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Volumn , Issue , 2011, Pages 119-137

Conotoxin-Based Leads in Drug Design

Author keywords

Conopeptides; Cyclic peptides; NMR; Structure

Indexed keywords


EID: 84887146787     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527636730.ch5     Document Type: Chapter
Times cited : (1)

References (64)
  • 1
    • 0001018607 scopus 로고
    • Preliminary studies on the venom of the marine snail conus
    • Kohn, A.J., Saunders, P.R., and Wiener, S. (1960) Preliminary studies on the venom of the marine snail conus. Ann. NY Acad. Sci., 90 (3), 706-725.
    • (1960) Ann. NY Acad. Sci. , vol.90 , Issue.3 , pp. 706-725
    • Kohn, A.J.1    Saunders, P.R.2    Wiener, S.3
  • 3
    • 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 (1), 41-68.
    • (2004) Physiol. Rev. , vol.84 , Issue.1 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 5
    • 0035033785 scopus 로고    scopus 로고
    • Alpha-conotoxins: nicotinic acetylcholine receptor antagonists as pharmacological tools and potential drug leads
    • Dutton, J.L. and Craik, D.J. (2001) Alpha-conotoxins: nicotinic acetylcholine receptor antagonists as pharmacological tools and potential drug leads. Curr. Med. Chem., 8 (4), 327-344.
    • (2001) Curr. Med. Chem. , vol.8 , Issue.4 , pp. 327-344
    • Dutton, J.L.1    Craik, D.J.2
  • 6
    • 67649592405 scopus 로고    scopus 로고
    • Conotoxins: natural product drug leads
    • Halai, R. and Craik, D.J. (2009) Conotoxins: natural product drug leads. Nat. Prod. Rep., 26 (4), 526-536.
    • (2009) Nat. Prod. Rep. , vol.26 , Issue.4 , pp. 526-536
    • Halai, R.1    Craik, D.J.2
  • 8
    • 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. Chimica Oggi-Chem. Today, 21 (6), 43-48.
    • (2003) Chimica Oggi-Chem. Today , vol.21 , Issue.6 , pp. 43-48
    • Mari, F.1    Fields, G.B.2
  • 9
    • 0002383277 scopus 로고
    • The ecology of conus in Hawaii
    • Kohn, A.J. (1959) The ecology of conus in Hawaii. Ecol. Monog., 29 (1), 47-90.
    • (1959) Ecol. Monog. , vol.29 , Issue.1 , pp. 47-90
    • Kohn, A.J.1
  • 10
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • Terlau, H., Shon, K.J., Grilley, M., Stocker, M., Stuhmer, W., and Olivera, B.M. (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
  • 11
    • 0016374522 scopus 로고
    • Pharmacology of venom of conus geographus
    • Endean, R., Parish, G., and Gyr, P. (1974) Pharmacology of venom of conus geographus. Toxicon, 12 (12), 131-138.
    • (1974) Toxicon , vol.12 , Issue.12 , pp. 131-138
    • Endean, R.1    Parish, G.2    Gyr, P.3
  • 12
    • 0017567302 scopus 로고
    • Characterization of neurotoxic constituents of Conus-Geographus(L) venom
    • Spence, I., Gillessen, D., Gregson, R.P., and Quinn, R.J. (1977) Characterization of neurotoxic constituents of Conus-Geographus(L) venom, Life Sci., 21, 1759-1769.
    • (1977) Life Sci. , vol.21 , pp. 1759-1769
    • Spence, I.1    Gillessen, D.2    Gregson, R.P.3    Quinn, R.J.4
  • 13
    • 0025342986 scopus 로고
    • Constant and hypervariable regions in conotoxin propeptides
    • Woodward, S.R., Cruz, L.J., Olivera, B. M., and Hillyard, D.R. (1990) Constant and hypervariable regions in conotoxin propeptides. Embo J., 9 (4), 1015-1020.
    • (1990) Embo J. , vol.9 , Issue.4 , pp. 1015-1020
    • Woodward, S.R.1    Cruz, L.J.2    Olivera, B.M.3    Hillyard, D.R.4
  • 14
    • 0032795276 scopus 로고    scopus 로고
    • Speciation of cone snails and interspecific hyperdivergence of their venom peptides potential-evolutionary significance of introns
    • Molecular Strategies in Biological Evolution
    • Olivera, B.M., Walker, C., Cartier, G.E., Hooper, D., Santos, A.D., Schoenfeld, R., Shetty, R., Watkins, M., Bandyopadhyay, P., and Hillyard, D.R. (1999) Speciation of cone snails and interspecific hyperdivergence of their venom peptides potential-evolutionary significance of introns. Ann. NY Acad. Sci., 870, (Molecular Strategies in Biological Evolution), 223-237.
    • (1999) Ann. NY Acad. Sci. , vol.870 , pp. 223-237
    • Olivera, B.M.1    Walker, C.2    Cartier, G.E.3    Hooper, D.4    Santos, A.D.5    Schoenfeld, R.6    Shetty, R.7    Watkins, M.8    Bandyopadhyay, P.9    Hillyard, D.R.10
  • 15
    • 34249310680 scopus 로고    scopus 로고
    • From the identification of gene organization of alpha conotoxins to the cloning of novel toxins
    • Yuan, D.D., Han, Y.H., Wang, C.G., and Chi, C.W. (2007) From the identification of gene organization of alpha conotoxins to the cloning of novel toxins. Toxicon, 49 (8), 1135-1149.
    • (2007) Toxicon , vol.49 , Issue.8 , pp. 1135-1149
    • Yuan, D.D.1    Han, Y.H.2    Wang, C.G.3    Chi, C.W.4
  • 16
    • 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 (23), 3029-3040.
    • (2004) Curr. Med. Chem. , vol.11 , Issue.23 , pp. 3029-3040
    • Miljanich, G.P.1
  • 18
    • 0344036929 scopus 로고    scopus 로고
    • Chronic neuropathic pain
    • Canavero, S. and Bonicalzi, V. (2003) Chronic neuropathic pain. New Engl. J. Med., 348 (26), 2688-2689.
    • (2003) New Engl. J. Med. , vol.348 , Issue.26 , pp. 2688-2689
    • Canavero, S.1    Bonicalzi, V.2
  • 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 (3), 163-169.
    • (1995) FEBS Lett. , vol.370 , Issue.3 , pp. 163-169
    • Basus, V.J.1    Nadasdi, L.2    Ramachandran, J.3    Miljanich, G.P.4
  • 20
    • 0033603390 scopus 로고    scopus 로고
    • Structure-activity relationships of omega-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels
    • Nielsen, K.J., Adams, D., Thomas, L., Bond, T., Alewood, P.F., Craik, D.J., and Lewis, R.J. (1999) Structure-activity relationships of omega-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels. J. Mol. Biol., 289 (5), 1405-1421.
    • (1999) J. Mol. Biol. , vol.289 , Issue.5 , pp. 1405-1421
    • Nielsen, K.J.1    Adams, D.2    Thomas, L.3    Bond, T.4    Alewood, P.F.5    Craik, D.J.6    Lewis, R.J.7
  • 21
    • 32344433189 scopus 로고    scopus 로고
    • The mu O-conotoxin MrVIA inhibits voltagegated sodium channels by associating with domain-3
    • Zorn, S., Leipold, E., Hansel, A., Bulaj, G., Olivera, B.M., Terlau, H., and Heinermann, S.H. (2006) The mu O-conotoxin MrVIA inhibits voltagegated sodium channels by associating with domain-3. FEBS Lett., 580 (5), 1360-1364.
    • (2006) FEBS Lett. , vol.580 , Issue.5 , pp. 1360-1364
    • Zorn, S.1    Leipold, E.2    Hansel, A.3    Bulaj, G.4    Olivera, B.M.5    Terlau, H.6    Heinermann, S.H.7
  • 23
    • 33747372837 scopus 로고    scopus 로고
    • The synthesis, structural characterization, and receptor specificity of the alphaconotoxin Vc1.1 J
    • 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 alphaconotoxin Vc1.1 J. Biol. Chem., 281 (32), 23254-23263.
    • (2006) Biol. Chem. , vol.281 , Issue.32 , pp. 23254-23263
    • Clark, R.J.1    Fischer, H.2    Nevin, S.T.3    Adams, D.J.4    Craik, D.J.5
  • 24
    • 0141994011 scopus 로고    scopus 로고
    • Chi-conopeptide MrIA partially overlaps desipramine and cocaine binding sites on the human norepinephrine transporter
    • Bryan-Lluka, L.J., Bonisch, H., and Lewis, R.J. (2003) Chi-conopeptide MrIA partially overlaps desipramine and cocaine binding sites on the human norepinephrine transporter. J. Biol. Chem., 278 (41), 40324-40329.
    • (2003) J. Biol. Chem. , vol.278 , Issue.41 , pp. 40324-40329
    • Bryan-Lluka, L.J.1    Bonisch, H.2    Lewis, R.J.3
  • 27
    • 0032501995 scopus 로고    scopus 로고
    • Gammaconotoxin-PnVIIA, a gammacarboxyglutamate-containing peptide agonist of neuronal pacemaker cation currents
    • Fainzilber, M., Nakamura, T., Lodder, J.C., Zlotkin, E., Kits, K.S., and Burlingame, A.L. (1998) Gammaconotoxin-PnVIIA, a gammacarboxyglutamate-containing peptide agonist of neuronal pacemaker cation currents. Biochemistry, 37 (6), 1470-1477.
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1470-1477
    • Fainzilber, M.1    Nakamura, T.2    Lodder, J.C.3    Zlotkin, E.4    Kits, K.S.5    Burlingame, A.L.6
  • 28
    • 12844282068 scopus 로고    scopus 로고
    • Differential antagonism by conotoxin p-TIA of contractions mediated by distinct alpha(1)-adrenoceptor subtypes in rat vas deferens, spleen and aorta
    • Lima, V., Mueller, A., Kamikihara, S.Y., Raymundi, V., Alewood, D., Lewis, R.J., Chen, Z.J., Minneman, K.P., and Pupo, A.S. (2005) Differential antagonism by conotoxin p-TIA of contractions mediated by distinct alpha(1)-adrenoceptor subtypes in rat vas deferens, spleen and aorta. Eur. J. Pharmacol., 508 (1-3), 183-192.
    • (2005) Eur. J. Pharmacol. , vol.508 , Issue.1-3 , pp. 183-192
    • Lima, V.1    Mueller, A.2    Kamikihara, S.Y.3    Raymundi, V.4    Alewood, D.5    Lewis, R.J.6    Chen, Z.J.7    Minneman, K.P.8    Pupo, A.S.9
  • 30
    • 0037044844 scopus 로고    scopus 로고
    • Structure of a novel P-superfamily spasmodic conotoxin reveals an inhibitory cystine knot motif
    • Miles, L.A., Dy, C.Y., Nielsen, J., Barnham, K.J., Hinds, M.G., Olivera, B.M., Bulaj, G., and Norton, R.S. (2002) Structure of a novel P-superfamily spasmodic conotoxin reveals an inhibitory cystine knot motif. J. Biol. Chem., 277 (45), 43033-43040.
    • (2002) J. Biol. Chem. , vol.277 , Issue.45 , pp. 43033-43040
    • Miles, L.A.1    Dy, C.Y.2    Nielsen, J.3    Barnham, K.J.4    Hinds, M.G.5    Olivera, B.M.6    Bulaj, G.7    Norton, R.S.8
  • 31
    • 77952240443 scopus 로고    scopus 로고
    • Conopeptide characterization and classifications: an analysis using ConoServer
    • Kaas, Q., Westermann, J.C., and Craik, D.J. (2010) Conopeptide characterization and classifications: an analysis using ConoServer. Toxicon, 55 (8), 1491-1509.
    • (2010) Toxicon , vol.55 , Issue.8 , pp. 1491-1509
    • Kaas, Q.1    Westermann, J.C.2    Craik, D.J.3
  • 32
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2.3 Å resolution crystal structure of nerve growth factor
    • McDonald, N.Q., Lapatto, R., Murrayrust, J., Gunning, J., Wlodawer, A., and Blundell, T.L. (1991) New protein fold revealed by a 2.3 Å resolution crystal structure of nerve growth factor. Nature, 354 (6352), 411-414.
    • (1991) Nature , vol.354 , Issue.6352 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murrayrust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 33
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple stranded beta sheet in toxic and inhibitory polypeptides
    • Pallaghy, P.K., Nielsen, K.J., Craik, D.J., and Norton, R.S. (1994) A common structural motif incorporating a cystine knot and a triple stranded beta sheet in toxic and inhibitory polypeptides. Protein Sci., 3 (10), 1833-1839.
    • (1994) Protein Sci. , vol.3 , Issue.10 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 35
    • 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 (1), 43-60.
    • (2001) Toxicon , vol.39 , Issue.1 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 36
    • 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 (2), 271-275.
    • (1999) Eur. J. Biochem. , vol.264 , Issue.2 , pp. 271-275
    • Craig, A.G.1    Bandyopadhyay, P.2    Olivera, B.M.3
  • 40
    • 0036324311 scopus 로고    scopus 로고
    • The synthesis and structure of an N-terminal dodecanoic acid conjugate of alphaconotoxin MII
    • Blanchfield, J., Dutton, J., Hogg, R., Craik, D., Adams, D., Lewis, R., Alewood, P., and Toth, I. (2001) The synthesis and structure of an N-terminal dodecanoic acid conjugate of alphaconotoxin MII. Lett. Pept. Sci., 8 (3-5), 235-239.
    • (2001) Lett. Pept. Sci. , vol.8 , Issue.3-5 , pp. 235-239
    • Blanchfield, J.1    Dutton, J.2    Hogg, R.3    Craik, D.4    Adams, D.5    Lewis, R.6    Alewood, P.7    Toth, I.8
  • 41
    • 0020417225 scopus 로고
    • Primary and secondary structure of conotoxin GI, a neurotoxic tridecapeptide from a marine snail
    • Nishiuchi, Y. and Sakakibara, S. (1982) Primary and secondary structure of conotoxin GI, a neurotoxic tridecapeptide from a marine snail. FEBS Lett., 148 (2), 260-262.
    • (1982) FEBS Lett. , vol.148 , Issue.2 , pp. 260-262
    • Nishiuchi, Y.1    Sakakibara, S.2
  • 42
    • 0021069422 scopus 로고
    • Conotoxin-MI-disulfide bonding and conformational states
    • Gray, W.R., Rivier, J.E., Galyean, R., Cruz, L.J., and Olivera, B.M. (1983) Conotoxin-MI-disulfide bonding and conformational states. J. Biol. Chem., 258 (20), 2247-2251.
    • (1983) J. Biol. Chem. , vol.258 , Issue.20 , pp. 2247-2251
    • Gray, W.R.1    Rivier, J.E.2    Galyean, R.3    Cruz, L.J.4    Olivera, B.M.5
  • 43
    • 0039508174 scopus 로고
    • Synthesis and secondary structure determination of omegaconotoxin GVIA-A 27-peptide with 3 intramolecular disulfide bonds
    • Nishiuchi, Y., Kumagaye, K., Noda, Y., Watanabe, T.X., and Sakakibara, S. (1986) Synthesis and secondary structure determination of omegaconotoxin GVIA-A 27-peptide with 3 intramolecular disulfide bonds. Biopolymers, 25, S61-S68.
    • (1986) Biopolymers , vol.25
    • Nishiuchi, Y.1    Kumagaye, K.2    Noda, Y.3    Watanabe, T.X.4    Sakakibara, S.5
  • 46
    • 33947091567 scopus 로고
    • 9-Fluorenylmethoxycarbonyl aminoprotecting group, J
    • Carpino, L.A. and Han, G.Y. (1972) 9-Fluorenylmethoxycarbonyl aminoprotecting group, J. Org. Chem., 37, 3404-3409.
    • (1972) Org. Chem. , vol.37 , pp. 3404-3409
    • Carpino, L.A.1    Han, G.Y.2
  • 47
    • 34250008546 scopus 로고    scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis: rapid, high yield assembly of difficult sequences
    • Schnölzer, M., Alewood, P., Jones, A., Alewood, D., and SBH, K. (2007) In situ neutralization in Boc-chemistry solid phase peptide synthesis: rapid, high yield assembly of difficult sequences. Int. J. Peptide Res. Ther., 13 (1-2), 31-44.
    • (2007) Int. J. Peptide Res. Ther. , vol.13 , Issue.1-2 , pp. 31-44
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Sbh, K.5
  • 48
    • 36148996891 scopus 로고    scopus 로고
    • Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of conus peptides
    • Bulaj, G. and Olivera, B.M. (2008) Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of conus peptides. Antiox. Redox Signal., 10 (1), 141-155.
    • (2008) Antiox. Redox Signal. , vol.10 , Issue.1 , pp. 141-155
    • Bulaj, G.1    Olivera, B.M.2
  • 49
    • 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-S50.
    • (2006) Magn. Reson. Chem. , vol.44
    • Marx, U.C.1    Daly, N.L.2    Craik, D.J.3
  • 50
    • 0032978197 scopus 로고    scopus 로고
    • Threedimensional structure of alpha-conotoxin EI determined by H-1 NMR spectroscopy
    • Franco, A. and Mari, F. (1999) Threedimensional structure of alpha-conotoxin EI determined by H-1 NMR spectroscopy. Lett. Peptide Sci., 6 (4), 199-207.
    • (1999) Lett. Peptide Sci. , vol.6 , Issue.4 , pp. 199-207
    • Franco, A.1    Mari, F.2
  • 51
    • 0030584684 scopus 로고    scopus 로고
    • The 1.1 angstrom crystal structure of the neuronal acetylcholine receptor antagonist, alpha-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 angstrom crystal structure of the neuronal acetylcholine receptor antagonist, alpha-conotoxin PnIA from Conus pennaceus. Structure, 4 (4), 417-423.
    • (1996) Structure , vol.4 , Issue.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
  • 52
    • 0029775108 scopus 로고    scopus 로고
    • Three-dimensional structure of the alphaconotoxin GI at 1.2 angstrom resolution
    • Guddat, L.W., Martin, J.L., Shan, L., Edmundson, A.B., and Gray,W.R. (1996) Three-dimensional structure of the alphaconotoxin GI at 1.2 angstrom resolution. Biochemistry, 35 (35), 11329-11335.
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11329-11335
    • Guddat, L.W.1    Martin, J.L.2    Shan, L.3    Edmundson, A.B.4    Gray, W.R.5
  • 53
    • 33644870155 scopus 로고    scopus 로고
    • Structural determinants of selective alphaconotoxin binding to a nicotinic acetylcholine receptor homolog AChBP
    • Ulens, C., Hogg, R.C., Celie, P.H., Bertrand, D., Tsetlin, V., Smit, A.B., and Sixma, T.K. (2006) Structural determinants of selective alphaconotoxin binding to a nicotinic acetylcholine receptor homolog AChBP. Proc. Natl. Acad. Sci. USA, 103 (10), 3615-3620.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.10 , pp. 3615-3620
    • Ulens, C.1    Hogg, R.C.2    Celie, P.H.3    Bertrand, D.4    Tsetlin, V.5    Smit, A.B.6    Sixma, T.K.7
  • 55
    • 0037423378 scopus 로고    scopus 로고
    • Omega-conotoxin CVID inhibits a pharmacologically distinct voltage sensitive calcium channel associated with transmitter release from preganglionic nerve terminals
    • Adams, D.J., Smith, A.B., Schroeder, C.I., Yasuda, T., and Lewis, R.J. (2003) Omega-conotoxin CVID inhibits a pharmacologically distinct voltage sensitive calcium channel associated with transmitter release from preganglionic nerve terminals. J. Biol. Chem., 278 (6), 4057-4062.
    • (2003) J. Biol. Chem. , vol.278 , Issue.6 , pp. 4057-4062
    • Adams, D.J.1    Smith, A.B.2    Schroeder, C.I.3    Yasuda, T.4    Lewis, R.J.5
  • 56
    • 33845212316 scopus 로고    scopus 로고
    • Molecular mechanism for analgesia involving specific antagonism of alpha 9 alpha 10 nicotinic acetylcholine receptors
    • Vincler, M., Wittenauer, S., Parker, R., Ellison, M., Olivera, B.M., and McIntosh, J.M. (2006) Molecular mechanism for analgesia involving specific antagonism of alpha 9 alpha 10 nicotinic acetylcholine receptors. Proc. Natl. Acad. Sci. USA, 103 (47), 17880-17884.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.47 , pp. 17880-17884
    • Vincler, M.1    Wittenauer, S.2    Parker, R.3    Ellison, M.4    Olivera, B.M.5    McIntosh, J.M.6
  • 57
    • 36348987984 scopus 로고    scopus 로고
    • Are alpha 9 alpha 10 nicotinic acetylcholine receptors a pain target for alpha-conotoxins? Mol
    • Nevin, S.T., Clark, R.J., Klimis, H., Christie, M.J., Craik, D.J., and Adams, D.J. (2007) Are alpha 9 alpha 10 nicotinic acetylcholine receptors a pain target for alpha-conotoxins? Mol. Pharmacol., 72 (6), 1406-1410.
    • (2007) Pharmacol. , vol.72 , Issue.6 , pp. 1406-1410
    • Nevin, S.T.1    Clark, R.J.2    Klimis, H.3    Christie, M.J.4    Craik, D.J.5    Adams, D.J.6
  • 58
    • 58149172098 scopus 로고    scopus 로고
    • Analgesic alphaconotoxins Vc1.1 and Rg1A inhibit Ntype calcium channels in rat sensory neurons via GABA(B) receptor activation
    • Callaghan, B., Haythornthwaite, A., Berecki, G., Clark, R.J., Craik, D.J., and Adams, D.J. (2008) Analgesic alphaconotoxins Vc1.1 and Rg1A inhibit Ntype calcium channels in rat sensory neurons via GABA(B) receptor activation. J. Neurosci., 28 (43), 10943-10951.
    • (2008) J. Neurosci. , vol.28 , Issue.43 , pp. 10943-10951
    • Callaghan, B.1    Haythornthwaite, A.2    Berecki, G.3    Clark, R.J.4    Craik, D.J.5    Adams, D.J.6
  • 59
    • 75749113276 scopus 로고    scopus 로고
    • Analgesic alpha-conotoxins Vc1.1 and RgIA inhibit N-type calcium channels in sensory neurons of alpha 9 nicotinic receptor knockout mice
    • Callaghan, B. and Adams, D.J. (2010) Analgesic alpha-conotoxins Vc1.1 and RgIA inhibit N-type calcium channels in sensory neurons of alpha 9 nicotinic receptor knockout mice. Channels, 4 (1), 51-54.
    • (2010) Channels , vol.4 , Issue.1 , pp. 51-54
    • Callaghan, B.1    Adams, D.J.2
  • 60
    • 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 (22), 6904-6911.
    • (2003) Biochemistry , vol.42 , Issue.22 , 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
  • 61
    • 26844476004 scopus 로고    scopus 로고
    • Alpha-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) Alpha-conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones. Brain Res., 1059 (2), 149-158.
    • (2005) Brain Res. , vol.1059 , Issue.2 , pp. 149-158
    • Satkunanathan, N.1    Livett, B.2    Gayler, K.3    Sandall, D.4    Down, J.5    Khalil, Z.6
  • 64
    • 33645077862 scopus 로고    scopus 로고
    • Chemistry-seamless proteins tie up their loose ends
    • Craik, D.J. (2006) Chemistry-seamless proteins tie up their loose ends. Science, 311 (5767), 1563-1564.
    • (2006) Science , vol.311 , Issue.5767 , pp. 1563-1564
    • Craik, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.