메뉴 건너뛰기




Volumn 43, Issue 8, 2004, Pages 901-908

Comparison of sea anemone and scorpion toxins binding to Kv1 channels: An example of convergent evolution

Author keywords

Kv1 channels; Scorpion; Sea anemone

Indexed keywords

ALANINE; AMINO ACID; LYSINE; SCORPION VENOM; SEA ANEMONE TOXIN; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 2942687338     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2004.03.029     Document Type: Article
Times cited : (32)

References (58)
  • 1
    • 0029989851 scopus 로고    scopus 로고
    • The signature sequence of voltage-gated potassium channels projects into the external vestibule
    • Aiyar J., Rizzi J.P., Gutman G.A., Chandy K.G. The signature sequence of voltage-gated potassium channels projects into the external vestibule. J. Biol. Chem. 271:1996;31013-31016
    • (1996) J. Biol. Chem. , vol.271 , pp. 31013-31016
    • Aiyar, J.1    Rizzi, J.P.2    Gutman, G.A.3    Chandy, K.G.4
  • 3
    • 0028339092 scopus 로고
    • Chemical synthesis and structure-function studies of margatoxin, a potent inhibitor of voltage-dependent potassium channel in human T lymphocytes
    • Bednarek M.A., Bugianesi R.M., Leonard R.J., Felix J.P. Chemical synthesis and structure-function studies of margatoxin, a potent inhibitor of voltage-dependent potassium channel in human T lymphocytes. Biochem. Biophys. Res. Commun. 198:1994;619-625
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 619-625
    • Bednarek, M.A.1    Bugianesi, R.M.2    Leonard, R.J.3    Felix, J.P.4
  • 4
    • 0042213113 scopus 로고    scopus 로고
    • Molecular dynamics of the KcsA K(+) channel in a bilayer membrane
    • Berneche S., Roux B. Molecular dynamics of the KcsA K(+) channel in a bilayer membrane. Biophys. J. 78:2000;2900-2917
    • (2000) Biophys. J. , vol.78 , pp. 2900-2917
    • Berneche, S.1    Roux, B.2
  • 5
    • 0035498860 scopus 로고    scopus 로고
    • Energetics of ion conduction through the K+ channel
    • Berneche S., Roux B. Energetics of ion conduction through the K+ channel. Nature. 414:2001;73-77
    • (2001) Nature , vol.414 , pp. 73-77
    • Berneche, S.1    Roux, B.2
  • 6
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems F., Roumestand C., Gilquin B., Menez A., 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
  • 9
    • 8044235836 scopus 로고    scopus 로고
    • A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity
    • Cotton J., Crest M., Bouet F., Alessandri N., Gola M., Forest E., Karlsson E., Castaneda O., Harvey A.L., Vita C., Menez A. A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity. Eur. J. Biochem. 244:1997;192-202
    • (1997) Eur. J. Biochem. , vol.244 , pp. 192-202
    • Cotton, J.1    Crest, M.2    Bouet, F.3    Alessandri, N.4    Gola, M.5    Forest, E.6    Karlsson, E.7    Castaneda, O.8    Harvey, A.L.9    Vita, C.10    Menez, A.11
  • 10
    • 0034880289 scopus 로고    scopus 로고
    • Extracellular blockade of K(+) channels by TEA: Results from molecular dynamics simulations of the KcsA channel
    • Crouzy S., Berneche S., Roux B. Extracellular blockade of K(+) channels by TEA: results from molecular dynamics simulations of the KcsA channel. J. Gen. Physiol. 118:2001;207-218
    • (2001) J. Gen. Physiol. , vol.118 , pp. 207-218
    • Crouzy, S.1    Berneche, S.2    Roux, B.3
  • 11
    • 6544276937 scopus 로고    scopus 로고
    • On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
    • Dauplais M., Lecoq A., Song J., Cotton J., Jamin N., Gilquin B., Roumestand C., Vita C., de Medeiros C.L., Rowan E.G., et al. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272:1997;4302-4309
    • (1997) J. Biol. Chem. , vol.272 , pp. 4302-4309
    • Dauplais, M.1    Lecoq, A.2    Song, J.3    Cotton, J.4    Jamin, N.5    Gilquin, B.6    Roumestand, C.7    Vita, C.8    De Medeiros, C.L.9    Rowan, E.G.10
  • 12
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano W.L., Ultsch M.H., de Vos A.M., Wells J.A. Convergent solutions to binding at a protein-protein interface. Science. 287:2000;1279-1283
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 13
    • 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. APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol. Pharmacol. 64:2003;59-69
    • (2003) Mol. Pharmacol. , vol.64 , pp. 59-69
    • Diochot, S.1    Loret, E.2    Bruhn, T.3    Beress, L.4    Lazdunski, M.5
  • 14
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle R.F. Convergent evolution: the need to be explicit. Trends Biochem. Sci. 19:1994;15-18
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 16
    • 0036840108 scopus 로고    scopus 로고
    • Modeling the structure of agitoxin in complex with the Shaker K+ channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • Eriksson M.A., Roux B. Modeling the structure of agitoxin in complex with the Shaker K+ channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles. Biophys. J. 83:2002;2595-2609
    • (2002) Biophys. J. , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 18
    • 0037999227 scopus 로고    scopus 로고
    • Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: Selectivity between voltage-gated and maxi-K channels
    • Gao Y.D., Garcia M.L. Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: selectivity between voltage-gated and maxi-K channels. Proteins. 52:2003;146-154
    • (2003) Proteins , vol.52 , pp. 146-154
    • Gao, Y.D.1    Garcia, M.L.2
  • 19
    • 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. Potassium channels: from scorpion venoms to high-resolution structure. Toxicon. 39:2001;739-748
    • (2001) Toxicon , vol.39 , pp. 739-748
    • Garcia, M.L.1    Gao, Y.2    McManus, O.B.3    Kaczorowski, G.J.4
  • 20
    • 0030885670 scopus 로고    scopus 로고
    • A new potassium channel toxin from the sea anemone Heteractis magnifica: Isolation, cDNA cloning, and functional expression
    • Gendeh G.S., Young L.C., de Medeiros C.L., Jeyaseelan K., Harvey A.L., Chung M.C. A new potassium channel toxin from the sea anemone Heteractis magnifica: isolation, cDNA cloning, and functional expression. Biochemistry. 36:1997;11461-11471
    • (1997) Biochemistry , vol.36 , pp. 11461-11471
    • Gendeh, G.S.1    Young, L.C.2    De Medeiros, C.L.3    Jeyaseelan, K.4    Harvey, A.L.5    Chung, M.C.6
  • 21
    • 0037020077 scopus 로고    scopus 로고
    • Structure of the BgK-Kv1.1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers
    • Gilquin B., Racape J., Wrisch A., Visan V., Lecoq A., Grissmer S., Menez A., Gasparini S. Structure of the BgK-Kv1.1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers. J. Biol. Chem. 277:2002;37406-37413
    • (2002) J. Biol. Chem. , vol.277 , pp. 37406-37413
    • Gilquin, B.1    Racape, J.2    Wrisch, A.3    Visan, V.4    Lecoq, A.5    Grissmer, S.6    Menez, A.7    Gasparini, S.8
  • 22
    • 0027443836 scopus 로고
    • Mechanism of charybdotoxin block of a voltage-gated K+ channel
    • Goldstein S.A., 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.1    Miller, C.2
  • 23
    • 0028276482 scopus 로고
    • The charybdotoxin receptor of a Shaker K+ channel: Peptide and channel residues mediating molecular recognition
    • Goldstein S.A., Pheasant D.J., 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.1    Pheasant, D.J.2    Miller, C.3
  • 24
    • 0030051784 scopus 로고    scopus 로고
    • Agitoxin footprinting the shaker potassium channel pore
    • Gross A., MacKinnon R. Agitoxin footprinting the shaker potassium channel pore. Neuron. 16:1996;399-406
    • (1996) Neuron , vol.16 , pp. 399-406
    • Gross, A.1    MacKinnon, R.2
  • 25
    • 0028105127 scopus 로고
    • Transfer of the scorpion toxin receptor to an insensitive potassium channel
    • Gross A., Abramson T., 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
  • 26
    • 0032875483 scopus 로고    scopus 로고
    • Single streptomyces lividans K(+) channels: Functional asymmetries and sidedness of proton activation
    • Heginbotham L., LeMasurier M., Kolmakova-Partensky L., Miller C. Single streptomyces lividans K(+) channels: functional asymmetries and sidedness of proton activation. J. Gen. Physiol. 114:1999;551-560
    • (1999) J. Gen. Physiol. , vol.114 , pp. 551-560
    • Heginbotham, L.1    Lemasurier, M.2    Kolmakova-Partensky, L.3    Miller, C.4
  • 27
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • Hidalgo P., 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
  • 29
    • 0033178906 scopus 로고    scopus 로고
    • Pharmacology of voltage-gated and calcium-activated potassium channels
    • Kaczorowski G.J., Garcia M.L. Pharmacology of voltage-gated and calcium-activated potassium channels. Curr. Opin. Chem. Biol. 3:1999;448-458
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 448-458
    • Kaczorowski, G.J.1    Garcia, M.L.2
  • 31
    • 0034714554 scopus 로고    scopus 로고
    • Convergent evolution with combinatorial peptides
    • Kay B.K., Kasanov J., Knight S., Kurakin A. Convergent evolution with combinatorial peptides. FEBS Lett. 480:2000;55-62
    • (2000) FEBS Lett. , vol.480 , pp. 55-62
    • Kay, B.K.1    Kasanov, J.2    Knight, S.3    Kurakin, A.4
  • 33
    • 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., 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
  • 34
    • 0037044313 scopus 로고    scopus 로고
    • Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel Kv1.3
    • Lanigan M.D., Kalman K., Lefievre Y., Pennington M.W., Chandy K.G., Norton R.S. Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel Kv1.3. Biochemistry. 41:2002;11963-11971
    • (2002) Biochemistry , vol.41 , pp. 11963-11971
    • Lanigan, M.D.1    Kalman, K.2    Lefievre, Y.3    Pennington, M.W.4    Chandy, K.G.5    Norton, R.S.6
  • 35
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon R., Cohen S.L., Kuo A., Lee A., Chait B.T. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:1998;106-109
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 36
    • 0025644364 scopus 로고
    • Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor
    • MacKinnon R., Heginbotham L., Abramson T. Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor. Neuron. 5:1990;767-771
    • (1990) Neuron , vol.5 , pp. 767-771
    • MacKinnon, R.1    Heginbotham, L.2    Abramson, T.3
  • 37
    • 0032079657 scopus 로고    scopus 로고
    • Primary structure of a potassium channel toxin from the sea anemone Actinia equina
    • Minagawa S., Ishida M., Nagashima Y., Shiomi K. Primary structure of a potassium channel toxin from the sea anemone Actinia equina. FEBS Lett. 427:1998;149-151
    • (1998) FEBS Lett. , vol.427 , pp. 149-151
    • Minagawa, S.1    Ishida, M.2    Nagashima, Y.3    Shiomi, K.4
  • 38
    • 0030002462 scopus 로고    scopus 로고
    • A symmetry-driven search for electrostatic interaction partners in charybdotoxin and a voltage-gated K+ channel
    • Naini A.A., Miller C. A symmetry-driven search for electrostatic interaction partners in charybdotoxin and a voltage-gated K+ channel. Biochemistry. 35:1996;6181-6187
    • (1996) Biochemistry , vol.35 , pp. 6181-6187
    • Naini, A.A.1    Miller, C.2
  • 39
    • 0030044863 scopus 로고    scopus 로고
    • A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K+ channel
    • Naranjo D., Miller C. A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K+ channel. Neuron. 16:1996;123-130
    • (1996) Neuron , vol.16 , pp. 123-130
    • Naranjo, D.1    Miller, C.2
  • 40
    • 0037053276 scopus 로고    scopus 로고
    • Mapping the binding site of a human ether-a-go-go-related gene-specific peptide toxin (ErgTx) to the channel's outer vestibule
    • Pardo-Lopez L., Zhang M., Liu J., Jiang M., Possani L.D., Tseng G.N. Mapping the binding site of a human ether-a-go-go-related gene-specific peptide toxin (ErgTx) to the channel's outer vestibule. J. Biol. Chem. 277:2002;16403-16411
    • (2002) J. Biol. Chem. , vol.277 , pp. 16403-16411
    • Pardo-Lopez, L.1    Zhang, M.2    Liu, J.3    Jiang, M.4    Possani, L.D.5    Tseng, G.N.6
  • 41
    • 0026803224 scopus 로고
    • Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel
    • Park C.S., 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
  • 42
  • 43
    • 0033001043 scopus 로고    scopus 로고
    • Voltage-gated potassium channels: From hyperexcitability to excitement
    • Pongs O. Voltage-gated potassium channels: from hyperexcitability to excitement. FEBS Lett. 452:1999;31-35
    • (1999) FEBS Lett. , vol.452 , pp. 31-35
    • Pongs, O.1
  • 44
    • 0037040249 scopus 로고    scopus 로고
    • Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain
    • Racape J., Lecoq A., Romi-Lebrun R., Liu J., Kohler M., Garcia M.L., Menez A., Gasparini S. Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain. J. Biol. Chem. 277:2002;3886-3893
    • (2002) J. Biol. Chem. , vol.277 , pp. 3886-3893
    • Racape, J.1    Lecoq, A.2    Romi-Lebrun, R.3    Liu, J.4    Kohler, M.5    Garcia, M.L.6    Menez, A.7    Gasparini, S.8
  • 45
    • 0030064382 scopus 로고    scopus 로고
    • Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis
    • Ranganathan R., Lewis J.H., MacKinnon R. Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis. Neuron. 16:1996;131-139
    • (1996) Neuron , vol.16 , pp. 131-139
    • Ranganathan, R.1    Lewis, J.H.2    MacKinnon, R.3
  • 46
    • 0033966212 scopus 로고    scopus 로고
    • Structure-guided transformation of charybdotoxin yields an analog that selectively targets Ca(2+)-activated over voltage-gated K(+) channels
    • Rauer H., Lanigan M.D., Pennington M.W., Aiyar J., Ghanshani S., Cahalan M.D., Norton R.S., Chandy K.G. Structure-guided transformation of charybdotoxin yields an analog that selectively targets Ca(2+)-activated over voltage-gated K(+) channels. J. Biol. Chem. 275:2000;1201-1208
    • (2000) J. Biol. Chem. , vol.275 , pp. 1201-1208
    • Rauer, H.1    Lanigan, M.D.2    Pennington, M.W.3    Aiyar, J.4    Ghanshani, S.5    Cahalan, M.D.6    Norton, R.S.7    Chandy, K.G.8
  • 47
    • 0033618255 scopus 로고    scopus 로고
    • Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin
    • Rauer H., Pennington M., Cahalan M., Chandy K.G. Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J. Biol. Chem. 274:1999;21885-21892
    • (1999) J. Biol. Chem. , vol.274 , pp. 21885-21892
    • Rauer, H.1    Pennington, M.2    Cahalan, M.3    Chandy, K.G.4
  • 49
    • 0037435021 scopus 로고    scopus 로고
    • Functional analysis of an archaebacterial voltage-dependent K+ channel
    • Ruta V., Jiang Y., Lee A., Chen J., MacKinnon R. Functional analysis of an archaebacterial voltage-dependent K+ channel. Nature. 422:2003;180-185
    • (2003) Nature , vol.422 , pp. 180-185
    • Ruta, V.1    Jiang, Y.2    Lee, A.3    Chen, J.4    MacKinnon, R.5
  • 50
    • 0027480617 scopus 로고
    • P05, a new leiurotoxin I-like scorpion toxin: Synthesis and structure-activity relationships of the alpha-amidated analog, a ligand of Ca(2+)-activated K+ channels with increased affinity
    • Sabatier J.M., Zerrouk H., Darbon H., Mabrouk K., Benslimane A., Rochat H., Martin-Eauclaire M.F., Van Rietschoten J. P05, a new leiurotoxin I-like scorpion toxin: synthesis and structure-activity relationships of the alpha-amidated analog, a ligand of Ca(2+)-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    Van Rietschoten, J.8
  • 51
    • 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., Beress L., 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    Beress, L.6    Lazdunski, M.7
  • 52
    • 0028117321 scopus 로고
    • Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin
    • Stampe P., Kolmakova-Partensky L., 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
  • 53
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • Terlau H., Shon K.J., Grilley M., Stocker M., Stuhmer W., Olivera B.M. Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 381:1996;148-151
    • (1996) Nature , vol.381 , pp. 148-151
    • Terlau, H.1    Shon, K.J.2    Grilley, M.3    Stocker, M.4    Stuhmer, W.5    Olivera, B.M.6
  • 54
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • Tudor J.E., Pallaghy P.K., Pennington M.W., Norton R.S. Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. Nat. Struct. Biol. 3:1996;317-320
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 317-320
    • Tudor, J.E.1    Pallaghy, P.K.2    Pennington, M.W.3    Norton, R.S.4
  • 56
    • 0034671888 scopus 로고    scopus 로고
    • Structural differences of bacterial and mammalian K+ channels
    • Wrisch A., Grissmer S. Structural differences of bacterial and mammalian K+ channels. J. Biol. Chem. 275:2000;39345-39353
    • (2000) J. Biol. Chem. , vol.275 , pp. 39345-39353
    • Wrisch, A.1    Grissmer, S.2
  • 57
    • 0036037576 scopus 로고    scopus 로고
    • Convergent evolution on the molecular level
    • Zakon H.H. Convergent evolution on the molecular level. Brain Behav. Evol. 59:2002;250-261
    • (2002) Brain Behav. Evol. , vol.59 , pp. 250-261
    • Zakon, H.H.1
  • 58
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 a resolution
    • Zhou Y., Morais-Cabral J.H., Kaufman A., MacKinnon R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature. 414:2001;43-48
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.