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Volumn 4, Issue 11, 2012, Pages 1236-1260

Conotoxins targeting neuronal voltage-gated sodium channel subtypes: Potential analgesics?

Author keywords

conotoxin; O conotoxin; Analgesic; Nav1.3; Nav1.7; Nav1.8; Nav1.9; Nociception; Pain; voltage gated sodium channel

Indexed keywords

CONOTOXIN; LIDOCAINE; MU CONOTOXIN; MU CONOTOXIN BUIIIA; MU CONOTOXIN BUIIIB; MU CONOTOXIN BUIIIC; MU CONOTOXIN CNIIIA; MU CONOTOXIN CNIIIB; MU CONOTOXIN CNIIIC; MU CONOTOXIN GIIIA; MU CONOTOXIN GIIIB; MU CONOTOXIN GIIIC; MU CONOTOXIN KIIIA; MU CONOTOXIN PIIIA; MU CONOTOXIN SIIIA; MU CONOTOXIN SMIIIA; MU CONOTOXIN SXIIIA; MU CONOTOXIN SXIIIB; MU CONOTOXIN TIIIA; MUO CONOTOXIN; MUO CONOTOXIN MFVIA; MUO CONOTOXIN MRVIA; MUO CONOTOXIN MRVIB; OMEGA CONOTOXIN MVIIA; SODIUM CHANNEL NAV1.3; SODIUM CHANNEL NAV1.7; SODIUM CHANNEL NAV1.8; SODIUM CHANNEL NAV1.9; UNCLASSIFIED DRUG; UNINDEXED DRUG; VOLTAGE GATED SODIUM CHANNEL;

EID: 84870567345     PISSN: 20726651     EISSN: None     Source Type: Journal    
DOI: 10.3390/toxins4111236     Document Type: Review
Times cited : (54)

References (146)
  • 1
    • 0032853087 scopus 로고    scopus 로고
    • Ion channels: From idea to reality
    • Hille, B.; Armstrong, C.M.; MacKinnon, R. Ion channels: from idea to reality. Nat. Med. 1999, 5, 1105-1109.
    • (1999) Nat. Med. , vol.5 , pp. 1105-1109
    • Hille, B.1    Armstrong, C.M.2    McKinnon, R.3
  • 3
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J.; Gamal El-Din, T.M.; Scheuer, T.; Zheng, N.; Catterall, W.A. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 2012, 486, 135-139.
    • (2012) Nature , vol.486 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 5
    • 29844438166 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels
    • Catterall, W.A.; Goldin, A.L.; Waxman, S.G. International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels. Pharmacol. Rev. 2005, 57, 397-409.
    • (2005) Pharmacol. Rev. , vol.57 , pp. 397-409
    • Catterall, W.A.1    Goldin, A.L.2    Waxman, S.G.3
  • 6
    • 33646764233 scopus 로고    scopus 로고
    • Marine toxins that target voltage-gated sodium channels
    • Al-Sabi, A.; McArthur, J.; Ostroumov, V.; French, R.J. Marine toxins that target voltage-gated sodium channels. Mar. Drugs 2006, 4, 157-192.
    • (2006) Mar. Drugs , vol.4 , pp. 157-192
    • Al-Sabi, A.1    McArthur, J.2    Ostroumov, V.3    French, R.J.4
  • 7
    • 64149102359 scopus 로고    scopus 로고
    • Interaction between voltage-gated sodium channels and the neurotoxin, tetrodotoxin
    • Lee, C.H.; Ruben, P.C. Interaction between voltage-gated sodium channels and the neurotoxin, tetrodotoxin. Channels (Austin) 2008, 2, 407-412.
    • (2008) Channels (Austin) , vol.2 , pp. 407-412
    • Lee, C.H.1    Ruben, P.C.2
  • 9
    • 0026637366 scopus 로고
    • A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties
    • Satin, J.; Kyle, J.W.; Chen, M.; Bell, P.; Cribbs, L.L.; Fozzard, H.A.; Rogart, R.B. A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties. Science 1992, 256, 1202-1205.
    • (1992) Science , vol.256 , pp. 1202-1205
    • Satin, J.1    Kyle, J.W.2    Chen, M.3    Bell, P.4    Cribbs, L.L.5    Fozzard, H.A.6    Rogart, R.B.7
  • 10
    • 0035139342 scopus 로고    scopus 로고
    • Sodium channel beta subunits: Anything but auxiliary
    • Isom, L.L. Sodium channel beta subunits: anything but auxiliary. Neuroscientist 2011, 7, 42-54.
    • (2011) Neuroscientist , vol.7 , pp. 42-54
    • Isom, L.L.1
  • 11
    • 0035107612 scopus 로고    scopus 로고
    • The intracellular segment of the sodium channel β1 subunit is required for its efficient association with the channel α subunit
    • Meadows, L.; Malhotra, J.D.; Stetzer, A.; Isom, L.L.; Ragsdale, D.S. The intracellular segment of the sodium channel β1 subunit is required for its efficient association with the channel α subunit. J. Neurochem. 2001, 76, 1871-1878.
    • (2001) J. Neurochem. , vol.76 , pp. 1871-1878
    • Meadows, L.1    Malhotra, J.D.2    Stetzer, A.3    Isom, L.L.4    Ragsdale, D.S.5
  • 12
    • 0036898064 scopus 로고    scopus 로고
    • + channels interact with different molecular regions of the β1 subunit
    • + channels interact with different molecular regions of the β1 subunit. J. Gen. Physiol. 2002, 120, 887-895.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 887-895
    • Zimmer, T.1    Benndorf, K.2
  • 14
    • 0037318162 scopus 로고    scopus 로고
    • Antidepressants for chronic neuropathic pain
    • Reisner, L. Antidepressants for chronic neuropathic pain. Curr. Pain Headache Rep. 2003, 7, 24-33.
    • (2003) Curr. Pain Headache Rep. , vol.7 , pp. 24-33
    • Reisner, L.1
  • 15
    • 43549106321 scopus 로고    scopus 로고
    • Prevalence of chronic pain with neuropathic characteristics in the general population
    • Bouhassira, D.; Lantéri-Minet, M.; Attal, N.; Laurent, B.; Touboul, C. Prevalence of chronic pain with neuropathic characteristics in the general population. Pain 2008, 136, 380-387.
    • (2008) Pain , vol.136 , pp. 380-387
    • Bouhassira, D.1    Lantéri-Minet, M.2    Attal, N.3    Laurent, B.4    Touboul, C.5
  • 16
    • 34247233687 scopus 로고    scopus 로고
    • The impact of neuropathic pain on health-related quality of life
    • Jensen, M.P.; Chodroff, M.J.; Dworkin, R.H. The impact of neuropathic pain on health-related quality of life. Neurology 2007, 68, 1178-1182.
    • (2007) Neurology , vol.68 , pp. 1178-1182
    • Jensen, M.P.1    Chodroff, M.J.2    Dworkin, R.H.3
  • 17
    • 77949916692 scopus 로고    scopus 로고
    • Impact of post-therapeutic neuralgia and painful diabetic peripheral neuropathy on health care costs
    • Dworkin, R.H.; Malone, D.C.; Panarites, C.J.; Armstrong, E.P.; Pham, S.V. Impact of post-therapeutic neuralgia and painful diabetic peripheral neuropathy on health care costs. J. Pain. 2010, 11, 360-368.
    • (2010) J. Pain. , vol.11 , pp. 360-368
    • Dworkin, R.H.1    Malone, D.C.2    Panarites, C.J.3    Armstrong, E.P.4    Pham, S.V.5
  • 22
    • 0030997916 scopus 로고    scopus 로고
    • Downregulation of tetrodotoxin-resistant sodium currents and upregulation of a rapidly repriming tetrodotoxin-sensitive sodium current in small spinal sensory neurons after nerve injury
    • Cummins, T.R.; Waxman, S.G. Downregulation of tetrodotoxin-resistant sodium currents and upregulation of a rapidly repriming tetrodotoxin-sensitive sodium current in small spinal sensory neurons after nerve injury. J. Neurosci. 1997, 17, 3503-3514.
    • (1997) J. Neurosci. , vol.17 , pp. 3503-3514
    • Cummins, T.R.1    Waxman, S.G.2
  • 24
    • 0031840375 scopus 로고    scopus 로고
    • Rescue of α-SNS sodium channel expression in small dorsal root ganglion neurons after axotomy by nerve growth factor in vivo
    • Dib-Hajj, S.D.; Black, J.A.; Cummins, T.R.; Kenney, A.M.; Kocsis, J.D.; Waxman, S.G. Rescue of α-SNS sodium channel expression in small dorsal root ganglion neurons after axotomy by nerve growth factor in vivo. J. Neurophysiol. 1998, 79, 2668-2676.
    • (1998) J. Neurophysiol. , vol.79 , pp. 2668-2676
    • Dib-Hajj, S.D.1    Black, J.A.2    Cummins, T.R.3    Kenney, A.M.4    Kocsis, J.D.5    Waxman, S.G.6
  • 25
    • 0032723079 scopus 로고    scopus 로고
    • Plasticity of sodium channel expression in DRG neurons in the chronic constriction injury model of neuropathic pain
    • Dib-Hajj, S.D.; Fjell, J.; Cummins, T.R.; Zheng, Z.; Fried, K.; LaMotte, R.; Black, J.A.; Waxman, S.G. Plasticity of sodium channel expression in DRG neurons in the chronic constriction injury model of neuropathic pain. Pain 1999, 83, 591-600.
    • (1999) Pain , vol.83 , pp. 591-600
    • Dib-Hajj, S.D.1    Fjell, J.2    Cummins, T.R.3    Zheng, Z.4    Fried, K.5    LaMotte, R.6    Black, J.A.7    Waxman, S.G.8
  • 27
    • 0033529191 scopus 로고    scopus 로고
    • + currents and inflammatory hyperalgesia
    • + currents and inflammatory hyperalgesia. Proc. Natl. Acad. Sci. USA 1999, 96, 7645-7649.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7645-7649
    • Gold, M.1
  • 31
    • 84864624177 scopus 로고    scopus 로고
    • Partial nerve injury induces electrophysiological changes in conducting (uninjured) nociceptive and nonnociceptive DRG neurons: Possible relationships to aspects of peripheral neuropathic pain and paresthesias
    • Djouhri, L.; Fang, X.; Koutsikou, S.; Lawson, S.N. Partial nerve injury induces electrophysiological changes in conducting (uninjured) nociceptive and nonnociceptive DRG neurons: Possible relationships to aspects of peripheral neuropathic pain and paresthesias. Pain 2012, 153, 1824-1836.
    • (2012) Pain , vol.153 , pp. 1824-1836
    • Djouhri, L.1    Fang, X.2    Koutsikou, S.3    Lawson, S.N.4
  • 32
    • 0027933696 scopus 로고
    • Type III sodium channel mRNA is expressed in embryonic but not adult spinal sensory neurons, and is re-expressed following axotomy
    • Waxman, S.G.; Kocsis, J.; Black, J.A. Type III sodium channel mRNA is expressed in embryonic but not adult spinal sensory neurons, and is re-expressed following axotomy. J. Neurophysiol. 1994, 72, 466-470.
    • (1994) J. Neurophysiol. , vol.72 , pp. 466-470
    • Waxman, S.G.1    Kocsis, J.2    Black, J.A.3
  • 33
    • 2442651551 scopus 로고    scopus 로고
    • Altered sodium channel expression in second-order spinal sensory neurons contributes to pain after peripheral nerve injury
    • Hains, B.C.; Saab, C.Y.; Klein, J.P.; Craner, M.J.; Waxman, S.G. Altered sodium channel expression in second-order spinal sensory neurons contributes to pain after peripheral nerve injury. J. Neurosci. 2004, 24, 4832-4839.
    • (2004) J. Neurosci. , vol.24 , pp. 4832-4839
    • Hains, B.C.1    Saab, C.Y.2    Klein, J.P.3    Craner, M.J.4    Waxman, S.G.5
  • 34
    • 1542498432 scopus 로고    scopus 로고
    • Changes in the expression of tetrodotoxin-sensitive sodium channels within dorsal root ganglia neurons in inflammatory pain
    • Black, J.A.; Lui, S.; Tanaka, M.; Cummins, T.R.; Waxman, S.G. Changes in the expression of tetrodotoxin-sensitive sodium channels within dorsal root ganglia neurons in inflammatory pain. Pain 2004, 108, 237-247.
    • (2004) Pain , vol.108 , pp. 237-247
    • Black, J.A.1    Lui, S.2    Tanaka, M.3    Cummins, T.R.4    Waxman, S.G.5
  • 35
    • 33749326179 scopus 로고    scopus 로고
    • Upregulation of persistent and ramp sodium current in dorsal horn neurons after spinal cord injury
    • Lampert, A.; Hains, B.C.; Waxman, S.G. Upregulation of persistent and ramp sodium current in dorsal horn neurons after spinal cord injury. Exp. Brain Res. 2006, 174, 660-666.
    • (2006) Exp. Brain Res. , vol.174 , pp. 660-666
    • Lampert, A.1    Hains, B.C.2    Waxman, S.G.3
  • 38
    • 0028588924 scopus 로고
    • Tetrodotoxin-resistant sodium channels
    • Yoshida, S. Tetrodotoxin-resistant sodium channels. Cell. Mol. Neurobiol. 1994, 14, 227-244.
    • (1994) Cell. Mol. Neurobiol. , vol.14 , pp. 227-244
    • Yoshida, S.1
  • 39
    • 55249124953 scopus 로고    scopus 로고
    • Sensory neuron voltage-gated sodium channels as analgesic drug targets
    • Momin, A.; Wood, J.N. Sensory neuron voltage-gated sodium channels as analgesic drug targets. Curr. Opin. Neurobiol. 2008, 18, 383-388.
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 383-388
    • Momin, A.1    Wood, J.N.2
  • 41
    • 0028985863 scopus 로고
    • Structure and functional expression of a new member of the tetrodotoxin-sensitive voltage-activated sodium channel family from human neuroendocrine cells
    • Klugbauer, N.; Lacinova, L.; Flockerzi, V.; Hofmann, F. Structure and functional expression of a new member of the tetrodotoxin-sensitive voltage-activated sodium channel family from human neuroendocrine cells. EMBO J. 1995, 14, 1084-1090.
    • (1995) EMBO J. , vol.14 , pp. 1084-1090
    • Klugbauer, N.1    Lacinova, L.2    Flockerzi, V.3    Hofmann, F.4
  • 42
    • 0031127498 scopus 로고    scopus 로고
    • Sodium channel α-subunit mRNAs I, II, III, NaG, Na6 and hNE (PN1): Different expression patterns in developing rat nervous system
    • Felts, P.A.; Yokoyama, S.; Dib-Hajj, S.; Black, J.A.; Waxman, S.G. Sodium channel α-subunit mRNAs I, II, III, NaG, Na6 and hNE (PN1): different expression patterns in developing rat nervous system. Brain Res. Mol. Brain Res. 1997, 45, 71-82.
    • (1997) Brain Res. Mol. Brain Res. , vol.45 , pp. 71-82
    • Felts, P.A.1    Yokoyama, S.2    Dib-Hajj, S.3    Black, J.A.4    Waxman, S.G.5
  • 45
    • 84865619737 scopus 로고    scopus 로고
    • Recent developments regarding voltage-gated sodium channel blockers for the treatment of inherited and acquired neuropathic pain syndromes
    • Theile, J.W.; Cummins, T.R. Recent developments regarding voltage-gated sodium channel blockers for the treatment of inherited and acquired neuropathic pain syndromes. Front. Pharmacol. 2011, 2, 54.
    • (2011) Front. Pharmacol. , vol.2 , pp. 54
    • Theile, J.W.1    Cummins, T.R.2
  • 47
    • 28244468409 scopus 로고    scopus 로고
    • Erythermalgia: Molecular basis for an inherited pain syndrome
    • Waxman, S.G.; Dib-Hajj, S. Erythermalgia: molecular basis for an inherited pain syndrome. Trends Mol. Med. 2005, 11, 555-562.
    • (2005) Trends Mol. Med. , vol.11 , pp. 555-562
    • Waxman, S.G.1    Dib-Hajj, S.2
  • 52
    • 70149105324 scopus 로고    scopus 로고
    • v1.7 sodium channel blocker reverses hyperalgesia and allodynia on rat models of inflammatory and neuropathic pain
    • v1.7 sodium channel blocker reverses hyperalgesia and allodynia on rat models of inflammatory and neuropathic pain. Anesth. Analg. 2009, 109, 951-958.
    • (2009) Anesth. Analg. , vol.109 , pp. 951-958
    • McGowan, E.1    Hoyt, S.2    Li, X.3    Lyons, K.A.4    Abbadie, C.5
  • 58
    • 0035809303 scopus 로고    scopus 로고
    • Sodium channel β1 and β2 subunits parallel SNS/PN3 α-subunit changes in injured human sensory neurons
    • Coward, K.; Jowett, A.; Plumpton, C.; Powell, A.; Birch, R.; Tate, S.; Bountra, C.; Anand, P. Sodium channel β1 and β2 subunits parallel SNS/PN3 α-subunit changes in injured human sensory neurons. Neuroreport 2001, 12, 483-488.
    • (2001) Neuroreport , vol.12 , pp. 483-488
    • Coward, K.1    Jowett, A.2    Plumpton, C.3    Powell, A.4    Birch, R.5    Tate, S.6    Bountra, C.7    Anand, P.8
  • 64
    • 0036221972 scopus 로고    scopus 로고
    • v1.9 does not change in uninjured primary sensory neurons in experimental neuropathic pain models
    • v1.9 does not change in uninjured primary sensory neurons in experimental neuropathic pain models. Pain 2002, 96, 269-277.
    • (2002) Pain , vol.96 , pp. 269-277
    • Decosterd, I.1    Ji, R.R.2    Abdi, S.3    Tate, S.4    Woolf, C.J.5
  • 66
    • 0033572137 scopus 로고    scopus 로고
    • A novel persistent tetrodotoxin-resistant sodium current in SNS-null and wild-type small primary sensory neurons
    • Cummins, T.R.; Dib-Hajj, S.D.; Black, J.A.; Akopian, A.N.; Wood, J.N.; Waxman, S.G. A novel persistent tetrodotoxin-resistant sodium current in SNS-null and wild-type small primary sensory neurons. J. Neurosci. 1999, 19, RC43.
    • (1999) J. Neurosci. , vol.19
    • Cummins, T.R.1    Dib-Hajj, S.D.2    Black, J.A.3    Akopian, A.N.4    Wood, J.N.5    Waxman, S.G.6
  • 67
    • 0034843601 scopus 로고    scopus 로고
    • + current affects resting potential and response to depolarization in simulated spinal sensory neurons
    • + current affects resting potential and response to depolarization in simulated spinal sensory neurons. J. Neurophysiol. 2001, 86, 1351-1364.
    • (2001) J. Neurophysiol. , vol.86 , pp. 1351-1364
    • Herzog, R.I.1    Cummins, T.R.2    Waxman, S.G.3
  • 71
    • 79955878897 scopus 로고    scopus 로고
    • v1.9, generates inhibitory effects on complete Freund's adjuvant-induced inflammatory pain in rat
    • v1.9, generates inhibitory effects on complete Freund's adjuvant-induced inflammatory pain in rat. PLoS One 2011, 6, e19865.
    • (2011) PLoS One , vol.6
    • Yu, Y.Q.1    Zhao, F.2    Guan, S.M.3    Chen, J.4
  • 72
    • 0036930324 scopus 로고    scopus 로고
    • Conus venom peptides: Reflections from the biology of clades and species
    • Oliver, B.M. Conus venom peptides: reflections from the biology of clades and species. Annu. Rev. Ecol. Syst. 2002, 33, 25-47.
    • (2002) Annu. Rev. Ecol. Syst. , vol.33 , pp. 25-47
    • Oliver, B.M.1
  • 73
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • Terlau, H.; Oliver, 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    Oliver, B.M.2
  • 74
    • 0014250201 scopus 로고
    • Report of fatal cone shell sting by Conus geographus Linnaeus
    • Rice, R.D.; Halstead, B.W. Report of fatal cone shell sting by Conus geographus Linnaeus. Toxicon 1968, 5, 223-224.
    • (1968) Toxicon , vol.5 , pp. 223-224
    • Rice, R.D.1    Halstead, B.W.2
  • 75
    • 67349175001 scopus 로고    scopus 로고
    • Remarkable inter-and intra-species complexity of conotoxins revealed by LC/MS
    • Davis, J.; Jones, A.; Lewis, R.J. Remarkable inter-and intra-species complexity of conotoxins revealed by LC/MS. Peptides 2009, 30, 1222-1227.
    • (2009) Peptides , vol.30 , pp. 1222-1227
    • Davis, J.1    Jones, A.2    Lewis, R.J.3
  • 76
    • 0036141825 scopus 로고    scopus 로고
    • Electrostatic and steric contributions to block of the skeletal muscle sodium channel by μ-conotoxin
    • Hui, K.; Lipkind, G.; Fozzard, H.A.; French, R.J. Electrostatic and steric contributions to block of the skeletal muscle sodium channel by μ-conotoxin. J. Gen. Physiol. 2002, 119, 45-54.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 45-54
    • Hui, K.1    Lipkind, G.2    Fozzard, H.A.3    French, R.J.4
  • 79
    • 36248939803 scopus 로고    scopus 로고
    • Isolation and characterization of a T-superfamily conotoxin from Conus litteratus with targeting tetrodotoxin-sensitive sodium channels
    • Liu, J.; Wu, Q.; Pi, C.; Zhao, Y.; Zhou, M.; Wang, L.; Chen, S.; Xu, A. Isolation and characterization of a T-superfamily conotoxin from Conus litteratus with targeting tetrodotoxin-sensitive sodium channels. Peptides 2007, 28, 2313-2319.
    • (2007) Peptides , vol.28 , pp. 2313-2319
    • Liu, J.1    Wu, Q.2    Pi, C.3    Zhao, Y.4    Zhou, M.5    Wang, L.6    Chen, S.7    Xu, A.8
  • 80
    • 21844466444 scopus 로고    scopus 로고
    • Molecular interaction of 8-conotoxins with voltage-gated sodium channels
    • Leipold, E.; Hansel, A.; Olivera, B.M.; Terlau, H.; Heinemann, S.H. Molecular interaction of 8-conotoxins with voltage-gated sodium channels. FEBS Lett. 2005, 579, 3881-3884.
    • (2005) FEBS Lett. , vol.579 , pp. 3881-3884
    • Leipold, E.1    Hansel, A.2    Olivera, B.M.3    Terlau, H.4    Heinemann, S.H.5
  • 81
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik, D.J.; Daly, N.L.; Waine, C. The cystine knot motif in toxins and implications for drug design. Toxicon 2001, 39, 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 83
    • 0028922707 scopus 로고
    • Alterations of voltage-activated sodium current by a novel conotoxin from the venom of Conus gloriamaris
    • Hasson, A.; Shon, K.J.; Olivera, B.M.; Spira, M.E. Alterations of voltage-activated sodium current by a novel conotoxin from the venom of Conus gloriamaris. J. Neurophysiol. 1995, 73, 1295-1301.
    • (1995) J. Neurophysiol. , vol.73 , pp. 1295-1301
    • Hasson, A.1    Shon, K.J.2    Olivera, B.M.3    Spira, M.E.4
  • 84
    • 0029826273 scopus 로고    scopus 로고
    • Interactions of 8-conotoxins with alkaloid neurotoxins reveal differences between the silent and effective binding sites on voltage-sensitive sodium channels
    • Shichor, I.; Fainzilber, M.; Pelhate, M.; Malecot, C.O.; Zlotkin, E.; Gordon, D. Interactions of 8-conotoxins with alkaloid neurotoxins reveal differences between the silent and effective binding sites on voltage-sensitive sodium channels. J. Neurochem. 1996, 167, 2451-2460.
    • (1996) J. Neurochem. , vol.167 , pp. 2451-2460
    • Shichor, I.1    Fainzilber, M.2    Pelhate, M.3    Malecot, C.O.4    Zlotkin, E.5    Gordon, D.6
  • 87
    • 18844443166 scopus 로고    scopus 로고
    • Solution structure of δ-Am2766: A highly hydrophobic δ-conotoxin from Conus amadis that inhibits inactivation of neuronal Voltage-gated sodium channels
    • Sarma, S.P.; Kumar, G.S.; Sudarslal, S.; Iengar, P.; Ramasamy, P.; Sikdar, S.K.; Krishnan, K.S.; Balaram, P. Solution structure of δ-Am2766: a highly hydrophobic δ-conotoxin from Conus amadis that inhibits inactivation of neuronal voltage-gated sodium channels. Chem. Biodivers. 2005, 2, 535-556.
    • (2005) Chem. Biodivers. , vol.2 , pp. 535-556
    • Sarma, S.P.1    Kumar, G.S.2    Sudarslal, S.3    Iengar, P.4    Ramasamy, P.5    Sikdar, S.K.6    Krishnan, K.S.7    Balaram, P.8
  • 88
    • 70349623944 scopus 로고    scopus 로고
    • Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents
    • Wang, L.; Lui, J.; Pi, C.; Zeng, X.; Zhou, M.; Jiang, X.; Chen, S.; Ren, Z.; Xu, A. Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents. Arch. Toxicol. 2009, 83, 925-932.
    • (2009) Arch. Toxicol. , vol.83 , pp. 925-932
    • Wang, L.1    Lui, J.2    Pi, C.3    Zeng, X.4    Zhou, M.5    Jiang, X.6    Chen, S.7    Ren, Z.8    Xu, A.9
  • 91
    • 0017567302 scopus 로고
    • Characterization of the neurotoxic constituents of Conus geographus (L) venom
    • Spence, I.; Gillessen, D.; Gregson, R.P.; Quinn, R.J. Characterization of the neurotoxic constituents of Conus geographus (L) venom. Life Sci. 1977, 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
  • 93
    • 0026657359 scopus 로고
    • Action of derivatives of μ-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates
    • Becker, S.; Prusak-Sochaczewski, E.; Zamponi, G.; Beck-Sickinger, A.G.; Gordon, R.D.; French, R.J. Action of derivatives of μ-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry 1992, 31, 8229-8238.
    • (1992) Biochemistry , vol.31 , pp. 8229-8238
    • Becker, S.1    Prusak-Sochaczewski, E.2    Zamponi, G.3    Beck-Sickinger, A.G.4    Gordon, R.D.5    French, R.J.6
  • 94
    • 0027078665 scopus 로고
    • Structure-activity relationships of μ-conotoxin GIIIA: Structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations
    • Wakamatsu, K.; Kohda, D.; Hatanaka, H.; Lancelin, J.M.; Ishida, Y.; Oya, M.; Nakamura, H.; Inagaki, F.; Sato, K. Structure-activity relationships of μ-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry 1992, 31, 12577-12584.
    • (1992) Biochemistry , vol.31 , pp. 12577-12584
    • Wakamatsu, K.1    Kohda, D.2    Hatanaka, H.3    Lancelin, J.M.4    Ishida, Y.5    Oya, M.6    Nakamura, H.7    Inagaki, F.8    Sato, K.9
  • 95
    • 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.; Craik, D.J. Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels. Biochemistry 1996, 35, 8824-8835.
    • (1996) Biochemistry , vol.35 , pp. 8824-8835
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 100
    • 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.; Simgh, 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    Simgh, G.2    McMaster, D.3    Winkfein, R.4    Tieleman, D.P.5    French, R.J.6
  • 102
    • 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
  • 104
    • 79957868138 scopus 로고    scopus 로고
    • Molecular determinants for the subtype specificity of μ-conotoxin SIIIA targeting neuronal voltage-gated sodium channels
    • Leipold, E.; Markgraf, R.; Miloslavina, A.; Kijas, M.; Schirmeyer, J.; Imhof, D.; Heinemann, S.H. Molecular determinants for the subtype specificity of μ-conotoxin SIIIA targeting neuronal voltage-gated sodium channels. Neuropharmacology 2011, 61, 105-111.
    • (2011) Neuropharmacology , vol.61 , pp. 105-111
    • Leipold, E.1    Markgraf, R.2    Miloslavina, A.3    Kijas, M.4    Schirmeyer, J.5    Imhof, D.6    Heinemann, S.H.7
  • 105
    • 53749086169 scopus 로고    scopus 로고
    • Structure, dynamics, and selectivity of the sodium channel blocker μ-conotoxin SIIIA
    • Yao, S.; Zhang, M.M.; Yoshikami, D.; Azam, L.; Olivera, B.M.; Bulaj, G.; Norton, R.S. Structure, dynamics, and selectivity of the sodium channel blocker μ-conotoxin SIIIA. Biochemistry 2008, 47, 10940-10949.
    • (2008) Biochemistry , vol.47 , pp. 10940-10949
    • Yao, S.1    Zhang, M.M.2    Yoshikami, D.3    Azam, L.4    Olivera, B.M.5    Bulaj, G.6    Norton, R.S.7
  • 106
    • 78650902764 scopus 로고    scopus 로고
    • Multiple, distributed interactions of μ-conotoxin PIIIA associated with broad targeting among voltage-gated sodium channels
    • McArthur, J.R.; Ostroumov, V.; Al-Sabi, A.; McMaster, D.; French, R.J. Multiple, distributed interactions of μ-conotoxin PIIIA associated with broad targeting among voltage-gated sodium channels. Biochemistry 2011, 50, 116-124.
    • (2011) Biochemistry , vol.50 , pp. 116-124
    • McArthur, J.R.1    Ostroumov, V.2    Al-Sabi, A.3    McMaster, D.4    French, R.J.5
  • 109
    • 52949118506 scopus 로고    scopus 로고
    • Conus venoms-a rich source of peptide-based therapeutics
    • Han, T.S.; Teichert, R.W.; Olivera, B.M.; Bulaj, G. Conus venoms-a rich source of peptide-based therapeutics. Curr. Pharm. Des. 2008, 14, 2462-2479.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 2462-2479
    • Han, T.S.1    Teichert, R.W.2    Olivera, B.M.3    Bulaj, G.4
  • 110
  • 115
    • 61949466107 scopus 로고    scopus 로고
    • Integrated oxidative folding of cysteine/selenocysteine containing peptides: Improving chemical synthesis of conotoxins
    • Walewska, A.; Zhang, M.M.; Skalicky, J.J.; Yoshikami, D.; Olivera, B.M.; Bulaj, G. Integrated oxidative folding of cysteine/selenocysteine containing peptides: improving chemical synthesis of conotoxins. Angew. Chem. Int. Ed. Engl. 2009, 48, 2221-2224.
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 2221-2224
    • Walewska, A.1    Zhang, M.M.2    Skalicky, J.J.3    Yoshikami, D.4    Olivera, B.M.5    Bulaj, G.6
  • 117
    • 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
  • 120
    • 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
  • 121
    • 84864524648 scopus 로고    scopus 로고
    • N-and C-terminal extensions of μ-conotoxins increase potency and selectivity for neuronal sodium channels
    • Schroeder, C.I.; Adams, D.; Thomas, L.; Alewood, P.F.; Lewis, R.J. N-and C-terminal extensions of μ-conotoxins increase potency and selectivity for neuronal sodium channels. Biopolymers 2012, 98, 161-165.
    • (2012) Biopolymers , vol.98 , pp. 161-165
    • Schroeder, C.I.1    Adams, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5
  • 125
    • 2942554865 scopus 로고    scopus 로고
    • Structures of μO-conotoxins from Conus marmoreus. Inhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons
    • Daly, N.L.; Ekberg, J.A.; Thomas, L.; Adams, D.J.; Lewis, R.J.; Craik, D.J. Structures of μO-conotoxins from Conus marmoreus. Inhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons. J. Biol. Chem. 2004, 279, 25774-25782.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25774-25782
    • Daly, N.L.1    Ekberg, J.A.2    Thomas, L.3    Adams, D.J.4    Lewis, R.J.5    Craik, D.J.6
  • 126
    • 0029658417 scopus 로고    scopus 로고
    • μO-conotoxin MrVIA inhibits mammalian sodium channels, but not through site I
    • Terlau, H.; Stocker, M.; Shon, K.J.; McIntosh, J.M.; Olivera, B.M. μO-conotoxin MrVIA inhibits mammalian sodium channels, but not through site I. J. Neurophysiol. 1996, 76, 1423-1429.
    • (1996) J. Neurophysiol. , vol.76 , pp. 1423-1429
    • Terlau, H.1    Stocker, M.2    Shon, K.J.3    McIntosh, J.M.4    Olivera, B.M.5
  • 128
    • 32344433189 scopus 로고    scopus 로고
    • The μO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3
    • Zorn, S.; Leipold, E.; Hansel, A.; Bulaj, G.; Olivera, B.M.; Terlau, H.; Heinemann, S.H. The μO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3. FEBS Lett. 2006, 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
  • 130
    • 79960271986 scopus 로고    scopus 로고
    • Functional properties and toxin pharmacology of a dorsal root ganglion sodium channel viewed through its voltage sensors
    • Bosmans, F.; Puopolo, M.; Martin-Eauclaire, M.F.; Bean, B.P.; Swartz, K.J. Functional properties and toxin pharmacology of a dorsal root ganglion sodium channel viewed through its voltage sensors. J. Gen. Physiol. 2011, 138, 59-72.
    • (2011) J. Gen. Physiol. , vol.138 , pp. 59-72
    • Bosmans, F.1    Puopolo, M.2    Martin-Eauclaire, M.F.3    Bean, B.P.4    Swartz, K.J.5
  • 131
    • 56249091754 scopus 로고    scopus 로고
    • Deconstructing voltage sensor function and pharmacology in sodium channels
    • Bosmans, F.; Martin-Eauclaire, M.F.; Swartz, K.J. Deconstructing voltage sensor function and pharmacology in sodium channels. Nature 2008, 456, 202-208.
    • (2008) Nature , vol.456 , pp. 202-208
    • Bosmans, F.1    Martin-Eauclaire, M.F.2    Swartz, K.J.3
  • 132
    • 77950515381 scopus 로고    scopus 로고
    • Targeting voltage sensors in sodium channels with spider toxins
    • Bosmans, F.; Swartz, K.J. Targeting voltage sensors in sodium channels with spider toxins. Trends Pharmacol. Sci. 2010, 31, 175-182.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 175-182
    • Bosmans, F.1    Swartz, K.J.2
  • 133
    • 84864135552 scopus 로고    scopus 로고
    • Isolation, characterization and total regioselective synthesis of the novel μO-conotoxin MfVIA from Conus magnificus that targets voltage-gated sodium channels
    • Vetter, I.; Dekan, Z.; Knapp, O.; Adams, D.J.; Alewood, P.F.; Lewis, R.J. Isolation, characterization and total regioselective synthesis of the novel μO-conotoxin MfVIA from Conus magnificus that targets voltage-gated sodium channels. Biochem. Pharmacol. 2012, 4, 540-548.
    • (2012) Biochem. Pharmacol. , vol.4 , pp. 540-548
    • Vetter, I.1    Dekan, Z.2    Knapp, O.3    Adams, D.J.4    Alewood, P.F.5    Lewis, R.J.6
  • 135
    • 33845761868 scopus 로고    scopus 로고
    • Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from
    • Pi, C.; Lui, J.; Wang, L.; Jiang, X.; Liu, Y.; Peng, C.; Chen, S.; Xu, A. Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from Conus litteratus. J. Biotechnol. 2007, 128, 184-193.
    • (2007) Conus litteratus. J. Biotechnol. , vol.128 , pp. 184-193
    • Pi, C.1    Lui, J.2    Wang, L.3    Jiang, X.4    Liu, Y.5    Peng, C.6    Chen, S.7    Xu, A.8
  • 139
    • 33748703289 scopus 로고    scopus 로고
    • Neuronal voltage-gated sodium channel subtypes: Key roles in inflammatory and neuropathic pain
    • Ekberg, J.; Adams, D.J. Neuronal voltage-gated sodium channel subtypes: key roles in inflammatory and neuropathic pain. Int. J. Biochem. Cell. Biol. 2006, 38, 2005-2010.
    • (2006) Int. J. Biochem. Cell. Biol. , vol.38 , pp. 2005-2010
    • Ekberg, J.1    Adams, D.J.2
  • 140
    • 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
  • 142
    • 20444477528 scopus 로고    scopus 로고
    • A toxin against pain
    • Stix, G. A toxin against pain. Sci. Am. 2005, 292, 70-75.
    • (2005) Sci. Am. , vol.292 , pp. 70-75
    • Stix, G.1
  • 144
    • 40849142344 scopus 로고    scopus 로고
    • Inhibition of sodium channel gating by trapping the domain II voltage sensor with protoxin II
    • Sokolov, S.; Kraus, R.L.; Scheuer, T.; Catterall, W.A. Inhibition of sodium channel gating by trapping the domain II voltage sensor with protoxin II. Mol. Pharmacol. 2008, 73, 1020-1028.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1020-1028
    • Sokolov, S.1    Kraus, R.L.2    Scheuer, T.3    Catterall, W.A.4


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