메뉴 건너뛰기




Volumn 39, Issue C, 1997, Pages 425-471

Pharmacology of Potassium Channels

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL; SCORPION VENOM; SNAKE VENOM;

EID: 0030629190     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(08)60078-2     Document Type: Article
Times cited : (116)

References (188)
  • 2
    • 4243696509 scopus 로고
    • Determination of Shaker K+ channel number and gating charge in individual Xenopus oocytes
    • Aggarwal S.K., and MacKinnon R. Determination of Shaker K+ channel number and gating charge in individual Xenopus oocytes. Biophys. J. 66 (1994) A136
    • (1994) Biophys. J. , vol.66
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 4
    • 77957145210 scopus 로고
    • The L401V mutation in Kv3.1 does not alter single channel conductance or K+/Rb+ selectivity
    • Aiyar J., Grissmer S., and Chandy K.G. The L401V mutation in Kv3.1 does not alter single channel conductance or K+/Rb+ selectivity. Biophys. J. 64 (1993) 197a
    • (1993) Biophys. J. , vol.64
    • Aiyar, J.1    Grissmer, S.2    Chandy, K.G.3
  • 8
    • 0024565802 scopus 로고
    • Polypeptide constitution of receptors for apamin, a neurotoxin which blocks a class of Ca2+-activated K+ channels
    • Auguste P., Hughes M., and Lazdunski M. Polypeptide constitution of receptors for apamin, a neurotoxin which blocks a class of Ca2+-activated K+ channels. FEBS Lett. 248 (1989) 150-154
    • (1989) FEBS Lett. , vol.248 , pp. 150-154
    • Auguste, P.1    Hughes, M.2    Lazdunski, M.3
  • 10
    • 0026584910 scopus 로고
    • Scyllatoxin, a blocker of Ca2+-activated K+ channels: Structure-function relationships and brain localization of the binding sites
    • Auguste P., Hugues M., Mourre C., Moinier D., Tartar A., and Lazdunski M. Scyllatoxin, a blocker of Ca2+-activated K+ channels: Structure-function relationships and brain localization of the binding sites. Biochemistry 31 (1992) 648-654
    • (1992) Biochemistry , vol.31 , pp. 648-654
    • Auguste, P.1    Hugues, M.2    Mourre, C.3    Moinier, D.4    Tartar, A.5    Lazdunski, M.6
  • 11
    • 0023747366 scopus 로고
    • Four polypeptide components of green mamba venom selectively block certain potassium channels in rat brain synaptosomes
    • Benishin C.G., Sorensen R.G., Brown W.E., Krueger B.K., and Blaustein M.P. Four polypeptide components of green mamba venom selectively block certain potassium channels in rat brain synaptosomes. Mol. Pharmacol. 34 (1988) 152-159
    • (1988) Mol. Pharmacol. , vol.34 , pp. 152-159
    • Benishin, C.G.1    Sorensen, R.G.2    Brown, W.E.3    Krueger, B.K.4    Blaustein, M.P.5
  • 12
    • 0027138664 scopus 로고
    • Nuclear magnetic resonance solution structure of dendrotoxin K from venom of Dendroaspis polylepis polylepis
    • Berndt K.D., Güntert P., and Wüthrich K. Nuclear magnetic resonance solution structure of dendrotoxin K from venom of Dendroaspis polylepis polylepis. J. Mol. Biol. 234 (1993) 735-750
    • (1993) J. Mol. Biol. , vol.234 , pp. 735-750
    • Berndt, K.D.1    Güntert, P.2    Wüthrich, K.3
  • 13
    • 0023106732 scopus 로고
    • Two potent central convulsant peptides, a bee venom toxin, the MCD peptide and a snake venom toxin, dendrotoxin I, known to block K+ channels, have interacting receptors sites
    • Bidard J.-N., Mourre C., and Lazdunski M. Two potent central convulsant peptides, a bee venom toxin, the MCD peptide and a snake venom toxin, dendrotoxin I, known to block K+ channels, have interacting receptors sites. Biochem. Biophys. Res. Commun. 143 (1987) 383-389
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 383-389
    • Bidard, J.-N.1    Mourre, C.2    Lazdunski, M.3
  • 14
    • 0022994018 scopus 로고
    • Single apamin blocked Ca-activated K+ channels of small conductance in cultured rat skeletal muscle
    • Blatz A.L., and Magleby K.L. Single apamin blocked Ca-activated K+ channels of small conductance in cultured rat skeletal muscle. Nature (London) 323 (1986) 718-720
    • (1986) Nature (London) , vol.323 , pp. 718-720
    • Blatz, A.L.1    Magleby, K.L.2
  • 15
    • 0025974392 scopus 로고
    • Three-dimensional structure of natural charybdotoxin in aquous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins
    • Bontems F., Roumestand C., Boyot P., Gilquin B., Doljansky Y., Menez A., and Toma F. Three-dimensional structure of natural charybdotoxin in aquous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins. Eur. J. Biochem. 196 (1991) 19-28
    • (1991) Eur. J. Biochem. , vol.196 , pp. 19-28
    • Bontems, F.1    Roumestand, C.2    Boyot, P.3    Gilquin, B.4    Doljansky, Y.5    Menez, A.6    Toma, F.7
  • 16
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems F., Roumestand C., Gilquin B., Menez A., and Toma F. Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins. Science 254 (1991) 1521-1523
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 17
    • 0027284153 scopus 로고
    • Comparison of the airways relaxant and hypotensive potencies of the potassium channel activators BRL 55834 and levcromakalim (BRL 38227) in vivo in guinea-pigs and rats
    • Bowring N.E., Arch J.R.S., Buckle D.R., and Taylor J.F. Comparison of the airways relaxant and hypotensive potencies of the potassium channel activators BRL 55834 and levcromakalim (BRL 38227) in vivo in guinea-pigs and rats. Br.J. Pharmacol. 109 (1993) 1133-1139
    • (1993) Br.J. Pharmacol. , vol.109 , pp. 1133-1139
    • Bowring, N.E.1    Arch, J.R.S.2    Buckle, D.R.3    Taylor, J.F.4
  • 18
    • 0024574941 scopus 로고
    • Interactions between discrete neuronal membrane binding sites for the putative K+-channel ligands β-bungarotoxin, dendrotoxin and mast-cell-degranulating peptide
    • Breeze A.L., and Dolly J.O. Interactions between discrete neuronal membrane binding sites for the putative K+-channel ligands β-bungarotoxin, dendrotoxin and mast-cell-degranulating peptide. Eur. J. Biochem. 178 (1989) 771-778
    • (1989) Eur. J. Biochem. , vol.178 , pp. 771-778
    • Breeze, A.L.1    Dolly, J.O.2
  • 19
    • 0028982438 scopus 로고
    • Ca2+-activated K+ channels of human and rabbit erythrocytes display distinctive patterns of inhibition by venom peptide toxins
    • Brugnara C., Armsby C.C., Franceschi L.D., Crest M., Euclaire M.-F.M., and Alper S.L. Ca2+-activated K+ channels of human and rabbit erythrocytes display distinctive patterns of inhibition by venom peptide toxins. J. Membr. Biol. 147 (1995) 71-82
    • (1995) J. Membr. Biol. , vol.147 , pp. 71-82
    • Brugnara, C.1    Armsby, C.C.2    Franceschi, L.D.3    Crest, M.4    Euclaire, M.-F.M.5    Alper, S.L.6
  • 20
    • 0027161159 scopus 로고
    • mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels
    • Butler A., Tsunoda S., McCobb D.P., Wei A., and Salkoff L. mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels. Science 261 (1993) 221-224
    • (1993) Science , vol.261 , pp. 221-224
    • Butler, A.1    Tsunoda, S.2    McCobb, D.P.3    Wei, A.4    Salkoff, L.5
  • 21
    • 0343941879 scopus 로고
    • Synthesis and characterization of dendrotoxin: A potent potassium channel inhibitor
    • Byrnes M.E., Mahnir V.M., Kern W.R., and Pennington M.W. Synthesis and characterization of dendrotoxin: A potent potassium channel inhibitor. Protein Pept. Lett. 1 (1995) 239-245
    • (1995) Protein Pept. Lett. , vol.1 , pp. 239-245
    • Byrnes, M.E.1    Mahnir, V.M.2    Kern, W.R.3    Pennington, M.W.4
  • 22
    • 0026673897 scopus 로고
    • Mode of action of iberiotoxin, a potent blocker of the large conductance Ca2+-activated K+ channel
    • Candia S., Garcia M.L., and Latorre R. Mode of action of iberiotoxin, a potent blocker of the large conductance Ca2+-activated K+ channel. Biophys. J. 63 (1992) 583-590
    • (1992) Biophys. J. , vol.63 , pp. 583-590
    • Candia, S.1    Garcia, M.L.2    Latorre, R.3
  • 23
    • 0020026499 scopus 로고
    • Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin
    • Carbone E., Wanke E., Prestipino G., Possani L.D., and Maelicke A. Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin. Nature (London) 296 (1982) 90-91
    • (1982) Nature (London) , vol.296 , pp. 90-91
    • Carbone, E.1    Wanke, E.2    Prestipino, G.3    Possani, L.D.4    Maelicke, A.5
  • 25
    • 0028817080 scopus 로고
    • Time- and voltage-dependent modulation of a Kv1.4 channel by a β-subunit (Kvβ3) cloned from ferret ventricle
    • Castellino R., Morales M.J., Strauss H.C., and Rasmusson R.L. Time- and voltage-dependent modulation of a Kv1.4 channel by a β-subunit (Kvβ3) cloned from ferret ventricle. Am. J. Physiol. 269 (1995) H385-H391
    • (1995) Am. J. Physiol. , vol.269
    • Castellino, R.1    Morales, M.J.2    Strauss, H.C.3    Rasmusson, R.L.4
  • 27
    • 0023740861 scopus 로고
    • Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus habraeus venom
    • Chicchi F.L.G.G., Gimenez-Gallego G., Ber E., Garcia M.L., Winquist R., and Cascieri M.A. Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus habraeus venom. J. Biol. Chem. 263 (1988) 10192-10197
    • (1988) J. Biol. Chem. , vol.263 , pp. 10192-10197
    • Chicchi, F.L.G.G.1    Gimenez-Gallego, G.2    Ber, E.3    Garcia, M.L.4    Winquist, R.5    Cascieri, M.A.6
  • 28
    • 0027417650 scopus 로고
    • The internal quaternary ammonium receptor site of Shaker potassium channels
    • Choi K.L., Mossman C., Aube J., and Yellen G. The internal quaternary ammonium receptor site of Shaker potassium channels. Neuron 10 (1993) 533-541
    • (1993) Neuron , vol.10 , pp. 533-541
    • Choi, K.L.1    Mossman, C.2    Aube, J.3    Yellen, G.4
  • 29
    • 0028116621 scopus 로고
    • Potassium channel blockers as antiarrhythmic drugs
    • Colatsky T.J., and Argentieri T.M. Potassium channel blockers as antiarrhythmic drugs. Drug Dev. Res. 33 (1994) 235-249
    • (1994) Drug Dev. Res. , vol.33 , pp. 235-249
    • Colatsky, T.J.1    Argentieri, T.M.2
  • 30
    • 0020529912 scopus 로고
    • High affinity binding of 125I-monoiodo apamin to isolated guinea-pig hepatocytes
    • Cook N.S., Haylett D.N., and Strong P. High affinity binding of 125I-monoiodo apamin to isolated guinea-pig hepatocytes. Febs Lett. 152 (1983) 265-269
    • (1983) Febs Lett. , vol.152 , pp. 265-269
    • Cook, N.S.1    Haylett, D.N.2    Strong, P.3
  • 31
    • 0026567123 scopus 로고
    • Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca2+-activated K+ channels characterized from Androctonus mauretanicus tnaure-tanicus venom
    • Crest M., Jacquet G., Gola M., Zerrouk H., Benslimane A., Rochat H., Mansuelle P., and Martin-Eauclaire M.-F. Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca2+-activated K+ channels characterized from Androctonus mauretanicus tnaure-tanicus venom. J. Biol. Chem. 267 (1992) 1640-1647
    • (1992) J. Biol. Chem. , vol.267 , pp. 1640-1647
    • Crest, M.1    Jacquet, G.2    Gola, M.3    Zerrouk, H.4    Benslimane, A.5    Rochat, H.6    Mansuelle, P.7    Martin-Eauclaire, M.-F.8
  • 34
    • 0029572430 scopus 로고
    • Determination of the three-dimensional solution structure of noxiustoxin: Analysis of structural differences with related short-chain scorpion toxins
    • Dauplais M., Gilquin B., Possani L.D., Gurrola-Briones G., Roumestand C., and Menez A. Determination of the three-dimensional solution structure of noxiustoxin: Analysis of structural differences with related short-chain scorpion toxins. Biochemistry 34 (1995) 16563-16573
    • (1995) Biochemistry , vol.34 , pp. 16563-16573
    • Dauplais, M.1    Gilquin, B.2    Possani, L.D.3    Gurrola-Briones, G.4    Roumestand, C.5    Menez, A.6
  • 35
    • 0029590782 scopus 로고
    • Stable expression of human Kv1.3 potassium channels resets the resting membrane potential of cultured mammalian cells
    • DeFarias F.P., Stevens S.P., and Leonard R.J. Stable expression of human Kv1.3 potassium channels resets the resting membrane potential of cultured mammalian cells. Recept. Channels 3 (1995) 273-281
    • (1995) Recept. Channels , vol.3 , pp. 273-281
    • DeFarias, F.P.1    Stevens, S.P.2    Leonard, R.J.3
  • 36
    • 0025805181 scopus 로고
    • Characterization of high affinity binding sites for charybdotoxin in human T lymphocytes: Evidence for association with the voltage-gated K+ channel
    • Deutsch C., Price M., Lee S., King V.F., and Garcia M.L. Characterization of high affinity binding sites for charybdotoxin in human T lymphocytes: Evidence for association with the voltage-gated K+ channel. J. Biol. Chem. 266 (1991) 3668-3674
    • (1991) J. Biol. Chem. , vol.266 , pp. 3668-3674
    • Deutsch, C.1    Price, M.2    Lee, S.3    King, V.F.4    Garcia, M.L.5
  • 40
    • 0028126679 scopus 로고
    • Cloning and expression of a human large-conductance calcium-activated potassium channel
    • Dworetzky S.I., Trojnacki J.T., and Gribkoff V.K. Cloning and expression of a human large-conductance calcium-activated potassium channel. Mol. Brain Res. 27 (1994) 189-193
    • (1994) Mol. Brain Res. , vol.27 , pp. 189-193
    • Dworetzky, S.I.1    Trojnacki, J.T.2    Gribkoff, V.K.3
  • 41
    • 0025094699 scopus 로고
    • Structure-activity relationship of K+ channel openers
    • Edwards G., and Weston A.H. Structure-activity relationship of K+ channel openers. Trends Pharmacol. Sci. 11 (1990) 417-422
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 417-422
    • Edwards, G.1    Weston, A.H.2
  • 42
    • 0027409532 scopus 로고
    • The pharmacology of ATP-sensitive potassium channels
    • Edwards G., and Weston A.H. The pharmacology of ATP-sensitive potassium channels. Annu. Rev. Pharmacol. Toxicol. 33 (1993) 597-637
    • (1993) Annu. Rev. Pharmacol. Toxicol. , vol.33 , pp. 597-637
    • Edwards, G.1    Weston, A.H.2
  • 43
    • 0029067547 scopus 로고
    • Pharmacology of the potassium channel openers
    • Edwards G., and Weston A.H. Pharmacology of the potassium channel openers. Cardiovasc. Drugs Thera. 9 (1995) 185-193
    • (1995) Cardiovasc. Drugs Thera. , vol.9 , pp. 185-193
    • Edwards, G.1    Weston, A.H.2
  • 44
    • 0028824132 scopus 로고
    • A novel K+ channel β-subunit (hKvβ1.3) is produced via alternative mRNA splicing
    • England S.K., Uebele V.N., Kodali J., Bennett P.B., and Tamkun M.M. A novel K+ channel β-subunit (hKvβ1.3) is produced via alternative mRNA splicing. J. Biol. Chem. 270 (1995) 28531-28534
    • (1995) J. Biol. Chem. , vol.270 , pp. 28531-28534
    • England, S.K.1    Uebele, V.N.2    Kodali, J.3    Bennett, P.B.4    Tamkun, M.M.5
  • 46
    • 4243424100 scopus 로고
    • Binding of mono-and di-iodinated margatoxin to human peripheral T lymphocytes and to Jurkat plasma membranes
    • Felix J.P., Bugianesi R.M., Abramsom A.A., and Slaughter R.S. Binding of mono-and di-iodinated margatoxin to human peripheral T lymphocytes and to Jurkat plasma membranes. Biophys. J. 68 (1995) 267a
    • (1995) Biophys. J. , vol.68
    • Felix, J.P.1    Bugianesi, R.M.2    Abramsom, A.A.3    Slaughter, R.S.4
  • 49
    • 0027339796 scopus 로고
    • Sequence-specific 1H-NMR assignment and secondary structure of black mamba dendrotoxin I, a highly selective blocker of voltage-gated potassium channels
    • Foray M.-F., Lancelin J.-M., Hollecker M., and Marion D. Sequence-specific 1H-NMR assignment and secondary structure of black mamba dendrotoxin I, a highly selective blocker of voltage-gated potassium channels. Eur. J. Biochem. 211 (1993) 813-820
    • (1993) Eur. J. Biochem. , vol.211 , pp. 813-820
    • Foray, M.-F.1    Lancelin, J.-M.2    Hollecker, M.3    Marion, D.4
  • 50
    • 0025299607 scopus 로고
    • Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus
    • Galvez A., Gimenez-Gallego G., Reuben J.P., Roy-Contancin L., Feigenbaum P., Kaczorow-ski G.J., and Garcia M.L. Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus. J. Biol. Chem. 265 (1990) 11083-11090
    • (1990) J. Biol. Chem. , vol.265 , pp. 11083-11090
    • Galvez, A.1    Gimenez-Gallego, G.2    Reuben, J.P.3    Roy-Contancin, L.4    Feigenbaum, P.5    Kaczorow-ski, G.J.6    Garcia, M.L.7
  • 51
    • 0028335105 scopus 로고
    • Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom
    • Garcia M.L., Garcia-Calvo M., Hidalgo P., Lee A., and MacKinnon R. Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom. Biochemistry 33 (1994) 6834-6839
    • (1994) Biochemistry , vol.33 , pp. 6834-6839
    • Garcia, M.L.1    Garcia-Calvo, M.2    Hidalgo, P.3    Lee, A.4    MacKinnon, R.5
  • 52
    • 0027320629 scopus 로고
    • Purification, characterization and biosynthesis of marga-toxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels
    • Garcia-Calvo M., Leonard R.J., Novick J., Stevens S.P., Schmalhofer W., Kaczorowski G.J., and Garcia M.L. Purification, characterization and biosynthesis of marga-toxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels. J. Biol. Chem. 268 (1993) 18866-18874
    • (1993) J. Biol. Chem. , vol.268 , pp. 18866-18874
    • Garcia-Calvo, M.1    Leonard, R.J.2    Novick, J.3    Stevens, S.P.4    Schmalhofer, W.5    Kaczorowski, G.J.6    Garcia, M.L.7
  • 53
    • 0027979245 scopus 로고
    • Purification and reconstitution of the high-conductance calcium-activated potassium channel from tracheal smooth muscle
    • Garcia-Calvo M., Knaus H.-G., McManus O.B., Giangiacomo K.M., Kaczorowski G.J., and Garcia M.L. Purification and reconstitution of the high-conductance calcium-activated potassium channel from tracheal smooth muscle. J. Biol. Chem. 269 (1994) 676-682
    • (1994) J. Biol. Chem. , vol.269 , pp. 676-682
    • Garcia-Calvo, M.1    Knaus, H.-G.2    McManus, O.B.3    Giangiacomo, K.M.4    Kaczorowski, G.J.5    Garcia, M.L.6
  • 55
    • 0026771320 scopus 로고
    • Mechanism of iberiotoxin block of the large-conductance calcium-activated potassium channel from bovine aortic smooth muscle
    • Giangiacomo K.M., Garcia M.L., and McManus O.B. Mechanism of iberiotoxin block of the large-conductance calcium-activated potassium channel from bovine aortic smooth muscle. Biochemistry 31 (1992) 6719-6727
    • (1992) Biochemistry , vol.31 , pp. 6719-6727
    • Giangiacomo, K.M.1    Garcia, M.L.2    McManus, O.B.3
  • 56
    • 0027461255 scopus 로고
    • Synthetic charybdotoxin-iberiotoxinchimeric peptides define toxin binding sites on calcium-activated and voltage-dependent potassium channels
    • Giangiacomo K.M., Sugg E.E., Garcia-Calvo M., Leonard R.J., McManus O.B., Kaczorowski G.J., and Garcia M.L. Synthetic charybdotoxin-iberiotoxinchimeric peptides define toxin binding sites on calcium-activated and voltage-dependent potassium channels. Biochemistry 32 (1993) 2363-2370
    • (1993) Biochemistry , vol.32 , pp. 2363-2370
    • Giangiacomo, K.M.1    Sugg, E.E.2    Garcia-Calvo, M.3    Leonard, R.J.4    McManus, O.B.5    Kaczorowski, G.J.6    Garcia, M.L.7
  • 57
    • 0028812725 scopus 로고
    • Functional reconstitution of the large-conductance, calcium-activated potassium channel purified from bovine aortic smooth muscle
    • Giangiacomo K.M., Garcia-Calvo M., Knaus H.-G., Mullmann T.J., Garcia M.L., and McManus O. Functional reconstitution of the large-conductance, calcium-activated potassium channel purified from bovine aortic smooth muscle. Biochemistry 34 (1995) 15849-15862
    • (1995) Biochemistry , vol.34 , pp. 15849-15862
    • Giangiacomo, K.M.1    Garcia-Calvo, M.2    Knaus, H.-G.3    Mullmann, T.J.4    Garcia, M.L.5    McManus, O.6
  • 58
    • 0006117915 scopus 로고
    • Purification, sequence and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels
    • Gimenez-Gallego G., Navia M.A., Reuben J.P., Katz G.M., Kaczorowski G.J., and Garcia M.L. Purification, sequence and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 3329-3333
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3329-3333
    • Gimenez-Gallego, G.1    Navia, M.A.2    Reuben, J.P.3    Katz, G.M.4    Kaczorowski, G.J.5    Garcia, M.L.6
  • 59
    • 0026646549 scopus 로고
    • Effect of charybdotoxin and leiurotoxin I on potassium currents in bullfrog sympathetic ganglion and hippocampal neurons
    • Goh J.W., Kelley M.E.M., Pennefather P.S., Chicchi G.G., Cascieri M.A., Garcia M.L., and Kaczorowski G.J. Effect of charybdotoxin and leiurotoxin I on potassium currents in bullfrog sympathetic ganglion and hippocampal neurons. Brain Res. 591 (1992) 165-170
    • (1992) Brain Res. , vol.591 , pp. 165-170
    • Goh, J.W.1    Kelley, M.E.M.2    Pennefather, P.S.3    Chicchi, G.G.4    Cascieri, M.A.5    Garcia, M.L.6    Kaczorowski, G.J.7
  • 60
    • 0027443836 scopus 로고
    • Mechanism of charybdotoxin block of a voltage-gated K+ channel
    • Goldstein S.A.N., and Miller C. Mechanism of charybdotoxin block of a voltage-gated K+ channel. Biophys. J. 65 (1993) 1613-1619
    • (1993) Biophys. J. , vol.65 , pp. 1613-1619
    • Goldstein, S.A.N.1    Miller, C.2
  • 61
    • 0028276482 scopus 로고
    • The charybdotoxin receptor of a Shaker K+ channel: Peptide and channel residues mediating molecular recognition
    • Goldstein S.A.N., Pheasant D.J., and Miller C. The charybdotoxin receptor of a Shaker K+ channel: Peptide and channel residues mediating molecular recognition. Neuron 12 (1994) 1377-1388
    • (1994) Neuron , vol.12 , pp. 1377-1388
    • Goldstein, S.A.N.1    Pheasant, D.J.2    Miller, C.3
  • 62
    • 0017913375 scopus 로고
    • Use of synthetic analogs for a study on the structure-activity relationship of apamin
    • Granier C., Pedroso-Muller E., and Rietschoten J.V. Use of synthetic analogs for a study on the structure-activity relationship of apamin. Eur. J. Biochem. 82 (1978) 293-299
    • (1978) Eur. J. Biochem. , vol.82 , pp. 293-299
    • Granier, C.1    Pedroso-Muller, E.2    Rietschoten, J.V.3
  • 63
    • 0028228251 scopus 로고
    • Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv 1.1, 1.2, 1.3, 1.5 and 3.1, stably expressed in mammalian cell lines
    • Grissmer S., Nguyen A.N., Aiyar J., Hanson D.C., Mather R.J., Gutman G.A., Karmilowicz M.J., Auperin D.D., and Chandy K.G. Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv 1.1, 1.2, 1.3, 1.5 and 3.1, stably expressed in mammalian cell lines. Mol. Pharmacol. 45 (1994) 1227-1234
    • (1994) Mol. Pharmacol. , vol.45 , pp. 1227-1234
    • Grissmer, S.1    Nguyen, A.N.2    Aiyar, J.3    Hanson, D.C.4    Mather, R.J.5    Gutman, G.A.6    Karmilowicz, M.J.7    Auperin, D.D.8    Chandy, K.G.9
  • 64
    • 0028105127 scopus 로고
    • Transfer of the scorpion toxin receptor to an insensitive potassium channel
    • Gross A., Abramson T., and MacKinnon R. Transfer of the scorpion toxin receptor to an insensitive potassium channel. Neuron 13 (1994) 961-966
    • (1994) Neuron , vol.13 , pp. 961-966
    • Gross, A.1    Abramson, T.2    MacKinnon, R.3
  • 65
    • 0342621203 scopus 로고
    • Central action of dendrotoxin: Selective reduction of a transient K conductance in hippocampus and binding to localized acceptors
    • Halliwell J.V., Othman I.B., Pelchen-Matthews A., and Dolly J.O. Central action of dendrotoxin: Selective reduction of a transient K conductance in hippocampus and binding to localized acceptors. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 493-497
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 493-497
    • Halliwell, J.V.1    Othman, I.B.2    Pelchen-Matthews, A.3    Dolly, J.O.4
  • 66
    • 0022332269 scopus 로고
    • Dendrotoxins: Snake toxins that block potassium channels and facilitate neurotransmitter release
    • Harvey A.L., and Anderson A. Dendrotoxins: Snake toxins that block potassium channels and facilitate neurotransmitter release. Pharmacol. Ther. 31 (1985) 33-55
    • (1985) Pharmacol. Ther. , vol.31 , pp. 33-55
    • Harvey, A.L.1    Anderson, A.2
  • 67
    • 0019956008 scopus 로고
    • Protein inhibitor homologues from Mamba venoms: Facilitation of acetylcholine release and interactions with prejunctional blocking toxins
    • Harvey A.L., and Karlsson E. Protein inhibitor homologues from Mamba venoms: Facilitation of acetylcholine release and interactions with prejunctional blocking toxins. Br. J. Pharmacol. 77 (1982) 153-161
    • (1982) Br. J. Pharmacol. , vol.77 , pp. 153-161
    • Harvey, A.L.1    Karlsson, E.2
  • 68
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • Hidalgo P., and MacKinnon R. Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor. Science 268 (1995) 307-310
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 70
    • 0027326935 scopus 로고
    • Structural features important for the biological activity of the potassium channel blocking dendrotoxins
    • Hollecker M., Marshall D.L., and Harvey A.L. Structural features important for the biological activity of the potassium channel blocking dendrotoxins. Br. J. Pharmacol. 110 (1993) 790-794
    • (1993) Br. J. Pharmacol. , vol.110 , pp. 790-794
    • Hollecker, M.1    Marshall, D.L.2    Harvey, A.L.3
  • 71
    • 0020024563 scopus 로고
    • Preparation of a pure monoiodo derivative of the bee venom neurotoxin apamin and its binding properties to rat brain synaptosomes
    • Hugues M., Duval D., Kitabi P., Lazdunski M., and Vincent J.P. Preparation of a pure monoiodo derivative of the bee venom neurotoxin apamin and its binding properties to rat brain synaptosomes. J. Biol. Chem. 257 (1982) 2762-2769
    • (1982) J. Biol. Chem. , vol.257 , pp. 2762-2769
    • Hugues, M.1    Duval, D.2    Kitabi, P.3    Lazdunski, M.4    Vincent, J.P.5
  • 72
    • 0020328664 scopus 로고
    • Specific binding and pharmacological interactions of apamin, the neurotoxin from bee venom, with guinea-pig colon
    • Hugues M., Duval D., Schmid H., Kitabgi P., and Lazdunski M. Specific binding and pharmacological interactions of apamin, the neurotoxin from bee venom, with guinea-pig colon. Life Sci. 31 (1982) 437-443
    • (1982) Life Sci. , vol.31 , pp. 437-443
    • Hugues, M.1    Duval, D.2    Schmid, H.3    Kitabgi, P.4    Lazdunski, M.5
  • 73
    • 0344100952 scopus 로고
    • Apamin as a selective blocker of the calcium dependent potassium channel in neuroblastoma cells: Voltage clamp and biochemical characterization of the toxin receptor
    • Hugues M., Schmid H., Romey G., Duval D., Frelin C., and Lazdunski M. Apamin as a selective blocker of the calcium dependent potassium channel in neuroblastoma cells: Voltage clamp and biochemical characterization of the toxin receptor. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 1308-1312
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 1308-1312
    • Hugues, M.1    Schmid, H.2    Romey, G.3    Duval, D.4    Frelin, C.5    Lazdunski, M.6
  • 74
    • 0013589156 scopus 로고
    • The Ca2+-dependent slow K+ conductance in cultured rat muscle cells: Characterization with apamin
    • Hugues M., Schmid H., Romey G., Duval D., Frelin C., and Lazdunski M. The Ca2+-dependent slow K+ conductance in cultured rat muscle cells: Characterization with apamin. EMBO J. 1 (1982) 1039-1042
    • (1982) EMBO J. , vol.1 , pp. 1039-1042
    • Hugues, M.1    Schmid, H.2    Romey, G.3    Duval, D.4    Frelin, C.5    Lazdunski, M.6
  • 75
    • 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., and Adelman J.P. Identification of amino acid residues involved in dendrotoxin block of rat voltage-dependent potassium channels. Mol. Pharmacol. 40 (1991) 572-576
    • (1991) Mol. Pharmacol. , vol.40 , 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
  • 77
    • 0026781766 scopus 로고
    • Determination of the three-dimensional structure of iberiotoxin in solution by 1H nuclear magnetic resonance spectroscopy
    • Johnson B.A., and Sugg E.E. Determination of the three-dimensional structure of iberiotoxin in solution by 1H nuclear magnetic resonance spectroscopy. Biochemistry 31 (1992) 8151-8159
    • (1992) Biochemistry , vol.31 , pp. 8151-8159
    • Johnson, B.A.1    Sugg, E.E.2
  • 78
    • 0028651908 scopus 로고
    • Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy
    • Johnson B.A., Stevens S.P., and Williamson J.M. Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 33 (1994) 15061-15070
    • (1994) Biochemistry , vol.33 , pp. 15061-15070
    • Johnson, B.A.1    Stevens, S.P.2    Williamson, J.M.3
  • 81
    • 0026533326 scopus 로고
    • Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium
    • Kavanaugh M.P., Hurst R.S., Yakel J., Varnum M.D., Adelman J.P., and North R.A. Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron 8 (1992) 493-497
    • (1992) Neuron , vol.8 , pp. 493-497
    • Kavanaugh, M.P.1    Hurst, R.S.2    Yakel, J.3    Varnum, M.D.4    Adelman, J.P.5    North, R.A.6
  • 82
    • 0028879083 scopus 로고
    • Cloned human inward rectifier K+ channel as a target for class III methanesulfonanilides
    • Kiehn J., Wible B., Ficker E., Taglialatela M., and Brown A.M. Cloned human inward rectifier K+ channel as a target for class III methanesulfonanilides. Circ. Res. 77 (1995) 1151-1155
    • (1995) Circ. Res. , vol.77 , pp. 1151-1155
    • Kiehn, J.1    Wible, B.2    Ficker, E.3    Taglialatela, M.4    Brown, A.M.5
  • 83
    • 0025946370 scopus 로고
    • Internal and external TEA block in single cloned K+ channels
    • Kirsch G.E., Taglialatela M., and Brown A.M. Internal and external TEA block in single cloned K+ channels. Am. J. Physiol. 261 (1991) C583-C590
    • (1991) Am. J. Physiol. , vol.261
    • Kirsch, G.E.1    Taglialatela, M.2    Brown, A.M.3
  • 84
    • 0026528497 scopus 로고
    • Differences between the deep pores of K+ channels determined by an interacting pair of nonpolar amino acids
    • Kirsch G.E., Drewe J.A., Hartmann H.A., Taglialatela M., DeBiasi M., Brown A.M., and Joho R.H. Differences between the deep pores of K+ channels determined by an interacting pair of nonpolar amino acids. Neuron 8 (1992) 499-505
    • (1992) Neuron , vol.8 , pp. 499-505
    • Kirsch, G.E.1    Drewe, J.A.2    Hartmann, H.A.3    Taglialatela, M.4    DeBiasi, M.5    Brown, A.M.6    Joho, R.H.7
  • 86
    • 0027482867 scopus 로고
    • Segmental exchanges define 4-aminopyridine binding and the inner mouth of K+ pores
    • Kirsch G.E., Shieh C.C., Drewe J.A., Vener D.F., and Brown A.M. Segmental exchanges define 4-aminopyridine binding and the inner mouth of K+ pores. Neuron 11 (1993) 1-20
    • (1993) Neuron , vol.11 , pp. 1-20
    • Kirsch, G.E.1    Shieh, C.C.2    Drewe, J.A.3    Vener, D.F.4    Brown, A.M.5
  • 87
    • 0028136565 scopus 로고
    • Subunit composition of the high conductance calcium-activated potassium channel from smooth muscle, a representative of the mSlo and slowpoke family of potassium channels
    • Knaus H.-G., Garcia-Calvo M., Kaczorowski G.J., and Garcia M.L. Subunit composition of the high conductance calcium-activated potassium channel from smooth muscle, a representative of the mSlo and slowpoke family of potassium channels. J. Biol. Chem. 269 (1994) 3921-3924
    • (1994) J. Biol. Chem. , vol.269 , pp. 3921-3924
    • Knaus, H.-G.1    Garcia-Calvo, M.2    Kaczorowski, G.J.3    Garcia, M.L.4
  • 88
    • 0028318835 scopus 로고
    • Primary sequence and immunological characterization of the β-subunit of the high-conductance Ca2+-activated K+ channel from smooth muscle
    • Knaus H.-G., Folander K., Garcia-Calvo M., Garcia M.L., Kaczorowski G.J., Smith M., and Swanson R. Primary sequence and immunological characterization of the β-subunit of the high-conductance Ca2+-activated K+ channel from smooth muscle. J. Biol. Chem. 269 (1994) 17274-17278
    • (1994) J. Biol. Chem. , vol.269 , pp. 17274-17278
    • Knaus, H.-G.1    Folander, K.2    Garcia-Calvo, M.3    Garcia, M.L.4    Kaczorowski, G.J.5    Smith, M.6    Swanson, R.7
  • 89
    • 0027964762 scopus 로고
    • Covalent attachment of charybdotoxin to the β-subunit of the high-conductance Ca2+-activated K+ channel
    • Knaus H.-G., Eberhart A., Kaczorowski G.J., and Garcia M.L. Covalent attachment of charybdotoxin to the β-subunit of the high-conductance Ca2+-activated K+ channel. J. Biol. Chem. 269 (1994) 23336-23341
    • (1994) J. Biol. Chem. , vol.269 , pp. 23336-23341
    • Knaus, H.-G.1    Eberhart, A.2    Kaczorowski, G.J.3    Garcia, M.L.4
  • 91
    • 0028971853 scopus 로고
    • [125I]Margatoxin, an extraordinarily high affinity ligand for voltage-gated potassium channels in mammalian brain
    • Knaus H.-G., Koch R.O.A., Eberhart A., Kaczorowski G.J., Garcia M.L., and Slaughter R.S. [125I]Margatoxin, an extraordinarily high affinity ligand for voltage-gated potassium channels in mammalian brain. Biochemistry 34 (1995) 13627-13634
    • (1995) Biochemistry , vol.34 , pp. 13627-13634
    • Knaus, H.-G.1    Koch, R.O.A.2    Eberhart, A.3    Kaczorowski, G.J.4    Garcia, M.L.5    Slaughter, R.S.6
  • 95
    • 0029113242 scopus 로고
    • Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry
    • Krezel A.M., Kasibhatla C., Hidalgo P., MacKinnon R., and Wagner G. Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry. Protein Sci. 4 (1995) 1478-1489
    • (1995) Protein Sci. , vol.4 , pp. 1478-1489
    • Krezel, A.M.1    Kasibhatla, C.2    Hidalgo, P.3    MacKinnon, R.4    Wagner, G.5
  • 99
    • 0026442383 scopus 로고
    • Selective blockers of voltage-gated K+ channels depolarize human T lymphocytes: Mechanism of the antipro-liferative effect of charybdotoxin
    • Leonard R.J., Garcia M.L., Slaughter R.S., and Reuben J.P. Selective blockers of voltage-gated K+ channels depolarize human T lymphocytes: Mechanism of the antipro-liferative effect of charybdotoxin. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 10094-10098
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10094-10098
    • Leonard, R.J.1    Garcia, M.L.2    Slaughter, R.S.3    Reuben, J.P.4
  • 100
    • 0025064810 scopus 로고
    • Polypeptide components of the apamin receptor associated with a calcium activated potassium channel
    • Leveque C., Marqueze B., Couraud F., and Seagar M. Polypeptide components of the apamin receptor associated with a calcium activated potassium channel. FEBS Lett. 275 (1990) 185-189
    • (1990) FEBS Lett. , vol.275 , pp. 185-189
    • Leveque, C.1    Marqueze, B.2    Couraud, F.3    Seagar, M.4
  • 102
    • 77957114880 scopus 로고    scopus 로고
    • Probing the pore of an inward-rectifier K+ channel with a scorpion toxin
    • Lu Z., Lewis J.H., and MacKinnon R. Probing the pore of an inward-rectifier K+ channel with a scorpion toxin. Biophys. J. 70 (1996) 145a
    • (1996) Biophys. J. , vol.70
    • Lu, Z.1    Lewis, J.H.2    MacKinnon, R.3
  • 103
    • 0024412151 scopus 로고
    • Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels
    • Lucchesi K., Ravindran A., Young H., and Moczydlowski E. Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels. J. Membr. Biol. 109 (1989) 269-281
    • (1989) J. Membr. Biol. , vol.109 , pp. 269-281
    • Lucchesi, K.1    Ravindran, A.2    Young, H.3    Moczydlowski, E.4
  • 104
    • 0023887273 scopus 로고
    • Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel
    • MacKinnon R., and Miller C. Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel. J. Gen. Physiol. 91 (1988) 335-349
    • (1988) J. Gen. Physiol. , vol.91 , pp. 335-349
    • MacKinnon, R.1    Miller, C.2
  • 105
    • 0024471942 scopus 로고
    • Functional modification of a Ca2+-activated K+ channel by trimethyloxonium
    • MacKinnon R., and Miller C. Functional modification of a Ca2+-activated K+ channel by trimethyloxonium. Biochemistry 28 (1989) 8087-8092
    • (1989) Biochemistry , vol.28 , pp. 8087-8092
    • MacKinnon, R.1    Miller, C.2
  • 106
    • 0025706152 scopus 로고
    • Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels
    • MacKinnon R., and Yellen G. Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels. Science 250 (1990) 276-279
    • (1990) Science , vol.250 , pp. 276-279
    • MacKinnon, R.1    Yellen, G.2
  • 107
    • 0024153562 scopus 로고
    • Charybdotoxin block of Shaker K+ channels suggests that different types of K+ channels share common structural features
    • MacKinnon R., Reinhart P.H., and White M.M. Charybdotoxin block of Shaker K+ channels suggests that different types of K+ channels share common structural features. Neuron 1 (1988) 997-1001
    • (1988) Neuron , vol.1 , pp. 997-1001
    • MacKinnon, R.1    Reinhart, P.H.2    White, M.M.3
  • 108
    • 0028949194 scopus 로고
    • Molecular cloning and functional expression of a novel potassium channel β-subunit from human atrium
    • Majumder K., Biasi M.D., Wang Z., and Wible B.A. Molecular cloning and functional expression of a novel potassium channel β-subunit from human atrium. FEBS Lett. 361 (1995) 13-16
    • (1995) FEBS Lett. , vol.361 , pp. 13-16
    • Majumder, K.1    Biasi, M.D.2    Wang, Z.3    Wible, B.A.4
  • 109
    • 0028019507 scopus 로고
    • Novel K+-channel-blocking toxins from the venom of the scorpion Centruroides litnpidus limpidus Karsch
    • Martin B.M., Ramirez A.N., Gurrola G.B., Nobile M., Prestipino G., and Possani L.D. Novel K+-channel-blocking toxins from the venom of the scorpion Centruroides litnpidus limpidus Karsch. Biochem. J. 304 (1994) 51-56
    • (1994) Biochem. J. , vol.304 , pp. 51-56
    • Martin, B.M.1    Ramirez, A.N.2    Gurrola, G.B.3    Nobile, M.4    Prestipino, G.5    Possani, L.D.6
  • 110
    • 0028811207 scopus 로고
    • Determination of the three-dimensional solution structure of scyllatoxin by 1H nuclear magnetic resonance
    • Martins J.C., Van de Ven F.J.M., and Borremans F.A.M. Determination of the three-dimensional solution structure of scyllatoxin by 1H nuclear magnetic resonance. J. Mol. Biol. 253 (1995) 590-603
    • (1995) J. Mol. Biol. , vol.253 , pp. 590-603
    • Martins, J.C.1    Van de Ven, F.J.M.2    Borremans, F.A.M.3
  • 111
    • 0029162526 scopus 로고
    • Alternative splicing of the human Shaker K+ channel β1 gene and functional expression of the β2 gene product
    • McCormack K., McCormack T., Tanouye M., Rudy B., and Stühmer W. Alternative splicing of the human Shaker K+ channel β1 gene and functional expression of the β2 gene product. FEBS Lett. 370 (1995) 32-36
    • (1995) FEBS Lett. , vol.370 , pp. 32-36
    • McCormack, K.1    McCormack, T.2    Tanouye, M.3    Rudy, B.4    Stühmer, W.5
  • 113
    • 0025864473 scopus 로고
    • Calcium-activated potassium channels: Regulation by calcium
    • McManus O.B. Calcium-activated potassium channels: Regulation by calcium. J. Bioenerg. Biomembr. 23 (1991) 537-560
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 537-560
    • McManus, O.B.1
  • 115
    • 0028926916 scopus 로고
    • Functional role of the β subunit of high-conductance calcium-activated potassium channels
    • McManus O.B., Helms L.M.H., Pallanck L., Ganetzky B., Swanson R., and Leonard R.J. Functional role of the β subunit of high-conductance calcium-activated potassium channels. Neuron 14 (1995) 1-20
    • (1995) Neuron , vol.14 , pp. 1-20
    • McManus, O.B.1    Helms, L.M.H.2    Pallanck, L.3    Ganetzky, B.4    Swanson, R.5    Leonard, R.J.6
  • 117
    • 0021918550 scopus 로고
    • Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle
    • Miller C., Moczydlowski E., Latorre R., and Phillips M. Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle. Nature (London) 313 (1985) 316-318
    • (1985) Nature (London) , vol.313 , pp. 316-318
    • Miller, C.1    Moczydlowski, E.2    Latorre, R.3    Phillips, M.4
  • 118
    • 0028957057 scopus 로고
    • A novel β subunit increases rate of inactivation of specific voltage-gated potassium channel α subunits
    • Morales M.J., Castellino R.C., Crews A.L., Rasmusson R.L., and Strauss H.C. A novel β subunit increases rate of inactivation of specific voltage-gated potassium channel α subunits. J. Biol. Chem. 270 (1995) 6272-6277
    • (1995) J. Biol. Chem. , vol.270 , pp. 6272-6277
    • Morales, M.J.1    Castellino, R.C.2    Crews, A.L.3    Rasmusson, R.L.4    Strauss, H.C.5
  • 119
    • 0027000070 scopus 로고
    • Characterization of monoclonal antibodies against voltage-dependent K+ channels raised using α-dendrotoxin acceptors purified from bovine brain
    • Muniz Z.M., Parcej D.N., and Dolly J.O. Characterization of monoclonal antibodies against voltage-dependent K+ channels raised using α-dendrotoxin acceptors purified from bovine brain. Biochemistry 31 (1992) 12297-12303
    • (1992) Biochemistry , vol.31 , pp. 12297-12303
    • Muniz, Z.M.1    Parcej, D.N.2    Dolly, J.O.3
  • 120
    • 0009606396 scopus 로고    scopus 로고
    • A novel class of potent organic blockers of the T-cell K channel, Kvl.3, that are selective for histidine 404
    • Nguyen A., Kath J., Hanson D., Dethlefs B., Gutman G., Cahalan M.D., and Chandy K.G. A novel class of potent organic blockers of the T-cell K channel, Kvl.3, that are selective for histidine 404. Biophys. J. 70 (1996) A446
    • (1996) Biophys. J. , vol.70
    • Nguyen, A.1    Kath, J.2    Hanson, D.3    Dethlefs, B.4    Gutman, G.5    Cahalan, M.D.6    Chandy, K.G.7
  • 121
    • 4243313218 scopus 로고
    • Purification and characterization of two novel peptidyl toxins directed against K+ channels from venom of new world scorpions
    • Novick J., Leonard R.J., King V.F., Schmalhofer W., Kaczorowski G.J., and Garcia M.L. Purification and characterization of two novel peptidyl toxins directed against K+ channels from venom of new world scorpions. Biophys. J. 59 (1991) 78a
    • (1991) Biophys. J. , vol.59
    • Novick, J.1    Leonard, R.J.2    King, V.F.3    Schmalhofer, W.4    Kaczorowski, G.J.5    Garcia, M.L.6
  • 122
    • 0027948426 scopus 로고
    • Activators of large-conductance Ca2+-dependent K+ channels
    • Olesen S.-P. Activators of large-conductance Ca2+-dependent K+ channels. Exp. Opin. Invest. Drugs 3 (1994) 1181-1188
    • (1994) Exp. Opin. Invest. Drugs , vol.3 , pp. 1181-1188
    • Olesen, S.-P.1
  • 123
    • 0028177490 scopus 로고
    • Selective activation of Ca2+-dependent K+ channels by novel benzimidazolone
    • Olesen S.-P., Munch E., Moldt P., and Drejer J. Selective activation of Ca2+-dependent K+ channels by novel benzimidazolone. Eur. J. Pharmacol. 251 (1994) 53-59
    • (1994) Eur. J. Pharmacol. , vol.251 , pp. 53-59
    • Olesen, S.-P.1    Munch, E.2    Moldt, P.3    Drejer, J.4
  • 124
  • 125
    • 0027956518 scopus 로고
    • Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke
    • Pallanck L., and Ganetzky B. Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke. Hum. Mol. Genet. 3 (1994) 1239-1243
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1239-1243
    • Pallanck, L.1    Ganetzky, B.2
  • 126
    • 0024495572 scopus 로고
    • Dendrotoxin acceptor from bovine synaptic plasma membranes: Binding properties, purification and subunit composition of a putative constituent of certain voltage-activated K+ channels
    • Parcej D.N., and Dolly J.O. Dendrotoxin acceptor from bovine synaptic plasma membranes: Binding properties, purification and subunit composition of a putative constituent of certain voltage-activated K+ channels. Biochem. J. 257 (1989) 899-903
    • (1989) Biochem. J. , vol.257 , pp. 899-903
    • Parcej, D.N.1    Dolly, J.O.2
  • 127
    • 0026803224 scopus 로고
    • Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel
    • Park C.-S., and Miller C. Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel. Neuron 9 (1992) 307-313
    • (1992) Neuron , vol.9 , pp. 307-313
    • Park, C.-S.1    Miller, C.2
  • 128
    • 0025966769 scopus 로고
    • Design, synthesis and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels
    • Park C.-S., Hausdorff S.F., and Miller C. Design, synthesis and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 2046-2050
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2046-2050
    • Park, C.-S.1    Hausdorff, S.F.2    Miller, C.3
  • 129
    • 0023685312 scopus 로고
    • Solution structure of apamin determined by nuclear magnetic resonance and distance geometry
    • Pease J.H.B., and Wemmer D.E. Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry 27 (1988) 8491-8498
    • (1988) Biochemistry , vol.27 , pp. 8491-8498
    • Pease, J.H.B.1    Wemmer, D.E.2
  • 130
    • 0022445599 scopus 로고
    • Dendrotoxin: a selective blocker of a non-inactivating potassium current in guinea pig dorsal root ganglion neurons
    • Penner R., Petersen M., Pierau F.-K., and Dreyer F. Dendrotoxin: a selective blocker of a non-inactivating potassium current in guinea pig dorsal root ganglion neurons. Pflüeger's Arch. 407 (1986) 365-369
    • (1986) Pflüeger's Arch. , vol.407 , pp. 365-369
    • Penner, R.1    Petersen, M.2    Pierau, F.-K.3    Dreyer, F.4
  • 132
    • 0029997350 scopus 로고    scopus 로고
    • Identification of three separate binding sites on SHK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocyte and rat brain
    • Pennington M.W., Mahnir V.M., Krafte D.S., Zaydenberg I., Byrnes M.E., Khaytin I., Crowley K., and Kem W.R. Identification of three separate binding sites on SHK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocyte and rat brain. Biochem. Biophys. Res. Commun. 219 (1996) 696-701
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 696-701
    • Pennington, M.W.1    Mahnir, V.M.2    Krafte, D.S.3    Zaydenberg, I.4    Byrnes, M.E.5    Khaytin, I.6    Crowley, K.7    Kem, W.R.8
  • 133
    • 0029038677 scopus 로고
    • Regulation of the activity of voltage-gated potassium channels by β subunits
    • Pongs O. Regulation of the activity of voltage-gated potassium channels by β subunits. Semin. Neurosci. 7 (1995) 137-146
    • (1995) Semin. Neurosci. , vol.7 , pp. 137-146
    • Pongs, O.1
  • 134
    • 51849183464 scopus 로고
    • The primary structure of Noxiustoxin: A K+ channel blocking peptide, purified from the venom of the scorpion Centruroides noxius Hoffmann
    • Possani L.D., Martin B.M., and Svendsen I.B. The primary structure of Noxiustoxin: A K+ channel blocking peptide, purified from the venom of the scorpion Centruroides noxius Hoffmann. Carlsberg Res. Commun. 47 (1982) 285-289
    • (1982) Carlsberg Res. Commun. , vol.47 , pp. 285-289
    • Possani, L.D.1    Martin, B.M.2    Svendsen, I.B.3
  • 135
    • 0024354763 scopus 로고
    • In vitro and in vivo comparison of two K+ channel openers diazoxide and cromakalim and their inhibition by glibenclamide
    • Quast U., and Cook N.S. In vitro and in vivo comparison of two K+ channel openers diazoxide and cromakalim and their inhibition by glibenclamide. J. Pharmacol. Exp. Ther. 250 (1989) 261-271
    • (1989) J. Pharmacol. Exp. Ther. , vol.250 , pp. 261-271
    • Quast, U.1    Cook, N.S.2
  • 136
    • 0023923539 scopus 로고
    • Existence of different populations of the dendrotoxin I binding protein associated with neuronal K+ channels
    • Rehm H., and Lazdunski M. Existence of different populations of the dendrotoxin I binding protein associated with neuronal K+ channels. Biochem. Biophys. Res. Commun. 153 (1988) 231-240
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 231-240
    • Rehm, H.1    Lazdunski, M.2
  • 137
    • 0024044104 scopus 로고
    • Purification and subunit structure of a putative K+-channel protein identified by its binding properties for dendrotoxin I
    • Rehm H., and Lazdunski M. Purification and subunit structure of a putative K+-channel protein identified by its binding properties for dendrotoxin I. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 4919-4923
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 4919-4923
    • Rehm, H.1    Lazdunski, M.2
  • 138
    • 0024294314 scopus 로고
    • The receptor site for bee venom mast cell degranulating peptide. Affinity labeling and evidence for a common target for mast cell degranulating peptide and dendrotoxin I, a snake toxin active on K+ channels
    • Rehm H., Bidard J.-N., Schweitz H., and Lazdunski M. The receptor site for bee venom mast cell degranulating peptide. Affinity labeling and evidence for a common target for mast cell degranulating peptide and dendrotoxin I, a snake toxin active on K+ channels. Biochemistry 27 (1988) 1827-1832
    • (1988) Biochemistry , vol.27 , pp. 1827-1832
    • Rehm, H.1    Bidard, J.-N.2    Schweitz, H.3    Lazdunski, M.4
  • 139
    • 0024375757 scopus 로고
    • Dendrotoxin-binding brain membrane protein displays a K+ channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations
    • Rehm H., Pelzer S., Cochet C., Chambaz E., Temple B.L., Trautwein W., Pelzer D., and Lazdunski M. Dendrotoxin-binding brain membrane protein displays a K+ channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations. Biochemistry 28 (1989) 6455-6460
    • (1989) Biochemistry , vol.28 , pp. 6455-6460
    • Rehm, H.1    Pelzer, S.2    Cochet, C.3    Chambaz, E.4    Temple, B.L.5    Trautwein, W.6    Pelzer, D.7    Lazdunski, M.8
  • 141
    • 0028181254 scopus 로고
    • Tityustoxin Kα blocks voltage-gated noninactivating K+ channels and unblocks inactivating K+ channels blocked by a-dendrotoxin in synaptosomes
    • Rogowski R.S., Krueger B.K., Collins J.H., and Blaustein M.P. Tityustoxin Kα blocks voltage-gated noninactivating K+ channels and unblocks inactivating K+ channels blocked by a-dendrotoxin in synaptosomes. Proc. Natl. Acad. Aci. U.S.A. 91 (1994) 1475-1479
    • (1994) Proc. Natl. Acad. Aci. U.S.A. , vol.91 , pp. 1475-1479
    • Rogowski, R.S.1    Krueger, B.K.2    Collins, J.H.3    Blaustein, M.P.4
  • 142
  • 144
    • 0027480617 scopus 로고
    • P05, a new leiurotoxin I-like scorpion toxin: Synthesis and structure-activity relationships of the α-amidated analog, a ligand of Ca2+-activated K+ channels with increased affinity
    • Sabatier J.-M., Zerrouk H., Darbon H., Mabrouk K., Benslimane A., Rochat H., Martin-Eauclaire M.-F., and Rietschoten J.V. P05, a new leiurotoxin I-like scorpion toxin: Synthesis and structure-activity relationships of the α-amidated analog, a ligand of Ca2+-activated K+ channels with increased affinity. Biochemistry 32 (1993) 2763-2770
    • (1993) Biochemistry , vol.32 , pp. 2763-2770
    • Sabatier, J.-M.1    Zerrouk, H.2    Darbon, H.3    Mabrouk, K.4    Benslimane, A.5    Rochat, H.6    Martin-Eauclaire, M.-F.7    Rietschoten, J.V.8
  • 146
    • 0029561629 scopus 로고
    • Cloning and functional expression of the cDNA encoding a novel ATP-sensitive potassium channel subunit expressed in pancreatic β-cells, brain, heart and skeletal muscle
    • Sakura H., Ämmälä C., Smith P.A., Gribble F.M., and Ashcroft F.M. Cloning and functional expression of the cDNA encoding a novel ATP-sensitive potassium channel subunit expressed in pancreatic β-cells, brain, heart and skeletal muscle. FEBS Lett. 377 (1995) 338-344
    • (1995) FEBS Lett. , vol.377 , pp. 338-344
    • Sakura, H.1    Ämmälä, C.2    Smith, P.A.3    Gribble, F.M.4    Ashcroft, F.M.5
  • 147
    • 0024318568 scopus 로고
    • Charybdotoxin blocks, voltage-gated K+ channels in human and murine T lymphocytes
    • Sands S.B., Lewis R.S., and Cahalan M.D. Charybdotoxin blocks, voltage-gated K+ channels in human and murine T lymphocytes. J. Gen. Physiol. 93 (1989) 1061-1074
    • (1989) J. Gen. Physiol. , vol.93 , pp. 1061-1074
    • Sands, S.B.1    Lewis, R.S.2    Cahalan, M.D.3
  • 150
    • 0029113262 scopus 로고
    • The voltage-dependent K+ channel (Kv1.5) cloned from rabbit heart and facilitation of inactivation of the delayed rectifier current by the rat β subunit
    • Sasaki Y., Ishii K., Nunoki K., Yamagishi T., and Taira N. The voltage-dependent K+ channel (Kv1.5) cloned from rabbit heart and facilitation of inactivation of the delayed rectifier current by the rat β subunit. FEBS Lett. 372 (1995) 20-24
    • (1995) FEBS Lett. , vol.372 , pp. 20-24
    • Sasaki, Y.1    Ishii, K.2    Nunoki, K.3    Yamagishi, T.4    Taira, N.5
  • 152
    • 0023028928 scopus 로고
    • Properties of the apamin-sensitive Ca2+-activated K+ channel in PC12 pheochromocytoma cells which hyper-produce the apamin receptor
    • Schmid-Antomarchi H., Hugues M., and Lazdunski M. Properties of the apamin-sensitive Ca2+-activated K+ channel in PC12 pheochromocytoma cells which hyper-produce the apamin receptor. J. Biol. Chetn. 261 (1986) 8633-8637
    • (1986) J. Biol. Chetn. , vol.261 , pp. 8633-8637
    • Schmid-Antomarchi, H.1    Hugues, M.2    Lazdunski, M.3
  • 153
    • 0025113314 scopus 로고
    • Purification and pharmacological characterization of peptide toxins from the black mamba (Dendroaspis polylepis) venom
    • Schweitz H., Bidard J.-N., and Lazdunski M. Purification and pharmacological characterization of peptide toxins from the black mamba (Dendroaspis polylepis) venom. Toxicon 28 (1990) 847-856
    • (1990) Toxicon , vol.28 , pp. 847-856
    • Schweitz, H.1    Bidard, J.-N.2    Lazdunski, M.3
  • 154
    • 0028865859 scopus 로고
    • Kalicludines and kaliseptine. Two different classes of sea anemone toxins for voltage-sensitive K+ channels
    • Schweitz H., Bruhn T., Guillemare E., Moinier D., Lancelin J.-M., Béress L., and Lazdunski M. Kalicludines and kaliseptine. Two different classes of sea anemone toxins for voltage-sensitive K+ channels. J. Biol. Chem. 270 (1995) 25121-25126
    • (1995) J. Biol. Chem. , vol.270 , pp. 25121-25126
    • Schweitz, H.1    Bruhn, T.2    Guillemare, E.3    Moinier, D.4    Lancelin, J.-M.5    Béress, L.6    Lazdunski, M.7
  • 155
  • 156
    • 0028333752 scopus 로고
    • Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of α-dendrotoxin-sensitive K+ channels in bovine brain
    • Scott V.E.S., Muniz Z.M., Sewing S., Lichtinghagen R., Parcej D.N., Pongs O., and Dolly J.O. Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of α-dendrotoxin-sensitive K+ channels in bovine brain. Biochemistry 33 (1994) 1617-1623
    • (1994) Biochemistry , vol.33 , pp. 1617-1623
    • Scott, V.E.S.1    Muniz, Z.M.2    Sewing, S.3    Lichtinghagen, R.4    Parcej, D.N.5    Pongs, O.6    Dolly, J.O.7
  • 158
    • 0021278878 scopus 로고
    • Interactions of the neurotoxin apamin with a Ca++ activated K+ channel in primary cultured neurons
    • Seagar M.J., Granier C., and Couraud F. Interactions of the neurotoxin apamin with a Ca++ activated K+ channel in primary cultured neurons. J. Biol. Chem. 259 (1984) 1491-1495
    • (1984) J. Biol. Chem. , vol.259 , pp. 1491-1495
    • Seagar, M.J.1    Granier, C.2    Couraud, F.3
  • 159
    • 0022473061 scopus 로고
    • Molecular structure of rat brain apamin receptor: differential photoaffinity labelling of putative K+ channel subunits and target size analysis
    • Seagar M.J., Labbe-Jullie C., Granier C., Goll A., Glossmann H., Rietschoten J.V., and Couraud F. Molecular structure of rat brain apamin receptor: differential photoaffinity labelling of putative K+ channel subunits and target size analysis. Biochemistry 25 (1986) 4051-4057
    • (1986) Biochemistry , vol.25 , pp. 4051-4057
    • Seagar, M.J.1    Labbe-Jullie, C.2    Granier, C.3    Goll, A.4    Glossmann, H.5    Rietschoten, J.V.6    Couraud, F.7
  • 160
    • 0028173889 scopus 로고
    • Engineering a uniquely reactive thiol into a cysteine-rich peptide
    • Shimony E., Sun T., Kolmakova-Partensky L., and Miller C. Engineering a uniquely reactive thiol into a cysteine-rich peptide. Protein Eng. 7 (1994) 503-507
    • (1994) Protein Eng. , vol.7 , pp. 503-507
    • Shimony, E.1    Sun, T.2    Kolmakova-Partensky, L.3    Miller, C.4
  • 162
    • 0022461362 scopus 로고
    • Noxiustoxin, a short-chain toxin from the Mexican scorpion CSentruroides noxius, induces transmitter release by blocking K+ permeability
    • Sitges M., Possani L.D., and Bayón A. Noxiustoxin, a short-chain toxin from the Mexican scorpion CSentruroides noxius, induces transmitter release by blocking K+ permeability. J. Neurosci. 6 (1986) 1570-1574
    • (1986) J. Neurosci. , vol.6 , pp. 1570-1574
    • Sitges, M.1    Possani, L.D.2    Bayón, A.3
  • 163
    • 0026511651 scopus 로고
    • Crystal structure of a-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor
    • Skarzynski T. Crystal structure of a-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 224 (1992) 671-683
    • (1992) J. Mol. Biol. , vol.224 , pp. 671-683
    • Skarzynski, T.1
  • 164
    • 0041108594 scopus 로고
    • Inhibition by toxins of charybdotoxin binding to the voltage-gated potassium channel of lymphocytes: Correlation with block of activation of human peripheral T-lymphocytes
    • Slaughter R.S., Shevell J.L., Felix J.P., Lin C.S., Sigal N.H., and Kaczorowski G.J. Inhibition by toxins of charybdotoxin binding to the voltage-gated potassium channel of lymphocytes: Correlation with block of activation of human peripheral T-lymphocytes. Biophys. J. 59 (1991) 213a
    • (1991) Biophys. J. , vol.59
    • Slaughter, R.S.1    Shevell, J.L.2    Felix, J.P.3    Lin, C.S.4    Sigal, N.H.5    Kaczorowski, G.J.6
  • 165
    • 0022854140 scopus 로고
    • Charybdotoxin, a specific inhibitor of the high conductance Ca2+-activated K+ channel
    • Smith C., Phillips M., and Miller C. Charybdotoxin, a specific inhibitor of the high conductance Ca2+-activated K+ channel. J. Biol. Chem. 261 (1986) 14607-14613
    • (1986) J. Biol. Chem. , vol.261 , pp. 14607-14613
    • Smith, C.1    Phillips, M.2    Miller, C.3
  • 167
    • 0024369430 scopus 로고
    • Rat brain dendrotoxin receptors associated with voltage-gated potassium channels: Dendrotoxin binding and receptor solubilization
    • Sorensen R.G., and Blaustein M.P. Rat brain dendrotoxin receptors associated with voltage-gated potassium channels: Dendrotoxin binding and receptor solubilization. Mol. Pharmacol. 36 (1989) 689-698
    • (1989) Mol. Pharmacol. , vol.36 , pp. 689-698
    • Sorensen, R.G.1    Blaustein, M.P.2
  • 168
    • 0030058762 scopus 로고    scopus 로고
    • Class III antiar-rhythmic drugs block HERG, a human cardiac delayed rectifier K+ channel
    • Spector P.S., Curran M.E., Keating M.T., and Sanguinetti M.C. Class III antiar-rhythmic drugs block HERG, a human cardiac delayed rectifier K+ channel. Circ. Res. 78 (1996) 499-503
    • (1996) Circ. Res. , vol.78 , pp. 499-503
    • Spector, P.S.1    Curran, M.E.2    Keating, M.T.3    Sanguinetti, M.C.4
  • 169
    • 0028117321 scopus 로고
    • Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin
    • Stampe P., Kolmakova-Partensky L., and Miller C. Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin. Biochemistry 33 (1994) 443-450
    • (1994) Biochemistry , vol.33 , pp. 443-450
    • Stampe, P.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 170
    • 0022635942 scopus 로고
    • 4-Aminopyridine and dendrotoxin induce repetitive firing in rat visceral sensory neurones by blocking a slowly inactivating outward current
    • Stansfeld C.E., Marsh S.J., Halliwell J.V., and Brown D.A. 4-Aminopyridine and dendrotoxin induce repetitive firing in rat visceral sensory neurones by blocking a slowly inactivating outward current. Neurosci. Lett. 64 (1986) 299-304
    • (1986) Neurosci. Lett. , vol.64 , pp. 299-304
    • Stansfeld, C.E.1    Marsh, S.J.2    Halliwell, J.V.3    Brown, D.A.4
  • 171
    • 0030064240 scopus 로고    scopus 로고
    • The modulation of the rate of inactivation of the mKv1.1 K+ channel by the β subunit, Kvβ1 and lack of effect of a Kvβ1 N-terminal peptide
    • Stephens G.J., Cockett M.I., Nawoschik S.P., Schecter L.E., and Owen D.G. The modulation of the rate of inactivation of the mKv1.1 K+ channel by the β subunit, Kvβ1 and lack of effect of a Kvβ1 N-terminal peptide. FEBS Lett. 378 (1996) 250-252
    • (1996) FEBS Lett. , vol.378 , pp. 250-252
    • Stephens, G.J.1    Cockett, M.I.2    Nawoschik, S.P.3    Schecter, L.E.4    Owen, D.G.5
  • 172
    • 0028031088 scopus 로고
    • Electrostatic distance geometry in a K+ channel vestibule
    • Stocker M., and Miller C. Electrostatic distance geometry in a K+ channel vestibule. Proc. Natl. Acad. Set. U.S.A. 91 (1994) 9509-9513
    • (1994) Proc. Natl. Acad. Set. U.S.A. , vol.91 , pp. 9509-9513
    • Stocker, M.1    Miller, C.2
  • 173
    • 0025081317 scopus 로고
    • Synthesis and structural characterization of charybdotoxin, a potent peptidyl inhibitor of the high conductance Ca2+-activated K+ channel
    • Sugg E.E., Garcia M.L., Reuben J.P., Patchett A.A., and Kaczorowski G.J. Synthesis and structural characterization of charybdotoxin, a potent peptidyl inhibitor of the high conductance Ca2+-activated K+ channel. J. Biol. Chem. 265 (1990) 18745-18748
    • (1990) J. Biol. Chem. , vol.265 , pp. 18745-18748
    • Sugg, E.E.1    Garcia, M.L.2    Reuben, J.P.3    Patchett, A.A.4    Kaczorowski, G.J.5
  • 174
    • 0028106688 scopus 로고
    • High-level expression and functional reconstitution of Shaker K+ channels
    • Sun T., Naini A.A., and Miller C. High-level expression and functional reconstitution of Shaker K+ channels. Biochemistry 33 (1994) 9992-9999
    • (1994) Biochemistry , vol.33 , pp. 9992-9999
    • Sun, T.1    Naini, A.A.2    Miller, C.3
  • 176
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz K.J., and MacKinnon R. An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron 15 (1995) 941-949
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 178
    • 0028579516 scopus 로고
    • Cloning, expression and distribution of functionally distinct Ca2+-activated K+ channel isoforms from human brain
    • Tseng-Crank J., Foster C.D., Krause J.D., Mertz R., Godinot N., DiChiara T.J., and Reinhart P.H. Cloning, expression and distribution of functionally distinct Ca2+-activated K+ channel isoforms from human brain. Neuron 13 (1994) 1315-1330
    • (1994) Neuron , vol.13 , pp. 1315-1330
    • Tseng-Crank, J.1    Foster, C.D.2    Krause, J.D.3    Mertz, R.4    Godinot, N.5    DiChiara, T.J.6    Reinhart, P.H.7
  • 179
    • 0028973231 scopus 로고
    • The α-dendrotoxin footprint on a mammalian potassium channel
    • Tytgat J., Debont T., Carmeliet E., and Daenens P. The α-dendrotoxin footprint on a mammalian potassium channel. J. Biol. Chem. 270 (1995) 24776-24781
    • (1995) J. Biol. Chem. , vol.270 , pp. 24776-24781
    • Tytgat, J.1    Debont, T.2    Carmeliet, E.3    Daenens, P.4
  • 180
    • 0030023714 scopus 로고    scopus 로고
    • Functional differences in Kv1.5 currents expressed in mammalian cell lines are due to the presence of endogenous Kvβ2.1 subunits
    • Uebele V.N., England S.K., Chaudhary A., Tamkun M.M., and Snyders D.J. Functional differences in Kv1.5 currents expressed in mammalian cell lines are due to the presence of endogenous Kvβ2.1 subunits. J. Biol. Chem. 271 (1996) 2406-2412
    • (1996) J. Biol. Chem. , vol.271 , pp. 2406-2412
    • Uebele, V.N.1    England, S.K.2    Chaudhary, A.3    Tamkun, M.M.4    Snyders, D.J.5
  • 181
    • 0024820005 scopus 로고
    • Characterization of high affinity binding sites for charybdotoxin in sarcolemmal membranes from bovine aortic smooth muscle: Evidence for a direct association with the high conductance calcium-activated potassium channel
    • Vazquez J., Feigenbaum P., Katz G., King V.F., Reuben J.P., Roy-Contancin L., Slaughter R.S., Kaczorowski G.J., and Garcia M.L. Characterization of high affinity binding sites for charybdotoxin in sarcolemmal membranes from bovine aortic smooth muscle: Evidence for a direct association with the high conductance calcium-activated potassium channel. J. Biol. Chem. 264 (1989) 20902-20909
    • (1989) J. Biol. Chem. , vol.264 , pp. 20902-20909
    • Vazquez, J.1    Feigenbaum, P.2    Katz, G.3    King, V.F.4    Reuben, J.P.5    Roy-Contancin, L.6    Slaughter, R.S.7    Kaczorowski, G.J.8    Garcia, M.L.9
  • 182
    • 0025113221 scopus 로고
    • Characterization of high affinity binding sites for charybdotoxin in synaptic plasma membranes from rat brain: Evidence for a direct association with an inactivating, voltage-dependent, potassium channel
    • Vazquez J., Feigenbaum P., King V.F., Kaczorowski G.J., and Garcia M.L. Characterization of high affinity binding sites for charybdotoxin in synaptic plasma membranes from rat brain: Evidence for a direct association with an inactivating, voltage-dependent, potassium channel. J. Biol. Chem. 256 (1990) 15564-15571
    • (1990) J. Biol. Chem. , vol.256 , pp. 15564-15571
    • Vazquez, J.1    Feigenbaum, P.2    King, V.F.3    Kaczorowski, G.J.4    Garcia, M.L.5
  • 184
    • 0008007880 scopus 로고
    • The novel benzopyranol potassium channel activator BRL55834 activates two potassium channels in bovine airway smooth muscle
    • Ward J.P.T., Taylor S.G., and Collier M.L. The novel benzopyranol potassium channel activator BRL55834 activates two potassium channels in bovine airway smooth muscle. Br. J. Pharmacol. 107 (1992) 49P
    • (1992) Br. J. Pharmacol. , vol.107
    • Ward, J.P.T.1    Taylor, S.G.2    Collier, M.L.3
  • 185
    • 0028001496 scopus 로고
    • Calcum sensitivity of BK-type KCa channels determined by a separable domain
    • Wei A., Solaro C., Lingle C., and Salkoff L. Calcum sensitivity of BK-type KCa channels determined by a separable domain. Neuron 13 (1994) 671-681
    • (1994) Neuron , vol.13 , pp. 671-681
    • Wei, A.1    Solaro, C.2    Lingle, C.3    Salkoff, L.4
  • 186
    • 0026796067 scopus 로고
    • Charybdotoxin, dendrotoxin and mast cell degranulating peptide block the voltage-activated K+ current of fibroblast cells stably transfected with NGK1 (Kv1.2) K+ channel complementary DNA
    • Werkman T.R., Kawamura T., Yokoyama S., Higashida H., and Rogawski M.A. Charybdotoxin, dendrotoxin and mast cell degranulating peptide block the voltage-activated K+ current of fibroblast cells stably transfected with NGK1 (Kv1.2) K+ channel complementary DNA. Neuroscience 4 (1992) 935-946
    • (1992) Neuroscience , vol.4 , pp. 935-946
    • Werkman, T.R.1    Kawamura, T.2    Yokoyama, S.3    Higashida, H.4    Rogawski, M.A.5
  • 187
    • 0025800956 scopus 로고
    • Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel
    • Yellen G., Jurman M.E., Abramson T., and MacKinnon R. Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel. Science 251 (1991) 939-942
    • (1991) Science , vol.251 , pp. 939-942
    • Yellen, G.1    Jurman, M.E.2    Abramson, T.3    MacKinnon, R.4
  • 188
    • 0023865687 scopus 로고
    • Concentration-dependent effects of tolbutamide, meglitinide, glipizide, glibenclamide and diazoxide on ATP-regulated K+ currents in pancreatic β-cells
    • Zünkler B.J., Lenzen S., Mauer K., Panten U., and Trube G. Concentration-dependent effects of tolbutamide, meglitinide, glipizide, glibenclamide and diazoxide on ATP-regulated K+ currents in pancreatic β-cells. Naunyn-Schmiedeberg's Arch. Pharmacol. 337 (1988) 225-230
    • (1988) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.337 , pp. 225-230
    • Zünkler, B.J.1    Lenzen, S.2    Mauer, K.3    Panten, U.4    Trube, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.