메뉴 건너뛰기




Volumn 46, Issue 18, 2007, Pages 5358-5364

Revealing the molecular determinants of neurotoxin specificity for calcium-activated versus voltage-dependent potassium channels

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; DISEASES; ELECTRIC POTENTIAL; FREE ENERGY; MOLECULAR STRUCTURE; POTASSIUM;

EID: 34248143507     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700150t     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft, F. M. (2006) From molecule to malady, Nature 440, 440-447.
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 3
    • 27544460565 scopus 로고    scopus 로고
    • Potassium channels, memory T cells, and multiple sclerosis
    • Beeton, C., and Chandy, K. G. (2005) Potassium channels, memory T cells, and multiple sclerosis, Neuroscientist 11, 550-562.
    • (2005) Neuroscientist , vol.11 , pp. 550-562
    • Beeton, C.1    Chandy, K.G.2
  • 6
    • 33644877489 scopus 로고    scopus 로고
    • Potassium channels as targets for therapeutic intervention
    • Garcia, M. L., and Kaczorowski, G. J. (2005) Potassium channels as targets for therapeutic intervention, Sci. STKE 302, 46.
    • (2005) Sci. STKE , vol.302 , pp. 46
    • Garcia, M.L.1    Kaczorowski, G.J.2
  • 7
    • 2942691708 scopus 로고    scopus 로고
    • Molecular basis of α-KTx specificity
    • Giangiacomo, K. M., Ceralde, Y., and Mullmann, T. J. (2004) Molecular basis of α-KTx specificity, Toxicon 43, 877-886.
    • (2004) Toxicon , vol.43 , pp. 877-886
    • Giangiacomo, K.M.1    Ceralde, Y.2    Mullmann, T.J.3
  • 9
    • 2942668352 scopus 로고    scopus 로고
    • BK potassium channels control transmitter release at CA3-CA3 synapses in the rat hippocampus
    • Raffaelli, G., Saviane, C., Mohajerani, M. H., Pedarzani, P., and Cherubini, E. (2004) BK potassium channels control transmitter release at CA3-CA3 synapses in the rat hippocampus, J. Physiol. 557, 147-157.
    • (2004) J. Physiol , vol.557 , pp. 147-157
    • Raffaelli, G.1    Saviane, C.2    Mohajerani, M.H.3    Pedarzani, P.4    Cherubini, E.5
  • 10
    • 0037063370 scopus 로고    scopus 로고
    • Glycine 30 in iberiotoxin is a critical determinant of its specificity for maxi-K versus K(V) channels
    • Schroeder, N., Mullmann, T. J., Schmalhofer, W. A., Gao, Y. D., Garcia, M. L., and Giangiacomo, K. M. (2002) Glycine 30 in iberiotoxin is a critical determinant of its specificity for maxi-K versus K(V) channels, FEBS Lett. 527, 298-302.
    • (2002) FEBS Lett , vol.527 , pp. 298-302
    • Schroeder, N.1    Mullmann, T.J.2    Schmalhofer, W.A.3    Gao, Y.D.4    Garcia, M.L.5    Giangiacomo, K.M.6
  • 13
    • 0023732047 scopus 로고
    • Use of simian virus 40 replication to amplify Epstein-Barr virus shuttle vectors in human cells
    • Heinzel, S. S., Krysan, P. J., Calos, M. P., and DuBridge, R. B. (1988) Use of simian virus 40 replication to amplify Epstein-Barr virus shuttle vectors in human cells, J. Virol. 62, 3738-3746.
    • (1988) J. Virol , vol.62 , pp. 3738-3746
    • Heinzel, S.S.1    Krysan, P.J.2    Calos, M.P.3    DuBridge, R.B.4
  • 14
    • 0032569024 scopus 로고    scopus 로고
    • The β subunit of the high conductance calcium-activated potassium channel. Identification of residues involved in charybdotoxin binding
    • Hanner, M., Vianna-Jorge, R., Kamassah, A., Schmalhofer, W. A., Knaus, H. G., Kaczorowski, G. J., and Garcia, M. L. (1998) The β subunit of the high conductance calcium-activated potassium channel. Identification of residues involved in charybdotoxin binding, J. Biol. Chem. 273, 16289-16296.
    • (1998) J. Biol. Chem , vol.273 , pp. 16289-16296
    • Hanner, M.1    Vianna-Jorge, R.2    Kamassah, A.3    Schmalhofer, W.A.4    Knaus, H.G.5    Kaczorowski, G.J.6    Garcia, M.L.7
  • 16
    • 0033596702 scopus 로고    scopus 로고
    • Electrostatic mutations in iberiotoxin as a unique tool for probing the electrostatic structure of the maxi-K channel outer vestibule
    • Mullmann, T. J., Munujos, P., Garcia, M. L., and Giangiacomo, K. M. (1999) Electrostatic mutations in iberiotoxin as a unique tool for probing the electrostatic structure of the maxi-K channel outer vestibule, Biochemistry 38, 2395-2402.
    • (1999) Biochemistry , vol.38 , pp. 2395-2402
    • Mullmann, T.J.1    Munujos, P.2    Garcia, M.L.3    Giangiacomo, K.M.4
  • 17
    • 0023432178 scopus 로고
    • An accurate method for determination of receptor-ligand and enzyme-inhibitor dissociation constants from displacement curves
    • Horovitz, A., and Levitzki, A. (1987) An accurate method for determination of receptor-ligand and enzyme-inhibitor dissociation constants from displacement curves, Proc. Natl. Acad. Sci. U.S.A. 84, 6654-6658.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 6654-6658
    • Horovitz, A.1    Levitzki, A.2
  • 18
    • 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. (1992) Mechanism of iberiotoxin block of the large-conductance calcium-activated potassium channel from bovine aortic smooth muscle, Biochemistry 31, 6719-6727.
    • (1992) Biochemistry , vol.31 , pp. 6719-6727
    • Giangiacomo, K.M.1    Garcia, M.L.2    McManus, O.B.3
  • 19
    • 0034705177 scopus 로고    scopus 로고
    • Interaction of charybdotoxin S10A with single maxi-K channels: Kinetics of blockade depend on the presence of the β1 subunit
    • Giangiacomo, K. M., Fremont, V., Mullmann, T. J., Hanner, M., Cox, R. H., and Garcia, M. L. (2000) Interaction of charybdotoxin S10A with single maxi-K channels: Kinetics of blockade depend on the presence of the β1 subunit, Biochemistry 39, 6115-6122.
    • (2000) Biochemistry , vol.39 , pp. 6115-6122
    • Giangiacomo, K.M.1    Fremont, V.2    Mullmann, T.J.3    Hanner, M.4    Cox, R.H.5    Garcia, M.L.6
  • 21
    • 0036840108 scopus 로고    scopus 로고
    • + channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • + channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles, Biophys. J. 83, 2595-2609.
    • (2002) Biophys. J , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 22
    • 2942677403 scopus 로고    scopus 로고
    • Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel
    • Yu, K., Fu, W., Liu, H., Luo, X., Chen, K. X., Ding, J., Shen, J., and Jiang, H. (2004) Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel, Biophys. J. 86, 3542-3555.
    • (2004) Biophys. J , vol.86 , pp. 3542-3555
    • Yu, K.1    Fu, W.2    Liu, H.3    Luo, X.4    Chen, K.X.5    Ding, J.6    Shen, J.7    Jiang, H.8
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: Isights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association: Isights from the interfacial and thermodynamic properties of hydrocarbons, Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 0030064382 scopus 로고    scopus 로고
    • + channel selectivity filter by mutant cycle-based structure analysis
    • + channel selectivity filter by mutant cycle-based structure analysis, Neuron 16, 131-139.
    • (1996) Neuron , vol.16 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    MacKinnon, R.3
  • 26
    • 0028987938 scopus 로고
    • + channel pore through mutant cycles with a peptide inhibitor
    • + channel pore through mutant cycles with a peptide inhibitor, Science 268, 307-310.
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 28
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • Lange, A., Giller, K., Hornig, S., Martin-Eauclaire, M. F., Pongs, O., Becker, S., and Baldus, M. (2006) Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR, Nature 440, 959-962.
    • (2006) Nature , vol.440 , pp. 959-962
    • Lange, A.1    Giller, K.2    Hornig, S.3    Martin-Eauclaire, M.F.4    Pongs, O.5    Becker, S.6    Baldus, M.7
  • 29
    • 0028276482 scopus 로고
    • + channel: Peptide and channel residues mediating molecular recognition
    • + channel: Peptide and channel residues mediating molecular recognition, Neuron 12, 1377-1388.
    • (1994) Neuron , vol.12 , pp. 1377-1388
    • Goldstein, S.A.1    Pheasant, D.J.2    Miller, C.3
  • 30
    • 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. (1991) Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins, Science 254, 1521-1523.
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 31
    • 0026781766 scopus 로고
    • 1H nuclear magnetic resonance spectroscopy
    • 1H nuclear magnetic resonance spectroscopy, Biochemistry 31, 8151-8159.
    • (1992) Biochemistry , vol.31 , pp. 8151-8159
    • Johnson, B.A.1    Sugg, E.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.