메뉴 건너뛰기




Volumn 24, Issue 3-4, 2005, Pages 289-312

Precious natural peptides from spider venoms: New tools for studying potassium channels

Author keywords

Animal toxins; Gating modifiers; Inhibitor cystine knot molecules; Spider peptides

Indexed keywords

CYSTINE; DISULFIDE; PEPTIDE; POTASSIUM CHANNEL; SPIDER VENOM;

EID: 27544476433     PISSN: 07313837     EISSN: 15256057     Source Type: Journal    
DOI: 10.1080/07313830500237059     Document Type: Review
Times cited : (4)

References (83)
  • 2
    • 0035863820 scopus 로고    scopus 로고
    • Selective blocking of voltage-gated K+ channels improves experimental autoimmune encephalomyelitis and inhibits T cell activation
    • Beeton, C., Barbaria, J., Girand, P., Devaux, J., Benoliel, A. M., Gola, M., Sabatier, J. M., Bernard, D., Crest, M., Beraud, E. (2001). Selective blocking of voltage-gated K+ channels improves experimental autoimmune encephalomyelitis and inhibits T cell activation. J. Immunol 166(2):936-944.
    • (2001) J. Immunol. , vol.166 , Issue.2 , pp. 936-944
    • Beeton, C.1    Barbaria, J.2    Girand, P.3    Devaux, J.4    Benoliel, A.M.5    Gola, M.6    Sabatier, J.M.7    Bernard, D.8    Crest, M.9    Beraud, E.10
  • 3
    • 0037646521 scopus 로고    scopus 로고
    • A novel fluorescent toxin to detect and investigate Kvl.3 channel up-regulation in chronically activated T lymphocytes
    • Beeton, C., Wulff, H., Singh, S., Botsko, S., Crossley, G., Gutman, G. A., Cahalan, M. D., Pennington, M., Chandy, K. G. (2003). A novel fluorescent toxin to detect and investigate Kvl.3 channel up-regulation in chronically activated T lymphocytes. J. Biol. Chem. 278(11):9928-9937.
    • (2003) J. Biol. Chem. , vol.278 , Issue.11 , pp. 9928-9937
    • Beeton, C.1    Wulff, H.2    Singh, S.3    Botsko, S.4    Crossley, G.5    Gutman, G.A.6    Cahalan, M.D.7    Pennington, M.8    Chandy, K.G.9
  • 4
    • 0034489434 scopus 로고    scopus 로고
    • Solution structure of hpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel
    • Bernard, C., Legros, C., Ferrat, G., Bischoff, U., Marquardt, A., Pongs, O., Darbon, H. (2000). Solution structure of hpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel. Protein Sci. 9(11):2059-2067.
    • (2000) Protein Sci. , vol.9 , Issue.11 , pp. 2059-2067
    • Bernard, C.1    Legros, C.2    Ferrat, G.3    Bischoff, U.4    Marquardt, A.5    Pongs, O.6    Darbon, H.7
  • 5
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla, F. (2000). The voltage sensor in voltage-dependent ion channels. Physiol Rev. 80(2):555-592.
    • (2000) Physiol Rev. , vol.80 , Issue.2 , pp. 555-592
    • Bezanilla, F.1
  • 6
    • 0024410660 scopus 로고
    • Analogies and differences in the mode of action and properties of binding sites (localization and mutual interactions) of two K+ channel toxins, MCD peptide and dendrotoxin 1
    • Bidard, J. N., Mourre, C., Gandolfo, G., Schweitz, H., Widmann, C., Gottesmann, C., Lazdunski, M. (1989). Analogies and differences in the mode of action and properties of binding sites (localization and mutual interactions) of two K+ channel toxins, MCD peptide and dendrotoxin 1. Brain Res. 495(1):45-57.
    • (1989) Brain Res. , vol.495 , Issue.1 , pp. 45-57
    • Bidard, J.N.1    Mourre, C.2    Gandolfo, G.3    Schweitz, H.4    Widmann, C.5    Gottesmann, C.6    Lazdunski, M.7
  • 8
    • 0034950016 scopus 로고    scopus 로고
    • Interaction of SNX482 vvitli domains III and IV inhibits activation gating of alpha(1E) [Ca(V)2.3] calcium channels
    • Bourinet, E., Stotz, S. C., Spaetgens, R. L., Dayanithi, G., Lemos, J., Nargeot, J., Zamponi, G. W. (2001). Interaction of SNX482 vvitli domains III and IV inhibits activation gating of alpha(1E) [Ca(V)2.3] calcium channels. Biophys. J. 81(1):79-88.
    • (2001) Biophys. J. , vol.81 , Issue.1 , pp. 79-88
    • Bourinet, E.1    Stotz, S.C.2    Spaetgens, R.L.3    Dayanithi, G.4    Lemos, J.5    Nargeot, J.6    Zamponi, G.W.7
  • 10
    • 0032191111 scopus 로고    scopus 로고
    • Voltage sensor-trapping: Enhanced activation of sodium channels by beta-scorpion toxin bound to the S3-S4 loop in domain II
    • Cestele, S., Qu, Y, Rogers, J. C., Rochat, H., Scheuer, T., Catterall, W. A. (1998). Voltage sensor-trapping: enhanced activation of sodium channels by beta-scorpion toxin bound to the S3-S4 loop in domain II. Neuron 21(4):919-931.
    • (1998) Neuron , vol.21 , Issue.4 , pp. 919-931
    • Cestele, S.1    Qu, Y.2    Rogers, J.C.3    Rochat, H.4    Scheuer, T.5    Catterall, W.A.6
  • 11
    • 16444376665 scopus 로고    scopus 로고
    • Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: A new fold for an HERG toxin
    • in press
    • Chagot, B., Diochot, S., Pimentel, C., Lazdunski, M., Darbon, H. (2005). Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: A new fold for an HERG toxin. Proteins in press
    • (2005) Proteins
    • Chagot, B.1    Diochot, S.2    Pimentel, C.3    Lazdunski, M.4    Darbon, H.5
  • 12
    • 1942441447 scopus 로고    scopus 로고
    • Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus
    • Chagot, B., Escoubas, P., Villegas, E., Bernard, C., Ferrat, G., Corzo, G., Lazdunski, M., Darbon, H. (2004). Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus. Protein Sci. 13(5):1197-1208.
    • (2004) Protein Sci. , vol.13 , Issue.5 , pp. 1197-1208
    • Chagot, B.1    Escoubas, P.2    Villegas, E.3    Bernard, C.4    Ferrat, G.5    Corzo, G.6    Lazdunski, M.7    Darbon, H.8
  • 14
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik, D. J., Daly, N. L., 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
  • 16
    • 0032921154 scopus 로고    scopus 로고
    • Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Itol in cardiac electrogenesis. Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4
    • Diochot, S., Drici, M. D., Moinier, D., Fink, M., Lazdunski, M., Schweitz, H., Beress, L. (1999). Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Itol in cardiac electrogenesis. Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. Br. J. Pharmacol. 126(1):251-263.
    • (1999) Br. J. Pharmacol. , vol.126 , Issue.1 , pp. 251-263
    • Diochot, S.1    Drici, M.D.2    Moinier, D.3    Fink, M.4    Lazdunski, M.5    Schweitz, H.6    Beress, L.7
  • 17
    • 0037899621 scopus 로고    scopus 로고
    • APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels
    • Diochot, S., Loret, E., Bruhn, T., Beress, L., Lazdunski, M. (2003). APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol. Pharmacol 64(1):59-69.
    • (2003) Mol. Pharmacol , vol.64 , Issue.1 , pp. 59-69
    • Diochot, S.1    Loret, E.2    Bruhn, T.3    Beress, L.4    Lazdunski, M.5
  • 18
    • 0032549630 scopus 로고    scopus 로고
    • Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4
    • Diochot, S., Schweitz, H., Beress, L., Lazdunski, M. (1998). Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol. Chem. 273(12):6744-6749.
    • (1998) J Biol. Chem. , vol.273 , Issue.12 , pp. 6744-6749
    • Diochot, S.1    Schweitz, H.2    Beress, L.3    Lazdunski, M.4
  • 20
    • 2942650423 scopus 로고    scopus 로고
    • Modulation of Kv4.2 channels by a peptide isolated from the venom of the giant bird-eating tarantula Theraphosa leblondi
    • Ebbinghaus, J., Legros, C., Nolting, A., Guette, C., Celerier, M. L., Pongs, O., Bahring, R. (2004). Modulation of Kv4.2 channels by a peptide isolated from the venom of the giant bird-eating tarantula Theraphosa leblondi. Toxicon 43(8):923-932.
    • (2004) Toxicon , vol.43 , Issue.8 , pp. 923-932
    • Ebbinghaus, J.1    Legros, C.2    Nolting, A.3    Guette, C.4    Celerier, M.L.5    Pongs, O.6    Bahring, R.7
  • 21
    • 0036088553 scopus 로고    scopus 로고
    • Novel tarantula toxins for subtypes of voltage-dependent potassium channels in tbe Kv2 and Kv4 subfamilies
    • Escoubas, R, Diochot, S., Celerier, M. L., Nakajima, T., Lazdunski, M. (2002). Novel tarantula toxins for subtypes of voltage-dependent potassium channels in tbe Kv2 and Kv4 subfamilies. Mol. Pharmacol. 62(1):48-57.
    • (2002) Mol. Pharmacol. , vol.62 , Issue.1 , pp. 48-57
    • Escoubas, R.1    Diochot, S.2    Celerier, M.L.3    Nakajima, T.4    Lazdunski, M.5
  • 22
    • 0033731951 scopus 로고    scopus 로고
    • Structure and pharmacology of spider venom neurotoxins
    • Escoubas, P., Diochot, S., Corzo, G. (2000). Structure and pharmacology of spider venom neurotoxins. Biochimie 82(9-10):893-907.
    • (2000) Biochimie , vol.82 , Issue.9-10 , pp. 893-907
    • Escoubas, P.1    Diochot, S.2    Corzo, G.3
  • 23
    • 1942438962 scopus 로고    scopus 로고
    • Tarantulas: Eight-legged pharmacists and combinatorial chemists
    • Escoubas, P., Rash, L. (2004). Tarantulas: eight-legged pharmacists and combinatorial chemists. Toxicon 43(5):555-574.
    • (2004) Toxicon , vol.43 , Issue.5 , pp. 555-574
    • Escoubas, P.1    Rash, L.2
  • 24
    • 0035184148 scopus 로고    scopus 로고
    • Potassium channels: From scorpion venoms to high-resolution structure
    • Garcia, M. L., Gao, Y., McManus, O. B., Kaczorowski, G. J. (2001). Potassium channels: from scorpion venoms to high-resolution structure. Toxicon 39(6):739-748.
    • (2001) Toxicon , vol.39 , Issue.6 , pp. 739-748
    • Garcia, M.L.1    Gao, Y.2    McManus, O.B.3    Kaczorowski, G.J.4
  • 25
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • Hidalgo, P., MacKinnon, R. (1995). Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor. Science 268(5208):307-310.
    • (1995) Science , vol.268 , Issue.5208 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 26
    • 0025996129 scopus 로고
    • Identification of amino acid residues involved in dendrotoxin block of rat voltage-dependent potassium channels
    • Hurst, R. S., Busch, A. E., Kavanaugh, M. P., Osborne, P. B., North, R. A., Adelman, J. P. (1991). Identification of amino acid residues involved in dendrotoxin block of rat voltage-dependent potassium channels. Mol. Pharmacol 40(4):572-576.
    • (1991) Mol. Pharmacol. , vol.40 , Issue.4 , pp. 572-576
    • Hurst, R.S.1    Busch, A.E.2    Kavanaugh, M.P.3    Osborne, P.B.4    North, R.A.5    Adelman, J.P.6
  • 27
    • 0027400860 scopus 로고
    • Contrasting immunohistochemical localizations in rat brain of two novel K+ channels of the Shab subfamily
    • Hwang, P. M., Fotuhi, M., Bredt, D. S., Cunningham, A. M., Snyder, S. H. (1993). Contrasting immunohistochemical localizations in rat brain of two novel K+ channels of the Shab subfamily. J. Neurosci 13(4):1569-1576.
    • (1993) J. Neurosci. , vol.13 , Issue.4 , pp. 1569-1576
    • Hwang, P.M.1    Fotuhi, M.2    Bredt, D.S.3    Cunningham, A.M.4    Snyder, S.H.5
  • 28
    • 1942470956 scopus 로고    scopus 로고
    • Clinical consequences of spider bites: Recent advances in our understanding
    • Isbister, G. K., White, J. (2004). Clinical consequences of spider bites: recent advances in our understanding. Toxicon 43(5):477-492.
    • (2004) Toxicon , vol.43 , Issue.5 , pp. 477-492
    • Isbister, G.K.1    White, J.2
  • 29
    • 0031465024 scopus 로고    scopus 로고
    • Voltage-gated and inwardly rectifying potassium channels
    • Jan, L. Y., Jan, Y. N. (1997). Voltage-gated and inwardly rectifying potassium channels. J. Physiol 505(Pt 2):267-282.
    • (1997) J. Physiol. , vol.505 , Issue.PART 2 , pp. 267-282
    • Jan, L.Y.1    Jan, Y.N.2
  • 30
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., MacKinnon, R. (2002). Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417(6888):515-522.
    • (2002) Nature , vol.417 , Issue.6888 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 32
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K+ channel
    • Jiang, Y., Ruta, V., Chen, J., Lee, A., MacKinnon, R. (2003b). The principle of gating charge movement in a voltage-dependent K+ channel. Nature 423(6935):42-48.
    • (2003) Nature , vol.423 , Issue.6935 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    MacKinnon, R.5
  • 33
    • 0037155771 scopus 로고    scopus 로고
    • Reduction of 1(to) causes hypertrophy in neonatal rat ventricular myocytes
    • Kassiri, Z., Zobel, C., Nguyen, T. T., Molkentin, J. D., Backx, P. H. (2002). Reduction of 1(to) causes hypertrophy in neonatal rat ventricular myocytes, Circ. Res. 90(5):578-585.
    • (2002) Circ. Res. , vol.90 , Issue.5 , pp. 578-585
    • Kassiri, Z.1    Zobel, C.2    Nguyen, T.T.3    Molkentin, J.D.4    Backx, P.H.5
  • 37
    • 0344256589 scopus 로고    scopus 로고
    • Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels
    • Lee, H. C., Wang, J. M., Swartz, K. J. (2003). Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels. Neuron 40(3):527-536.
    • (2003) Neuron , vol.40 , Issue.3 , pp. 527-536
    • Lee, H.C.1    Wang, J.M.2    Swartz, K.J.3
  • 38
    • 0032555210 scopus 로고    scopus 로고
    • Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels
    • Li-Smerin, Y., Swartz, K. J. (1998), Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels. Proc. Natl. Acad. Sci. USA 95(15):8585-8589.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.15 , pp. 8585-8589
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 39
    • 0034130607 scopus 로고    scopus 로고
    • Localization and molecular determinants of the Hanatoxin receptors on the voltage-sensing domains of a K(+) channel
    • Li-Smerin, Y., Swartz, K. J. (2000). Localization and molecular determinants of the Hanatoxin receptors on the voltage-sensing domains of a K(+) channel. J. Gen. Physiol, 115(6):673-684.
    • (2000) J. Gen. Physiol. , vol.115 , Issue.6 , pp. 673-684
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 40
    • 0035023528 scopus 로고    scopus 로고
    • Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels
    • Li-Smerin, Y., Swartz, K. J. (2001). Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels. J. Gen. Physiol. 117(3):205-218.
    • (2001) J. Gen. Physiol. , vol.117 , Issue.3 , pp. 205-218
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 41
    • 0142177158 scopus 로고    scopus 로고
    • A possible molecular mechanism of hanatoxin binding-modified gating in voltage-gated K+-channels
    • Lou, K. L., Huang, P. T., Shiau, Y. S., Liaw, Y. C., Shiau, Y. Y., Liou, H. H. (2003). A possible molecular mechanism of hanatoxin binding-modified gating in voltage-gated K+-channels. J. Mol. Recognit. 16(6):392-395.
    • (2003) J. Mol. Recognit. , vol.16 , Issue.6 , pp. 392-395
    • Lou, K.L.1    Huang, P.T.2    Shiau, Y.S.3    Liaw, Y.C.4    Shiau, Y.Y.5    Liou, H.H.6
  • 42
    • 0036630111 scopus 로고    scopus 로고
    • Molecular determinants of the hanatoxin binding in voltage-gated K+-channel drk1
    • Lou, K. L., Huang, P. T., Shiau, Y. S., Shiau, Y. Y. (2002). Molecular determinants of the hanatoxin binding in voltage-gated K+-channel drk1. J. Mol. Recognit. 15(4):175-179.
    • (2002) J. Mol. Recognit. , vol.15 , Issue.4 , pp. 175-179
    • Lou, K.L.1    Huang, P.T.2    Shiau, Y.S.3    Shiau, Y.Y.4
  • 43
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon, R. (1991). Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature 350(6315):232-235.
    • (1991) Nature , vol.350 , Issue.6315 , pp. 232-235
    • MacKinnon, R.1
  • 44
    • 0025644364 scopus 로고
    • Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor
    • MacKinnon, R., Heginbotham, L., Abramson, T. (1990). Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor. Neuron 5(6):767-771.
    • (1990) Neuron , vol.5 , Issue.6 , pp. 767-771
    • MacKinnon, R.1    Heginbotham, L.2    Abramson, T.3
  • 45
    • 0024426645 scopus 로고
    • Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor
    • MacKinnon, R., Miller, C. (1989). Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor. Science 245(4924):1382-1385.
    • (1989) Science , vol.245 , Issue.4924 , pp. 1382-1385
    • MacKinnon, R.1    Miller, C.2
  • 46
    • 0033570060 scopus 로고    scopus 로고
    • Isolation, amino acid sequence and functional assays of SGTx1. The first toxin purified from the venom of the spider scodra griseipes
    • Marvin, L., De, E., Cosette, P., Gagnon, J., Molle, G., Lange, C. (1999). Isolation, amino acid sequence and functional assays of SGTx1. The first toxin purified from the venom of the spider scodra griseipes. Eur. J. Biochem. 265(2):572-579.
    • (1999) Eur. J. Biochem. , vol.265 , Issue.2 , pp. 572-579
    • Marvin, L.1    De, E.2    Cosette, P.3    Gagnon, J.4    Molle, G.5    Lange, C.6
  • 47
    • 1942470943 scopus 로고    scopus 로고
    • Targeting ionotropic receptors with polyamine-containing toxins
    • Mellor, I. R., Usherwood, P. N. (2004). Targeting ionotropic receptors with polyamine-containing toxins. Toxicon 43(5):493-508.
    • (2004) Toxicon , vol.43 , Issue.5 , pp. 493-508
    • Mellor, I.R.1    Usherwood, P.N.2
  • 48
    • 0028983387 scopus 로고
    • The charybdotoxin family of K+ channel-blocking peptides
    • Miller, C. (1995). The charybdotoxin family of K+ channel-blocking peptides. Neuron 15(1):5-10.
    • (1995) Neuron , vol.15 , Issue.1 , pp. 5-10
    • Miller, C.1
  • 49
    • 0030748242 scopus 로고    scopus 로고
    • Behaviors and neurodegeneration induced by two blockers of K+ channels, the mast cell degranulating peptide and Dendrotoxin I
    • Mourre, C., Lazdunski, M., Jarrard, L. E. (1997). Behaviors and neurodegeneration induced by two blockers of K+ channels, the mast cell degranulating peptide and Dendrotoxin I. Brain Res. 762(1-2):223-227.
    • (1997) Brain Res. , vol.762 , Issue.1-2 , pp. 223-227
    • Mourre, C.1    Lazdunski, M.2    Jarrard, L.E.3
  • 50
    • 0035909061 scopus 로고    scopus 로고
    • Insights into alpha-K toxin specificity for K+ channels revealed through mutations in noxiustoxin
    • Mullinann, T. J., Spence, K. T., Schroeder, N. E., Fremont, V., Christian, E. P., Giangiacomo, K. M. (2001). Insights into alpha-K toxin specificity for K+ channels revealed through mutations in noxiustoxin. Biochemistry 40(37):10987-10997.
    • (2001) Biochemistry , vol.40 , Issue.37 , pp. 10987-10997
    • Mullinann, T.J.1    Spence, K.T.2    Schroeder, N.E.3    Fremont, V.4    Christian, E.P.5    Giangiacomo, K.M.6
  • 51
    • 0036378336 scopus 로고    scopus 로고
    • Spiders of medical importance in the Asia-Pacific: Atracotoxin, latrotoxin and related spider neurotoxins
    • Nicholson, G. M., Graudins, A. (2002). Spiders of medical importance in the Asia-Pacific: atracotoxin, latrotoxin and related spider neurotoxins. Clin. Exp. Pharmacol. Physiol. 29(9):785-794.
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , Issue.9 , pp. 785-794
    • Nicholson, G.M.1    Graudins, A.2
  • 52
    • 0028111357 scopus 로고
    • Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta
    • Nicholson, G. M., Willow, M., Howden, M. E., Narahashi, T. (1994). Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta. Pflugers Arch. 428(3-4):400-409.
    • (1994) Pflugers Arch. , vol.428 , Issue.3-4 , pp. 400-409
    • Nicholson, G.M.1    Willow, M.2    Howden, M.E.3    Narahashi, T.4
  • 53
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton, R. S., Pallaghy, P. K. (1998). The cystine knot structure of ion channel toxins and related polypeptides. Toxicon 36(11):1573-1583.
    • (1998) Toxicon , vol.36 , Issue.11 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 54
    • 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., 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
  • 55
    • 0026032209 scopus 로고
    • Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence
    • Papazian, D. M., Timpe, L. C., Jan, Y. N., Jan, L. Y. (1991). Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence. Nature 349(6307):305-310.
    • (1991) Nature , vol.349 , Issue.6307 , pp. 305-310
    • Papazian, D.M.1    Timpe, L.C.2    Jan, Y.N.3    Jan, L.Y.4
  • 56
    • 0033010374 scopus 로고    scopus 로고
    • Kv2.1/Kv9.3, an ATP-dependent delayed-rectifier K+ channel in pulmonary artery myocytes
    • Patel, A. J., Lazchunski, M., Honore, E. (1999). Kv2.1/Kv9.3, an ATP-dependent delayed-rectifier K+ channel in pulmonary artery myocytes. Ann. N. Y. Acad. Sci. 868:438-441.
    • (1999) Ann. N. Y. Acad. Sci. , vol.868 , pp. 438-441
    • Patel, A.J.1    Lazchunski, M.2    Honore, E.3
  • 57
    • 0035425355 scopus 로고    scopus 로고
    • Lipid and mechano-gated 2P domain K(+) channels
    • Patel, A. J., Lazdunski, M., Honore, E. (2001). Lipid and mechano-gated 2P domain K(+) channels. Curr. Opin. Cell. Biol. 13(4):422-428.
    • (2001) Curr. Opin. Cell. Biol. , vol.13 , Issue.4 , pp. 422-428
    • Patel, A.J.1    Lazdunski, M.2    Honore, E.3
  • 58
    • 0026486232 scopus 로고
    • Molecular biology of voltage-dependent potassium channels
    • Pongs, O. (1992). Molecular biology of voltage-dependent potassium channels. Physiol. Rev. 72(4 Suppl):S69-88.
    • (1992) Physiol. Rev. , vol.72 , Issue.4 SUPPL.
    • Pongs, O.1
  • 59
    • 0030064382 scopus 로고
    • Spatial localization of the K+ channel selectivity Filter by mutant cycle-based structure analysis
    • Ranganathan, R., Lewis, J. H., MacKinnon, R. (1990). Spatial localization of the K+ channel selectivity Filter by mutant cycle-based structure analysis. Neuron 16(1):131-139.
    • (1990) Neuron , vol.16 , Issue.1 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    MacKinnon, R.3
  • 61
    • 0030037704 scopus 로고    scopus 로고
    • Molecular determinants of high affinity binding of alpha-scorpion toxin and sea anemone toxin in the S3-S4 extracellular loop in domain IV of the Na+ channel alpha subunit
    • Rogers, J. C., Qu, Y., Tanada, T. N., Scheuer, T., Catterall, W. A. (1996). Molecular determinants of high affinity binding of alpha-scorpion toxin and sea anemone toxin in the S3-S4 extracellular loop in domain IV of the Na+ channel alpha subunit. J. Biol. Chem. 271(27):15950-15962.
    • (1996) J. Biol. Chem. , vol.271 , Issue.27 , pp. 15950-15962
    • Rogers, J.C.1    Qu, Y.2    Tanada, T.N.3    Scheuer, T.4    Catterall, W.A.5
  • 62
    • 0037435021 scopus 로고    scopus 로고
    • Functional analysis of an archaebacterial voltage-dependent K+ channel
    • Ruta, V., Jiang, Y., Lee, A., Chen, J., MacKinnon, R. (2003). Functional analysis of an archaebacterial voltage-dependent K+ channel. Nature 422(6928):180-185.
    • (2003) Nature , vol.422 , Issue.6928 , pp. 180-185
    • Ruta, V.1    Jiang, Y.2    Lee, A.3    Chen, J.4    MacKinnon, R.5
  • 63
    • 3543107260 scopus 로고    scopus 로고
    • Localization of the voltage-sensor toxin receptor on KvAP
    • Ruta, V., MacKinnon, R. (2004). Localization of the voltage-sensor toxin receptor on KvAP. Biochemistry 43(31):10071-10079.
    • (2004) Biochemistry , vol.43 , Issue.31 , pp. 10071-10079
    • Ruta, V.1    MacKinnon, R.2
  • 65
    • 0030001325 scopus 로고    scopus 로고
    • Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain
    • Serodio, P., Vega-Saenz de Miera, E., Rudy, B. (1996). Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain. J. Neurophysiol. 75(5):2174-2179.
    • (1996) J. Neurophysiol. , vol.75 , Issue.5 , pp. 2174-2179
    • Serodio, P.1    Vega-Saenz De Miera, E.2    Rudy, B.3
  • 66
    • 0142232008 scopus 로고    scopus 로고
    • Structural basis of binding and inhibition of novel tarantula toxins in mammalian voltage-dependent potassium channels
    • Shiau, Y. S., Huang, P. T., Liou, H. H., Liaw, Y. C., Shiau, Y. Y., Lou, K. L. (2003). Structural basis of binding and inhibition of novel tarantula toxins in mammalian voltage-dependent potassium channels. Chem. Res. Toxicol. 16(10):1217-1225.
    • (2003) Chem. Res. Toxicol. , vol.16 , Issue.10 , pp. 1217-1225
    • Shiau, Y.S.1    Huang, P.T.2    Liou, H.H.3    Liaw, Y.C.4    Shiau, Y.Y.5    Lou, K.L.6
  • 67
    • 0036979653 scopus 로고    scopus 로고
    • Molecular simulation reveals structural determinants of the hanatoxin binding in Kv2.1 channels
    • Shiau, Y. S., Lin, T. B., Liou, H. H., Huang, P. T., Lou, K. L., Shiau, Y. Y. (2002). Molecular simulation reveals structural determinants of the hanatoxin binding in Kv2.1 channels. J. Mol. Model (Online) 8(8):253-257.
    • (2002) J. Mol. Model (Online) , vol.8 , Issue.8 , pp. 253-257
    • Shiau, Y.S.1    Lin, T.B.2    Liou, H.H.3    Huang, P.T.4    Lou, K.L.5    Shiau, Y.Y.6
  • 68
    • 0033635776 scopus 로고    scopus 로고
    • Potassium channels: Molecular defects, diseases, and therapeutic opportunities
    • Shieh, C. C., Coghlan, M., Sullivan, J. P., Gopalakrishnan, M. (2000). Potassium channels: molecular defects, diseases, and therapeutic opportunities. Pharmacol. Rev. 52(4):557-594.
    • (2000) Pharmacol. Rev. , vol.52 , Issue.4 , pp. 557-594
    • Shieh, C.C.1    Coghlan, M.2    Sullivan, J.P.3    Gopalakrishnan, M.4
  • 70
    • 9944226711 scopus 로고    scopus 로고
    • Towards a structural view of gating in potassium channels
    • Swartz, K. J. (2004). Towards a structural view of gating in potassium channels. Nat. Rev. Neurosci. 5(12):905-916.
    • (2004) Nat. Rev. Neurosci. , vol.5 , Issue.12 , pp. 905-916
    • Swartz, K.J.1
  • 71
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz, K. J., MacKinnon, R. (1995). An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron 15(4):941-949.
    • (1995) Neuron , vol.15 , Issue.4 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 72
    • 0030952979 scopus 로고    scopus 로고
    • Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites
    • Swartz, K. J., MacKinnon, R. (1997a). Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron 18(4):665-673.
    • (1997) Neuron , vol.18 , Issue.4 , pp. 665-673
    • Swartz, K.J.1    MacKinnon, R.2
  • 73
    • 0030935699 scopus 로고    scopus 로고
    • Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels
    • Swartz, K. J., MacKinnon, R. (1997b). Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron 18(4):675-682.
    • (1997) Neuron , vol.18 , Issue.4 , pp. 675-682
    • Swartz, K.J.1    MacKinnon, R.2
  • 74
    • 0034737306 scopus 로고    scopus 로고
    • Solution structure of hanatoxin 1, a gating modifier of voltage-dependent K(+) channels: Common surface features of gating modifier toxins
    • Takahashi, H., Kim, J. I., Min, H. J., Sato, K., Swartz, K. J., Shimada, I. (2000). Solution structure of hanatoxin 1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins. J. Mol. Biol. 297(3):771-780.
    • (2000) J. Mol. Biol. , vol.297 , Issue.3 , pp. 771-780
    • Takahashi, H.1    Kim, J.I.2    Min, H.J.3    Sato, K.4    Swartz, K.J.5    Shimada, I.6
  • 75
    • 0036382850 scopus 로고    scopus 로고
    • Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel
    • Takeuchi, K., Park, E., Lee, C., Kim, J., Takahashi, H., Swartz, K., Shimada, I. (2002). Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel. J. Mol. Biol. 321(3):517-526.
    • (2002) J. Mol. Biol. , vol.321 , Issue.3 , pp. 517-526
    • Takeuchi, K.1    Park, E.2    Lee, C.3    Kim, J.4    Takahashi, H.5    Swartz, K.6    Shimada, I.7
  • 76
    • 0032500898 scopus 로고    scopus 로고
    • Sphingomyelinases in the venom of the spider Loxosceles intermedia are responsible for both dermonecrosis and complement-dependent hemolysis
    • Tambourgi, D. V., Magnoli, F. C., van den Berg, C. W., Morgan, B. P., de Araujo, P. S., Alves, E. W., Da Silva, W. D. (1998). Sphingomyelinases in the venom of the spider Loxosceles intermedia are responsible for both dermonecrosis and complement-dependent hemolysis. Biochem. Biophys. Res. Commun. 251(1):366-373.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , Issue.1 , pp. 366-373
    • Tambourgi, D.V.1    Magnoli, F.C.2    Van Den Berg, C.W.3    Morgan, B.P.4    De Araujo, P.S.5    Alves, E.W.6    Da Silva, W.D.7
  • 77
    • 1942438974 scopus 로고    scopus 로고
    • The multiple actions of black widow spider toxins and their selective use in neurosecretion studies
    • Ushkaryov, Y. A., Volynski, K. E., Ashton, A. C. (2004). The multiple actions of black widow spider toxins and their selective use in neurosecretion studies. Toxicon 43(5):527-542.
    • (2004) Toxicon , vol.43 , Issue.5 , pp. 527-542
    • Ushkaryov, Y.A.1    Volynski, K.E.2    Ashton, A.C.3
  • 78
    • 0026802393 scopus 로고
    • Antagonism of synaptosomal calcium channels by subtypes of omega-agatoxins
    • Venema, V. J., Swiderek, K. M., Lee, T. D., Hathaway, G. M., Adams, M. E. (1992). Antagonism of synaptosomal calcium channels by subtypes of omega-agatoxins. J. Biol. Chem. 267(4):2610-2615.
    • (1992) J. Biol. Chem. , vol.267 , Issue.4 , pp. 2610-2615
    • Venema, V.J.1    Swiderek, K.M.2    Lee, T.D.3    Hathaway, G.M.4    Adams, M.E.5
  • 79
    • 1842786935 scopus 로고    scopus 로고
    • Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels
    • Wang, J. M., Roh, S. H., Kim, S., Lee, C. W., Kim, J. I., Swartz, K. J. (2004). Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels. J Gen. Physiol. 123(4):455-467.
    • (2004) J. Gen. Physiol. , vol.123 , Issue.4 , pp. 455-467
    • Wang, J.M.1    Roh, S.H.2    Kim, S.3    Lee, C.W.4    Kim, J.I.5    Swartz, K.J.6
  • 80
    • 0033767401 scopus 로고    scopus 로고
    • A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels
    • Winterfield, J. R., Swartz, K. J. (2000). A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels. J Gen. Physiol. 116 (5):637-644.
    • (2000) J. Gen. Physiol. , vol.116 , Issue.5 , pp. 637-644
    • Winterfield, J.R.1    Swartz, K.J.2
  • 81
    • 0031057192 scopus 로고    scopus 로고
    • Electrophysiological and pharmacological correspondence between Kv4.2 current and rat cardiac transient outward current
    • Yeola, S. W., Snyders, D. J. (1997). Electrophysiological and pharmacological correspondence between Kv4.2 current and rat cardiac transient outward current. Cardiovasc. Res. 33(3):540-547.
    • (1997) Cardiovasc. Res. , vol.33 , Issue.3 , pp. 540-547
    • Yeola, S.W.1    Snyders, D.J.2
  • 83
    • 0141706802 scopus 로고    scopus 로고
    • Evolutionary origin of inhibitor cystine knot peptides
    • Epub 2003 Jul 1763
    • Zhu, S., Darbon, H., Dyason, K., Verdonck, F., Tytgat, J. (2003). Evolutionary origin of inhibitor cystine knot peptides. FASEB. J. 17(12):1765-1767. Epub 2003 Jul 1763.
    • (2003) FASEB. J. , vol.17 , Issue.12 , pp. 1765-1767
    • Zhu, S.1    Darbon, H.2    Dyason, K.3    Verdonck, F.4    Tytgat, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.