas, J.5    Abogadie, F.C.6    Porter, J.7    Rivier, J.E.8    Cruz, L.J.9    Olivera, B.M.10    McIntosh, J.M.11
  • 71
    • 0035968281 scopus 로고    scopus 로고
    • Site-specific charge interactions of alpha-conotoxin MI with the nicotinic acetylcholine receptor
    • Papineni, R. V., Sanchez, J. U., Baksi, K., Willcockson, I. U., and Pedersen, S. E. (2001) Site-specific charge interactions of alpha-conotoxin MI with the nicotinic acetylcholine receptor, J. Biol. Chem. 276, 23589-23598.
    • (2001) J. Biol. Chem , vol.276 , pp. 23589-23598
    • Papineni, R.V.1    Sanchez, J.U.2    Baksi, K.3    Willcockson, I.U.4    Pedersen, S.E.5
  • 72
    • 33847159894 scopus 로고    scopus 로고
    • High-throughput synthesis of conopeptides: A safety-catch linker approach enabling disulfide formation in 96-well format
    • Brust, A., and Tickle, A. E. (2007) High-throughput synthesis of conopeptides: a safety-catch linker approach enabling disulfide formation in 96-well format, J. Pept. Sci. 13, 133-141.
    • (2007) J. Pept. Sci , vol.13 , pp. 133-141
    • Brust, A.1    Tickle, A.E.2
  • 75
    • 0037474213 scopus 로고    scopus 로고
    • Isolation, structure, and activity of GID, a novel α 4/7-conotoxin with an extended N-terminal sequence
    • Nicke, A., Loughnan, M. L., Millard, E. L., Alemood, P. F., Adams, D. J., Daly, N. L., Craik, D. J., and Lewis, R. J. (2003) Isolation, structure, and activity of GID, a novel α 4/7-conotoxin with an extended N-terminal sequence, J. Biol. Chem. 278, 3137-3144.
    • (2003) J. Biol. Chem , vol.278 , pp. 3137-3144
    • Nicke, A.1    Loughnan, M.L.2    Millard, E.L.3    Alemood, P.F.4    Adams, D.J.5    Daly, N.L.6    Craik, D.J.7    Lewis, R.J.8
  • 76
    • 0032079381 scopus 로고    scopus 로고
    • Structure determination of the three disulfide bond isomers of α-conotoxin GI: A model for the role of disulfide bonds in structural stability
    • Gehrmann, J., Alewood, P. F., and Craik, D. J. (1998) Structure determination of the three disulfide bond isomers of α-conotoxin GI: a model for the role of disulfide bonds in structural stability, J. Mol. Biol. 278, 401-415.
    • (1998) J. Mol. Biol , vol.278 , pp. 401-415
    • Gehrmann, J.1    Alewood, P.F.2    Craik, D.J.3
  • 77
    • 0037073683 scopus 로고    scopus 로고
    • A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity
    • Dutton, J. L., Bansal, P. S., Hogg, R. C., Adams, D. J., Alewood, P. F., and Craik, D. J. (2002) A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity, J. Biol. Chem. 277, 48849-48857.
    • (2002) J. Biol. Chem , vol.277 , pp. 48849-48857
    • Dutton, J.L.1    Bansal, P.S.2    Hogg, R.C.3    Adams, D.J.4    Alewood, P.F.5    Craik, D.J.6
  • 78
    • 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., and Alewood, P. F. (2006) α-Selenoconotoxins, a new class of potent α7 neuronal nicotinic receptor antagonists, J. Biol. Chem. 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
  • 79
    • 0032484231 scopus 로고    scopus 로고
    • Isomorphous replacement of cystine with selenocystine in endothelin: Oxidative refolding, biological and conformational properties of [Sec3,Sec11,Nle7]-endothelin-1
    • Pegoraro, S., Fiori, S., Rudolph-Bohner, S., Watanabe, T. X., and Moroder, L. (1998) Isomorphous replacement of cystine with selenocystine in endothelin: oxidative refolding, biological and conformational properties of [Sec3,Sec11,Nle7]-endothelin-1, J. Mol. Biol. 284, 779-792.
    • (1998) J. Mol. Biol , vol.284 , pp. 779-792
    • Pegoraro, S.1    Fiori, S.2    Rudolph-Bohner, S.3    Watanabe, T.X.4    Moroder, L.5
  • 80
    • 0037416471 scopus 로고    scopus 로고
    • Solid-phase synthesis and biological activity of a thioether analogue of conotoxin G1
    • Bondebjerg, J., Grunnet, M., Jespersen, T., and Meldal, M. (2003) Solid-phase synthesis and biological activity of a thioether analogue of conotoxin G1, ChemBioChem 4, 186-194.
    • (2003) ChemBioChem , vol.4 , pp. 186-194
    • Bondebjerg, J.1    Grunnet, M.2    Jespersen, T.3    Meldal, M.4
  • 81
    • 0034649554 scopus 로고    scopus 로고
    • Chemical syntheses and biological activities of lactam analogues of alpha-conotoxin SI
    • Hargittai, B., Sole, N. A., Groebe, D. R., Abramson, S. N., and Barany, G. (2000) Chemical syntheses and biological activities of lactam analogues of alpha-conotoxin SI, J. Med. Chem. 43, 4787-4792.
    • (2000) J. Med. Chem , vol.43 , pp. 4787-4792
    • Hargittai, B.1    Sole, N.A.2    Groebe, D.R.3    Abramson, S.N.4    Barany, G.5
  • 83
    • 1642357546 scopus 로고    scopus 로고
    • Cyclosporine: 20 years of experience at the University of Munich
    • Graeb, C., Arbogast, H., Guba, M., Jauch, K. W., and Land, W. (2004) Cyclosporine: 20 years of experience at the University of Munich, Transplant. Proc. 36, S125-S129.
    • (2004) Transplant. Proc , vol.36
    • Graeb, C.1    Arbogast, H.2    Guba, M.3    Jauch, K.W.4    Land, W.5
  • 84
    • 33846430034 scopus 로고    scopus 로고
    • Structure-activity relationships of cyclic peptide-based chemokine receptor CXCR4 antagonists: Disclosing the importance of side-chain and backbone functionalities
    • Usda, S., Oishi, S., Wang, Z. X., Araki, T., Tamamura, H., Cluzeau, J., Ohno, H., Kusano, S., Nakashima, H., Trent, J. O., Peiper, S. C., and Fujii, N. (2007) Structure-activity relationships of cyclic peptide-based chemokine receptor CXCR4 antagonists: disclosing the importance of side-chain and backbone functionalities, J. Med. Chem. 50, 192-198.
    • (2007) J. Med. Chem , vol.50 , pp. 192-198
    • Usda, S.1    Oishi, S.2    Wang, Z.X.3    Araki, T.4    Tamamura, H.5    Cluzeau, J.6    Ohno, H.7    Kusano, S.8    Nakashima, H.9    Trent, J.O.10    Peiper, S.C.11    Fujii, N.12
  • 85
    • 0022398712 scopus 로고
    • Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution
    • Chazin, W. J., Goldenberg, D. P., Creighton, T. E., and Wuthrich, K. (1985) Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution, Eur. J. Biochem. 152, 429-437.
    • (1985) Eur. J. Biochem , vol.152 , pp. 429-437
    • Chazin, W.J.1    Goldenberg, D.P.2    Creighton, T.E.3    Wuthrich, K.4
  • 87
    • 33750460621 scopus 로고    scopus 로고
    • Cyclic MrIA: A stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter
    • Lovelace, E. S., Armishaw, C. J., Colgrave, M. L., Wahlstrom, M. E., Alewood, P. F., Daly, N. L., and Craik, D. J. (2006) Cyclic MrIA: a stable and potent cyclic conotoxin with a novel topological fold that targets the norepinephrine transporter, J. Med. Chem. 49, 6561-6568.
    • (2006) J. Med. Chem , vol.49 , pp. 6561-6568
    • Lovelace, E.S.1    Armishaw, C.J.2    Colgrave, M.L.3    Wahlstrom, M.E.4    Alewood, P.F.5    Daly, N.L.6    Craik, D.J.7
  • 88
    • 33750585964 scopus 로고    scopus 로고
    • Novel approaches to pain relief using venom-derived peptides
    • Hogg, R. C. (2006) Novel approaches to pain relief using venom-derived peptides, Curr. Med. Chem. 13, 3191-3201.
    • (2006) Curr. Med. Chem , vol.13 , pp. 3191-3201
    • Hogg, R.C.1
  • 93
    • 34250767683 scopus 로고    scopus 로고
    • A vasopressin/oxytocin-related conopeptide with a gamma-carboxyglutamate at position 8
    • Moller, C., and Mari, F. (2007) A vasopressin/oxytocin-related conopeptide with a gamma-carboxyglutamate at position 8, Biochem. J. 404, 413-419.
    • (2007) Biochem. J , vol.404 , pp. 413-419
    • Moller, C.1    Mari, F.2
  • 94
    • 0031887369 scopus 로고    scopus 로고
    • The contryphans, a D-tryptophan-containing family of Conus peptides: Interconversion between conformers
    • Jacobsen, R., Jimenez, E. C., Grilley, M., Watkins, M., Hillyard, D., Cruz, L. J., and Olivera, B. M. (1998) The contryphans, a D-tryptophan-containing family of Conus peptides: interconversion between conformers, J. Pept. Res. 51, 173-179.
    • (1998) J. Pept. Res , vol.51 , pp. 173-179
    • Jacobsen, R.1    Jimenez, E.C.2    Grilley, M.3    Watkins, M.4    Hillyard, D.5    Cruz, L.J.6    Olivera, B.M.7
  • 99
    • 0030016085 scopus 로고    scopus 로고
    • Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels
    • Hill, J. M., Alewood, P. F., and Craik, D. J. (1996) Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels, Biochemistry 35, 8824-8835.
    • (1996) Biochemistry , vol.35 , pp. 8824-8835
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 100
    • 0032506167 scopus 로고    scopus 로고
    • Three-dimensional solution structure of α-conotoxin MII by NMR spectroscopv: Effects of solution environment on helicity
    • Hill, J. M., Oomen, C. J., Miranda, L. P., Bingham, J. P., Alewood, P. F., and Craik, D. J. (1998) Three-dimensional solution structure of α-conotoxin MII by NMR spectroscopv: effects of solution environment on helicity, Biochemistry 37, 15621-15630.
    • (1998) Biochemistry , vol.37 , pp. 15621-15630
    • Hill, J.M.1    Oomen, C.J.2    Miranda, L.P.3    Bingham, J.P.4    Alewood, P.F.5    Craik, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.