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Volumn 68, Issue 2, 2007, Pages 568-580

Drug block of the hERG potassium channel: Insight from modeling

Author keywords

Drug block; Gating; Helix motion; hERG; Molecular modeling; Potassium channel

Indexed keywords

1 [2 (6 METHYL 2 PYRIDYL)ETHYL] 4 (4 METHYLSULFONYLAMINOBENZOYL)PIPERIDINE; 1' (6 CYANO 1,2,3,4 TETRAHYDRO 2 NAPHTHYL) 3,4 DIHYDRO 6 METHANESULFONAMIDOSPIRO[2H 1 BENZOPYRAN 2,4' PIPERIDIN] 4 OL; AMIODARONE; ASTEMIZOLE; CETIRIZINE; CHLOROQUINE; CISAPRIDE; CLOFILIUM; DOFETILIDE; DRONEDARONE; FEXOFENADINE; FLUVOXAMINE; GLYCINE; IBUTILIDE; LIGAND; LORATADINE; MOSAPRIDE CITRATE; PIPERANOMETOZINE; POTASSIUM CHANNEL HERG; PROPAFENONE; QUINIDINE; SERTINDOLE; TERFENADINE;

EID: 34250836484     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21400     Document Type: Article
Times cited : (101)

References (75)
  • 1
    • 0029002969 scopus 로고
    • A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel
    • Sanguinetti MC, Jiang C, Curran ME, Keating MT. A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel. Cell 1995; 81:299-307.
    • (1995) Cell , vol.81 , pp. 299-307
    • Sanguinetti, M.C.1    Jiang, C.2    Curran, M.E.3    Keating, M.T.4
  • 2
    • 0034975654 scopus 로고    scopus 로고
    • I(Kr): The hERG channel
    • Tseng GN. I(Kr): the hERG channel. J Mol Cell Cardiol 2001; 33:835-849.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 835-849
    • Tseng, G.N.1
  • 4
    • 0035936798 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cardiac arrhythmias
    • Keating MT, Sanguinetti MC. Molecular and cellular mechanisms of cardiac arrhythmias. Cell 2001;104:569-580.
    • (2001) Cell , vol.104 , pp. 569-580
    • Keating, M.T.1    Sanguinetti, M.C.2
  • 5
    • 0038471102 scopus 로고    scopus 로고
    • The impact of drug-induced QT interval prolongation on drug discovery and development
    • Fermini B, Fossa AA. The impact of drug-induced QT interval prolongation on drug discovery and development. Nat Rev Drug Discov 2003;2:439-447.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 439-447
    • Fermini, B.1    Fossa, A.A.2
  • 6
    • 14544268139 scopus 로고    scopus 로고
    • QT prolongation through hERG K(+) channel blockade: Current knowledge and strategies for the early prediction during drug development
    • Recanatini M, Poluzzi E, Masetti M, Cavalli A, De Ponti F. QT prolongation through hERG K(+) channel blockade: current knowledge and strategies for the early prediction during drug development. Med Res Rev 2005;25:133-166.
    • (2005) Med Res Rev , vol.25 , pp. 133-166
    • Recanatini, M.1    Poluzzi, E.2    Masetti, M.3    Cavalli, A.4    De Ponti, F.5
  • 7
    • 14644412444 scopus 로고    scopus 로고
    • Predicting drug-hERG channel interactions that cause acquired long QT syndrome
    • Sanguinetti MC, Mitcheson JS. Predicting drug-hERG channel interactions that cause acquired long QT syndrome. Trends Pharmacol Sci 2005;26:119-124.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 119-124
    • Sanguinetti, M.C.1    Mitcheson, J.S.2
  • 8
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to eag in Drosophila and mammals
    • Warmke JW, Ganetzky B. A family of potassium channel genes related to eag in Drosophila and mammals. Proc Natl Acad Sci USA 1994;91:3438-3442.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3438-3442
    • Warmke, J.W.1    Ganetzky, B.2
  • 9
    • 0036845677 scopus 로고    scopus 로고
    • Structural and functional role of the extracellular s5-p linker in the HERG potassium channel
    • Liu J, Zhang M, Jiang M, Tseng GN. Structural and functional role of the extracellular s5-p linker in the HERG potassium channel. J Gen Physiol 2002;120:723-737.
    • (2002) J Gen Physiol , vol.120 , pp. 723-737
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.N.4
  • 11
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: A eukaryotic PAS domain
    • Morais Cabral JH, Lee A, Cohen SL, Chait BT, Li M, Mackinnon R. Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell 1998;95:649-655.
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    Mackinnon, R.6
  • 12
    • 0033818157 scopus 로고    scopus 로고
    • Trapping of a methanesulfonanilide by closure of the HERG potassium channel activation gate
    • Mitcheson JS, Chen J, Sanguinetti MC. Trapping of a methanesulfonanilide by closure of the HERG potassium channel activation gate. J Gen Physiol 2000;115:229-240.
    • (2000) J Gen Physiol , vol.115 , pp. 229-240
    • Mitcheson, J.S.1    Chen, J.2    Sanguinetti, M.C.3
  • 13
    • 0030058762 scopus 로고    scopus 로고
    • Class III antiarrhythmic drugs block HERG, a human cardiac delayed rectifier K+ channel. Open-channel block by methanesulfonanilides
    • Spector PS, Curran ME, Keating MT, Sanguinetti MC. Class III antiarrhythmic drugs block HERG, a human cardiac delayed rectifier K+ channel. Open-channel block by methanesulfonanilides. Circ Res 1996;78:499-503.
    • (1996) Circ Res , vol.78 , pp. 499-503
    • Spector, P.S.1    Curran, M.E.2    Keating, M.T.3    Sanguinetti, M.C.4
  • 18
    • 31044447745 scopus 로고    scopus 로고
    • Drug binding interactions in the inner cavity of HERG channels: Molecular insights from structure-activity relationships of clofilium and ibutilide analogs
    • Perry M, Stansfeld PJ, Leaney J, Wood C, de Groot MJ, Leishman D, Sutcliffe MJ, Mitcheson JS. Drug binding interactions in the inner cavity of HERG channels: molecular insights from structure-activity relationships of clofilium and ibutilide analogs. Mol Pharmacol 2006;69:509-519.
    • (2006) Mol Pharmacol , vol.69 , pp. 509-519
    • Perry, M.1    Stansfeld, P.J.2    Leaney, J.3    Wood, C.4    de Groot, M.J.5    Leishman, D.6    Sutcliffe, M.J.7    Mitcheson, J.S.8
  • 19
    • 1642370447 scopus 로고    scopus 로고
    • Physicochemical features of the HERG channel drug binding site
    • Fernandez D, Ghanta A, Kauffman GW, Sanguinetti MC. Physicochemical features of the HERG channel drug binding site. J Biol Chem 2004;279:10120- 10127.
    • (2004) J Biol Chem , vol.279 , pp. 10120-10127
    • Fernandez, D.1    Ghanta, A.2    Kauffman, G.W.3    Sanguinetti, M.C.4
  • 20
  • 21
    • 0038407463 scopus 로고    scopus 로고
    • Voltage-dependent profile of human ether-a-go-go-related gene channel block is influenced by a single residue in the S6 transmembrane domain
    • Sanchez-Chapula JA, Ferrer T, Navarro-Polanco RA, Sanguinetti MC. Voltage-dependent profile of human ether-a-go-go-related gene channel block is influenced by a single residue in the S6 transmembrane domain. Mol Pharmacol 2003;63:1051-1058.
    • (2003) Mol Pharmacol , vol.63 , pp. 1051-1058
    • Sanchez-Chapula, J.A.1    Ferrer, T.2    Navarro-Polanco, R.A.3    Sanguinetti, M.C.4
  • 22
    • 0037194634 scopus 로고    scopus 로고
    • Toward a pharmacophore for drugs inducing the long QT syndrome: Insights from a CoMFA study of HERG K(+) channel blockers
    • Cavalli A, Poluzzi E, De Ponti F, Recanatini M. Toward a pharmacophore for drugs inducing the long QT syndrome: insights from a CoMFA study of HERG K(+) channel blockers. J Med Chem 2002;45:3844-3853.
    • (2002) J Med Chem , vol.45 , pp. 3844-3853
    • Cavalli, A.1    Poluzzi, E.2    De Ponti, F.3    Recanatini, M.4
  • 24
    • 0035850941 scopus 로고    scopus 로고
    • An amino acid residue whose change by mutation affects drug binding to the HERG channel
    • Ishii K, Kondo K, Takahashi M, Kimura M, Endoh M. An amino acid residue whose change by mutation affects drug binding to the HERG channel. FEBS Lett 2001;506:191-195.
    • (2001) FEBS Lett , vol.506 , pp. 191-195
    • Ishii, K.1    Kondo, K.2    Takahashi, M.3    Kimura, M.4    Endoh, M.5
  • 25
    • 2142808323 scopus 로고    scopus 로고
    • Molecular determinants for high-affinity block of human EAG potassium channels by antiarrhythmic agents
    • Gessner G, Zacharias M, Bechstedt S, Schonherr R, Heinemann SH. Molecular determinants for high-affinity block of human EAG potassium channels by antiarrhythmic agents. Mol Pharmacol 2004;65:1120-1129.
    • (2004) Mol Pharmacol , vol.65 , pp. 1120-1129
    • Gessner, G.1    Zacharias, M.2    Bechstedt, S.3    Schonherr, R.4    Heinemann, S.H.5
  • 27
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 2002;417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 30
    • 19444375852 scopus 로고    scopus 로고
    • Exploring blocker binding to a homology model of the open hERG K+ channel using docking and molecular dynamics methods
    • Osterberg F, Aqvist J. Exploring blocker binding to a homology model of the open hERG K+ channel using docking and molecular dynamics methods. FEBS Lett 2005;579:2939-2944.
    • (2005) FEBS Lett , vol.579 , pp. 2939-2944
    • Osterberg, F.1    Aqvist, J.2
  • 31
    • 33644967111 scopus 로고    scopus 로고
    • New insights about HERG blockade obtained from protein modeling, potential energy mapping, and docking studies
    • Farid R, Day T, Friesner RA, Pearlstein RA. New insights about HERG blockade obtained from protein modeling, potential energy mapping, and docking studies. Bioorg Med Chem 2006; 14:3160-3173.
    • (2006) Bioorg Med Chem , vol.14 , pp. 3160-3173
    • Farid, R.1    Day, T.2    Friesner, R.A.3    Pearlstein, R.A.4
  • 32
    • 14644392097 scopus 로고    scopus 로고
    • A two-state homology model of the hERG K+ channel: Application to ligand binding
    • Rajamani R, Tounge BA, Li J, Reynolds CH. A two-state homology model of the hERG K+ channel: application to ligand binding. Bioorg Med Chem Lett 2005;15:1737-1741.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 1737-1741
    • Rajamani, R.1    Tounge, B.A.2    Li, J.3    Reynolds, C.H.4
  • 33
    • 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 JH, Kaufman A, MacKinnon R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature 2001;414:43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 34
    • 6344285843 scopus 로고    scopus 로고
    • Conserved gating hinge in ligand- and voltage-dependent K+ channels
    • Magidovich E, Yifrach O. Conserved gating hinge in ligand- and voltage-dependent K+ channels. Biochemistry 2004;43:13242-13247.
    • (2004) Biochemistry , vol.43 , pp. 13242-13247
    • Magidovich, E.1    Yifrach, O.2
  • 36
    • 0037126062 scopus 로고    scopus 로고
    • Position of aromatic residues in the S6 domain, not inactivation, dictates cisapride sensitivity of HERG and eag potassium channels
    • Chen J, Seebohm G, Sanguinetti MC. Position of aromatic residues in the S6 domain, not inactivation, dictates cisapride sensitivity of HERG and eag potassium channels. Proc Natl Acad Sci USA 2002;99:12461-12466.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12461-12466
    • Chen, J.1    Seebohm, G.2    Sanguinetti, M.C.3
  • 37
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 38
    • 0032570779 scopus 로고    scopus 로고
    • Do transmembrane protein superfolds exist?
    • Jones DT. Do transmembrane protein superfolds exist? FEBS Lett 1998;423:281-285.
    • (1998) FEBS Lett , vol.423 , pp. 281-285
    • Jones, D.T.1
  • 39
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics 2000;16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 44
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou M, Morais-Cabral JH, Mann S, MacKinnon R. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature 2001;411:657-661.
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 45
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long SB, Campbell EB, Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 2005;309:897-903.
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999; 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 48
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 49
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RK, Sali A. Modeling of loops in protein structures. Protein Sci 2000;9:1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 50
    • 3242875210 scopus 로고    scopus 로고
    • Suhre K, Sanejouand YH. ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res 2004;32(Web Server issue):W610-W614.
    • Suhre K, Sanejouand YH. ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res 2004;32(Web Server issue):W610-W614.
  • 52
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane-proteins
    • Schiffer M, Chang CH, Stevens FJ. The functions of tryptophan residues in membrane-proteins. Protein Eng 1992;5:213-214.
    • (1992) Protein Eng , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.H.2    Stevens, F.J.3
  • 53
    • 0037623288 scopus 로고    scopus 로고
    • Sequence-function analysis of the K+-selective family of ion channels using a comprehensive alignment and the KcsA channel structure
    • Shealy RT, Murphy AD, Ramarathnam R, Jakobsson E, Subramaniam S. Sequence-function analysis of the K+-selective family of ion channels using a comprehensive alignment and the KcsA channel structure. Biophys J 2003;84:2929-2942.
    • (2003) Biophys J , vol.84 , pp. 2929-2942
    • Shealy, R.T.1    Murphy, A.D.2    Ramarathnam, R.3    Jakobsson, E.4    Subramaniam, S.5
  • 54
    • 0037129911 scopus 로고    scopus 로고
    • Pharmacological rescue of human K(+) channel long-QT2 mutations: Human ether-a-go-go-related gene rescue without block
    • Rajamani S, Anderson CL, Anson BD, January CT. Pharmacological rescue of human K(+) channel long-QT2 mutations: human ether-a-go-go-related gene rescue without block. Circulation 2002;105:2830-2835.
    • (2002) Circulation , vol.105 , pp. 2830-2835
    • Rajamani, S.1    Anderson, C.L.2    Anson, B.D.3    January, C.T.4
  • 55
    • 0032559552 scopus 로고    scopus 로고
    • Molecular determinants of dofetilide block of HERG K+ channels
    • Ficker E, Jarolimek W, Kiehn J, Baumann A, Brown AM. Molecular determinants of dofetilide block of HERG K+ channels. Circ Res 1998;82(3):386-395.
    • (1998) Circ Res , vol.82 , Issue.3 , pp. 386-395
    • Ficker, E.1    Jarolimek, W.2    Kiehn, J.3    Baumann, A.4    Brown, A.M.5
  • 56
    • 0032410714 scopus 로고    scopus 로고
    • The antipsychotic agent sertindole is a high affinity antagonist of the human cardiac potassium channel HERG
    • Rampe D, Murawsky MK, Grau J, Lewis EW. The antipsychotic agent sertindole is a high affinity antagonist of the human cardiac potassium channel HERG. J Pharmacol Exp Ther 1998; 286(2):788-793.
    • (1998) J Pharmacol Exp Ther , vol.286 , Issue.2 , pp. 788-793
    • Rampe, D.1    Murawsky, M.K.2    Grau, J.3    Lewis, E.W.4
  • 57
    • 0035499447 scopus 로고    scopus 로고
    • Energetic optimization of ion conduction rate by the K+ selectivity filter
    • Morais-Cabral JH, Zhou Y, MacKinnon R. Energetic optimization of ion conduction rate by the K+ selectivity filter. Nature 2001;414:37-42.
    • (2001) Nature , vol.414 , pp. 37-42
    • Morais-Cabral, J.H.1    Zhou, Y.2    MacKinnon, R.3
  • 58
    • 0031867789 scopus 로고    scopus 로고
    • Molecular basis for the lack of HERG K+ channel block-related eardiotoxicity by the H1 receptor blocker cetirizine compared with other second-generation antihistamines
    • Taglialatela M, Pannaccione A, Castaldo P, Giorgio G, Zhou Z, January CT, Genovese A, Marone G, Annunziato L. Molecular basis for the lack of HERG K+ channel block-related eardiotoxicity by the H1 receptor blocker cetirizine compared with other second-generation antihistamines. Mol Pharmacol 1998;54:113-121.
    • (1998) Mol Pharmacol , vol.54 , pp. 113-121
    • Taglialatela, M.1    Pannaccione, A.2    Castaldo, P.3    Giorgio, G.4    Zhou, Z.5    January, C.T.6    Genovese, A.7    Marone, G.8    Annunziato, L.9
  • 59
    • 0038497465 scopus 로고    scopus 로고
    • Blockade of HERG potassium currents by fluvoxamine: Incomplete attenuation by S6 mutations at F656 or Y652
    • Milnes JT, Crociani O, Arcangeli A, Hancox JC, Witchel HJ. Blockade of HERG potassium currents by fluvoxamine: incomplete attenuation by S6 mutations at F656 or Y652. Br J Pharmacol 2003;139:887-898.
    • (2003) Br J Pharmacol , vol.139 , pp. 887-898
    • Milnes, J.T.1    Crociani, O.2    Arcangeli, A.3    Hancox, J.C.4    Witchel, H.J.5
  • 60
    • 0033952902 scopus 로고    scopus 로고
    • Molecular determinant of high-affinity dofetilide binding to HERG1 expressed in Xenopus oocytes: Involvement of S6 sites
    • Lees-Miller JP, Duan Y, Teng GQ, Duff HJ. Molecular determinant of high-affinity dofetilide binding to HERG1 expressed in Xenopus oocytes: involvement of S6 sites. Mol Pharmacol 2000;57:367-374.
    • (2000) Mol Pharmacol , vol.57 , pp. 367-374
    • Lees-Miller, J.P.1    Duan, Y.2    Teng, G.Q.3    Duff, H.J.4
  • 61
    • 8444244427 scopus 로고    scopus 로고
    • High affinity HERG K(+) channel blockade by the antiarrhythmic agent dronedarone: Resistance to mutations of the S6 residues Y652 and F656
    • Ridley JM, Milnes JT, Witchel HJ, Hancox JC. High affinity HERG K(+) channel blockade by the antiarrhythmic agent dronedarone: resistance to mutations of the S6 residues Y652 and F656. Biochem Biophys Res Commun 2004;325:883-891.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 883-891
    • Ridley, J.M.1    Milnes, J.T.2    Witchel, H.J.3    Hancox, J.C.4
  • 63
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997;267:727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 64
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions. I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge MD, Murray CW, Auton TR, Paolini GV, Mee RP. Empirical scoring functions. I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J Comput Aided Mol Des 1997;11:425-445.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 66
    • 34250881826 scopus 로고    scopus 로고
    • DeLano WL.The PyMOL Molecular Graphics System. 2002; http://www.pymol. org.
    • (2002)
    • DeLano, W.L.1
  • 67
    • 0033681165 scopus 로고    scopus 로고
    • A conserved glutamate is important for slow inactivation in K+ channels
    • Larsson HP, Elinder F. A conserved glutamate is important for slow inactivation in K+ channels. Neuron 2000;27:573-583.
    • (2000) Neuron , vol.27 , pp. 573-583
    • Larsson, H.P.1    Elinder, F.2
  • 68
    • 0033872713 scopus 로고    scopus 로고
    • Collapse of conductance is prevented by a glutamate residue conserved in voltage-dependent K(+) channels
    • Ortega-Saenz P, Pardal R, Castellano A, Lopez-Barneo J. Collapse of conductance is prevented by a glutamate residue conserved in voltage-dependent K(+) channels. J Gen Physiol 2000; 116:181-190.
    • (2000) J Gen Physiol , vol.116 , pp. 181-190
    • Ortega-Saenz, P.1    Pardal, R.2    Castellano, A.3    Lopez-Barneo, J.4
  • 69
    • 0033756431 scopus 로고    scopus 로고
    • Molecular coupling of S4 to a K+ channel's slow inactivation gate
    • Loots E, Isacoff EY. Molecular coupling of S4 to a K+ channel's slow inactivation gate. J Gen Physiol 2000;116:623-635.
    • (2000) J Gen Physiol , vol.116 , pp. 623-635
    • Loots, E.1    Isacoff, E.Y.2
  • 70
    • 25844437886 scopus 로고    scopus 로고
    • Molecular mapping of a site for Cd2+-induced modification of human ether-a-go-go-related gene (hERG) channel activation
    • Fernandez D, Ghanta A, Kinard KI, Sanguinetti MC. Molecular mapping of a site for Cd2+-induced modification of human ether-a-go-go-related gene (hERG) channel activation. J Physiol (London) 2005;567:737-755.
    • (2005) J Physiol (London) , vol.567 , pp. 737-755
    • Fernandez, D.1    Ghanta, A.2    Kinard, K.I.3    Sanguinetti, M.C.4
  • 71
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau WM, Wimley WC, Gawrisch K, White SH. The preference of tryptophan for membrane interfaces. Biochemistry 1998;37: 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 72
    • 0038298482 scopus 로고    scopus 로고
    • Drug binding to HERG channels: Evidence for a 'non-aromatic' binding site for fluvoxamine
    • Mitcheson JS. Drug binding to HERG channels: evidence for a 'non-aromatic' binding site for fluvoxamine. Br J Pharmacol 2003;139:883-884.
    • (2003) Br J Pharmacol , vol.139 , pp. 883-884
    • Mitcheson, J.S.1
  • 73
    • 0343485099 scopus 로고    scopus 로고
    • Loratadine blockade of K(+) channels in human heart: Comparison with terfenadine under physiological conditions
    • Crumb WJ, Jr. Loratadine blockade of K(+) channels in human heart: comparison with terfenadine under physiological conditions. J Pharmacol Exp Ther 2000;292:261-264.
    • (2000) J Pharmacol Exp Ther , vol.292 , pp. 261-264
    • Crumb Jr., W.J.1
  • 74
    • 0035197735 scopus 로고    scopus 로고
    • Gastrointestinal prokinetic drugs have different affinity for the human cardiac human ether-a-gogo K(+) channel
    • Potet F, Bouyssou T, Escande D, Baro I. Gastrointestinal prokinetic drugs have different affinity for the human cardiac human ether-a-gogo K(+) channel. J Pharmacol Exp Ther 2001;299: 1007-1012.
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 1007-1012
    • Potet, F.1    Bouyssou, T.2    Escande, D.3    Baro, I.4
  • 75
    • 0030740295 scopus 로고    scopus 로고
    • Drug interactions with the nonsedating antihistamines
    • Ament PW, Paterson A. Drug interactions with the nonsedating antihistamines. Am Fam Physician 1997;56:223-231.
    • (1997) Am Fam Physician , vol.56 , pp. 223-231
    • Ament, P.W.1    Paterson, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.