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Volumn 145, Issue 2, 2015, Pages 93-106

Gating pore currents are defects in common with two Nav1.5 mutations in patients with mixed arrhythmias and dilated cardiomyopathy

Author keywords

[No Author keywords available]

Indexed keywords

SODIUM CHANNEL NAV1.5;

EID: 84921710685     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201411304     Document Type: Article
Times cited : (61)

References (72)
  • 1
    • 84871826522 scopus 로고    scopus 로고
    • Exploring conformational states of the bacterial voltage-gated sodium channel NavAb via molecular dynamics simulations
    • Amaral, C., V. Carnevale, M.L. Klein, and W. Treptow. 2012. Exploring conformational states of the bacterial voltage-gated sodium channel NavAb via molecular dynamics simulations. Proc. Natl. Acad. Sci. USA. 109:21336-21341. http://dx.doi.org/10.1073/pnas.1218087109
    • (2012) Proc. Natl. Acad. Sci. USA. , vol.109 , pp. 21336-21341
    • Amaral, C.1    Carnevale, V.2    Klein, M.L.3    Treptow, W.4
  • 2
    • 77955582765 scopus 로고    scopus 로고
    • Cardiac sodium channelopathies
    • Amin, A.S., A. Asghari-Roodsari, and H.L. Tan. 2010. Cardiac sodium channelopathies. Pflugers Arch. 460:223-237. http://dx.doi .org/10.1007/s00424-009-0761-0
    • (2010) Pflugers Arch. , vol.460 , pp. 223-237
    • Amin, A.S.1    Asghari-Roodsari, A.2    Tan, H.L.3
  • 3
    • 84155191394 scopus 로고    scopus 로고
    • The pore of the voltage-gated proton channel
    • Berger, T.K., and E.Y. Isacoff. 2011. The pore of the voltage-gated proton channel. Neuron. 72:991-1000. http://dx.doi.org/10.1016/ j.neuron.2011.11.014
    • (2011) Neuron. , vol.72 , pp. 991-1000
    • Berger, T.K.1    Isacoff, E.Y.2
  • 4
    • 55249088669 scopus 로고    scopus 로고
    • Dilated cardiomyopathy due to sodium channel dysfunction: What is the connection?
    • Bezzina, C.R., and C.A. Remme. 2008. Dilated cardiomyopathy due to sodium channel dysfunction: What is the connection? Circ Arrhythm Electrophysiol. 1:80-82. http://dx.doi.org/10.1161/ CIRCEP.108.791434
    • (2008) Circ Arrhythm Electrophysiol. , vol.1 , pp. 80-82
    • Bezzina, C.R.1    Remme, C.A.2
  • 5
    • 0037423552 scopus 로고    scopus 로고
    • Compound heterozygosity for mutations (W156X and R225W) in SCN5A associated with severe cardiac conduction disturbances and degenerative changes in the conduction system
    • Bezzina, C.R., M.B. Rook, W.A. Groenewegen, L.J. Herfst, A.C. van der Wal, J. Lam, H.J. Jongsma, A.A. Wilde, and M.M. Mannens. 2003. Compound heterozygosity for mutations (W156X and R225W) in SCN5A associated with severe cardiac conduction disturbances and degenerative changes in the conduction system. Circ. Res. 92:159- 168. http://dx.doi.org/10.1161/01.RES.0000052672.97759.36
    • (2003) Circ. Res. , vol.92 , pp. 159- 168
    • Bezzina, C.R.1    Rook, M.B.2    Groenewegen, W.A.3    Herfst, L.J.4    van der Wal, A.C.5    Lam, J.6    Jongsma, H.J.7    Wilde, A.A.8    Mannens, M.M.9
  • 6
    • 34548038151 scopus 로고    scopus 로고
    • Accessibility of four arginine residues on the S4 segment of the Bacillus halodurans sodium channel
    • Blanchet, J., and M. Chahine. 2007. Accessibility of four arginine residues on the S4 segment of the Bacillus halodurans sodium channel. J. Membr. Biol. 215:169-180. http://dx.doi.org/10.1007/ s00232-007-9016-1
    • (2007) J. Membr. Biol. , vol.215 , pp. 169-180
    • Blanchet, J.1    Chahine, M.2
  • 7
    • 0034957206 scopus 로고    scopus 로고
    • Gating properties of gap junction channels assembled from connexin43 and connexin43 fused with green fluorescent protein
    • Bukauskas, F.F., A. Bukauskiene, M.V. Bennett, and V.K. Verselis. 2001. Gating properties of gap junction channels assembled from connexin43 and connexin43 fused with green fluorescent protein. Biophys. J. 81:137-152. http://dx.doi.org/10.1016/S0006- 3495(01)75687-1
    • (2001) Biophys. J. , vol.81 , pp. 137-152
    • Bukauskas, F.F.1    Bukauskiene, A.2    Bennett, M.V.3    Verselis, V.K.4
  • 8
    • 0032963770 scopus 로고    scopus 로고
    • Voltage sensors in domains III and IV, but not I and II, are immobilized by Na+ channel fast inactivation
    • Cha, A., P.C. Ruben, A.L. George Jr., E. Fujimoto, and F. Bezanilla. 1999. Voltage sensors in domains III and IV, but not I and II, are immobilized by Na+ channel fast inactivation. Neuron. 22:73-87. http://dx.doi.org/10.1016/S0896-6273(00)80680-7
    • (1999) Neuron. , vol.22 , pp. 73-87
    • Cha, A.1    Ruben, P.C.2    George Jr., A.L.3    Fujimoto, E.4    Bezanilla, F.5
  • 9
    • 11244356723 scopus 로고    scopus 로고
    • Role of arginine residues on the S4 segment of the Bacillus halodurans Na+ channel in voltage-sensing
    • Chahine, M., S. Pilote, V. Pouliot, H. Takami, and C. Sato. 2004. Role of arginine residues on the S4 segment of the Bacillus halodurans Na+ channel in voltage-sensing. J. Membr. Biol. 201:9-24. http://dx.doi.org/10.1007/s00232-004-0701-z
    • (2004) J. Membr. Biol. , vol.201 , pp. 9-24
    • Chahine, M.1    Pilote, S.2    Pouliot, V.3    Takami, H.4    Sato, C.5
  • 10
    • 78650248936 scopus 로고    scopus 로고
    • SCN5A rare variants in familial dilated cardiomyopathy decrease peak sodium current depending on the common polymorphism H558R and common splice variant Q1077del
    • Cheng, J., A. Morales, J.D. Siegfried, D. Li, N. Norton, J. Song, J. Gonzalez-Quintana, J.C. Makielski, and R.E. Hershberger. 2010. SCN5A rare variants in familial dilated cardiomyopathy decrease peak sodium current depending on the common polymorphism H558R and common splice variant Q1077del. Clin. Transl. Sci. 3:287-294. http://dx.doi.org/10.1111/j.1752- 8062.2010.00249.x
    • (2010) Clin. Transl. Sci. , vol.3 , pp. 287-294
    • Cheng, J.1    Morales, A.2    Siegfried, J.D.3    Li, D.4    Norton, N.5    Song, J.6    Gonzalez-Quintana, J.7    Makielski, J.C.8    Hershberger, R.E.9
  • 11
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An Nlog(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle Mesh Ewald: An Nlog(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092. http://dx.doi.org/10.1063/1.464397
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 12
    • 78349287755 scopus 로고    scopus 로고
    • Effect of sensor domain mutations on the properties of voltage-gated ion channels: Molecular dynamics studies of the potassium channel Kv1.2
    • Delemotte, L., W. Treptow, M.L. Klein, and M. Tarek. 2010. Effect of sensor domain mutations on the properties of voltage-gated ion channels: Molecular dynamics studies of the potassium channel Kv1.2. Biophys. J. 99:L72-L74. http://dx.doi.org/10.1016/j. bpj.2010.08.069
    • (2010) Biophys. J. , vol.99 , pp. L72-L74
    • Delemotte, L.1    Treptow, W.2    Klein, M.L.3    Tarek, M.4
  • 13
    • 79954991393 scopus 로고    scopus 로고
    • Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations
    • Delemotte, L., M. Tarek, M.L. Klein, C. Amaral, and W. Treptow. 2011. Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations. Proc. Natl. Acad. Sci. USA. 108:6109-6114. http://dx.doi.org/10.1073/pnas.1102724108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 6109-6114
    • Delemotte, L.1    Tarek, M.2    Klein, M.L.3    Amaral, C.4    Treptow, W.5
  • 14
    • 0343819791 scopus 로고    scopus 로고
    • Electrophysiological characterization of SCN5A mutations causing long QT (E1784K) and Brugada (R1512W and R1432G) syndromes
    • Deschênes, I., G. Baroudi, M. Berthet, I. Barde, T. Chalvidan, I. Denjoy, P. Guicheney, and M. Chahine. 2000. Electrophysiological characterization of SCN5A mutations causing long QT (E1784K) and Brugada (R1512W and R1432G) syndromes. Cardiovasc. Res. 46:55-65. http://dx.doi.org/10.1016/S0008-6363(00)00006-7
    • (2000) Cardiovasc. Res. , vol.46 , pp. 55-65
    • Deschênes, I.1    Baroudi, G.2    Berthet, M.3    Barde, I.4    Chalvidan, T.5    Denjoy, I.6    Guicheney, P.7    Chahine, M.8
  • 16
    • 84890604639 scopus 로고    scopus 로고
    • Transient compartment-like syndrome and normokalaemic periodic paralysis due to a Ca(v)1.1 mutation
    • Fan, C., F. Lehmann-Horn, M.A. Weber, M. Bednarz, J.R. Groome, M.K. Jonsson, and K. Jurkat-Rott. 2013. Transient compartment-like syndrome and normokalaemic periodic paralysis due to a Ca(v)1.1 mutation. Brain. 136:3775-3786. http://dx.doi.org/10.1093/brain/ awt300
    • (2013) Brain. , vol.136 , pp. 3775-3786
    • Fan, C.1    Lehmann-Horn, F.2    Weber, M.A.3    Bednarz, M.4    Groome, J.R.5    Jonsson, M.K.6    Jurkat-Rott, K.7
  • 17
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S.E., and A.D. MacKerrell Jr. 2000. An improved empirical potential energy function for molecular simulations of phospholipids. J. Phys. Chem. B. 104:7510-7515. http://dx.doi.org/ 10.1021/jp0007843
    • (2000) J. Phys. Chem. B. , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerrell Jr., A.D.2
  • 18
    • 77953560367 scopus 로고    scopus 로고
    • Double gaps along Shaker S4 demonstrate omega currents at three different closed states
    • Gamal El-Din, T.M., H. Heldstab, C. Lehmann, and N.G. Greeff. 2010. Double gaps along Shaker S4 demonstrate omega currents at three different closed states. Channels (Austin). 4:93-100. http://dx.doi.org/10.4161/chan.4.2.10672
    • (2010) Channels (Austin). , vol.4 , pp. 93-100
    • Gamal El-Din, T.M.1    Heldstab, H.2    Lehmann, C.3    Greeff, N.G.4
  • 19
    • 84883254270 scopus 로고    scopus 로고
    • A gating charge interaction required for late slow inactivation of the bacterial sodium channel NavAb
    • Gamal El-Din, T.M., G.Q. Martinez, J. Payandeh, T. Scheuer, and W.A. Catterall. 2013. A gating charge interaction required for late slow inactivation of the bacterial sodium channel NavAb. J. Gen. Physiol. 142:181-190. http://dx.doi.org/10.1085/jgp.201311012
    • (2013) J. Gen. Physiol. , vol.142 , pp. 181-190
    • Gamal El-Din, T.M.1    Martinez, G.Q.2    Payandeh, J.3    Scheuer, T.4    Catterall, W.A.5
  • 20
    • 84905397615 scopus 로고    scopus 로고
    • Tracking S4 movement by gating pore currents in the bacterial sodium channel NaChBac
    • Gamal El-Din, T.M., T. Scheuer, and W.A. Catterall. 2014. Tracking S4 movement by gating pore currents in the bacterial sodium channel NaChBac. J. Gen. Physiol. 144:147-157. http://dx.doi.org/ 10.1085/jgp.201411210
    • (2014) J. Gen. Physiol. , vol.144 , pp. 147-157
    • Gamal El-Din, T.M.1    Scheuer, T.2    Catterall, W.A.3
  • 21
    • 0026530472 scopus 로고
    • Primary structure and functional expression of the human cardiac tetrodotoxin-insensitive voltage-dependent sodium channel
    • Gellens, M.E., A.L. George Jr., L.Q. Chen, M. Chahine, R. Horn, R.L. Barchi, and R.G. Kallen. 1992. Primary structure and functional expression of the human cardiac tetrodotoxin-insensitive voltage-dependent sodium channel. Proc. Natl. Acad. Sci. USA. 89:554-558. http://dx.doi.org/10.1073/pnas.89.2.554
    • (1992) Proc. Natl. Acad. Sci. USA. , vol.89 , pp. 554-558
    • Gellens, M.E.1    George Jr., A.L.2    Chen, L.Q.3    Chahine, M.4    Horn, R.5    Barchi, R.L.6    Kallen, R.G.7
  • 23
    • 84861664954 scopus 로고    scopus 로고
    • A proton leak current through the cardiac sodium channel is linked to mixed arrhythmia and the dilated cardiomyopathy phenotype.
    • Gosselin-Badaroudine, P., D.I. Keller, H. Huang, V. Pouliot, A. Chatelier, S. Osswald, M. Brink, and M. Chahine. 2012b. A proton leak current through the cardiac sodium channel is linked to mixed arrhythmia and the dilated cardiomyopathy phenotype. PLoS ONE. 7:e38331. http://dx.doi.org/10.1371/journal.pone .0038331
    • (2012) PLoS ONE. , vol.7
    • Gosselin-Badaroudine, P.1    Keller, D.I.2    Huang, H.3    Pouliot, V.4    Chatelier, A.5    Osswald, S.6    Brink, M.7    Chahine, M.8
  • 24
    • 84901487880 scopus 로고    scopus 로고
    • Nav1.5 mutations linked to dilated cardiomyopathy phenotypes: Is the gating pore current the missing link?
    • Gosselin-Badaroudine, P., A. Moreau, and M. Chahine. 2014. Nav1.5 mutations linked to dilated cardiomyopathy phenotypes: Is the gating pore current the missing link? Channels (Austin). 8:90-94. http://dx.doi.org/10.4161/chan.27179
    • (2014) Channels (Austin). , vol.8 , pp. 90-94
    • Gosselin-Badaroudine, P.1    Moreau, A.2    Chahine, M.3
  • 25
    • 84897901479 scopus 로고    scopus 로고
    • NaV1.4 mutations cause hypokalaemic periodic paralysis by disrupting IIIS4 movement during recovery
    • Groome, J.R., F. Lehmann-Horn, C. Fan, M. Wolf, V. Winston, L. Merlini, and K. Jurkat-Rott. 2014. NaV1.4 mutations cause hypokalaemic periodic paralysis by disrupting IIIS4 movement during recovery. Brain. 137:998-1008. http://dx.doi.org/10.1093/ brain/awu015
    • (2014) Brain. , vol.137 , pp. 998-1008
    • Groome, J.R.1    Lehmann-Horn, F.2    Fan, C.3    Wolf, M.4    Winston, V.5    Merlini, L.6    Jurkat-Rott, K.7
  • 28
    • 0000921742 scopus 로고    scopus 로고
    • Longer time steps for molecular dynamics
    • Izaguirre, J.A., S. Reich, and R.D. Skeel. 1999. Longer time steps for molecular dynamics. J. Chem. Phys. 110:9853-9864. http://dx.doi .org/10.1063/1.478995
    • (1999) J. Chem. Phys. , vol.110 , pp. 9853-9864
    • Izaguirre, J.A.1    Reich, S.2    Skeel, R.D.3
  • 30
    • 34547628129 scopus 로고    scopus 로고
    • Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment
    • Jogini, V., and B. Roux. 2007. Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Biophys. J. 93:3070- 3082. http://dx.doi.org/10.1529/biophysj.107.112540
    • (2007) Biophys. J. , vol.93 , pp. 3070- 3082
    • Jogini, V.1    Roux, B.2
  • 31
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W.L., J. Chandrasekhar, J.D. Madura, R.W. Impey, and M.L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935. http://dx.doi .org/10.1063/1.445869
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 33
    • 84855997898 scopus 로고    scopus 로고
    • Molecular dynamics investigation of the ω-current in the Kv1.2 voltage sensor domains
    • Khalili-Araghi, F., E. Tajkhorshid, B. Roux, and K. Schulten. 2012. Molecular dynamics investigation of the ω-current in the Kv1.2 voltage sensor domains. Biophys. J. 102:258-267. http://dx.doi.org/ 10.1016/j.bpj.2011.10.057
    • (2012) Biophys. J. , vol.102 , pp. 258-267
    • Khalili-Araghi, F.1    Tajkhorshid, E.2    Roux, B.3    Schulten, K.4
  • 36
    • 84900508031 scopus 로고    scopus 로고
    • Moving gating charges through the gating pore in a Kv channel voltage sensor
    • Lacroix, J.J., H.C. Hyde, F.V. Campos, and F. Bezanilla. 2014. Moving gating charges through the gating pore in a Kv channel voltage sensor. Proc. Natl. Acad. Sci. USA. 111:E1950-E1959. http://dx.doi .org/10.1073/pnas.1406161111
    • (2014) Proc. Natl. Acad. Sci. USA. , vol.111 , pp. E1950-E1959
    • Lacroix, J.J.1    Hyde, H.C.2    Campos, F.V.3    Bezanilla, F.4
  • 39
    • 84893723768 scopus 로고    scopus 로고
    • Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain
    • Li, Q., S. Wanderling, P. Sompornpisut, and E. Perozo. 2014. Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain. Nat. Struct. Mol. Biol. 21:160-166. http://dx.doi.org/10.1038/nsmb.2747
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 160-166
    • Li, Q.1    Wanderling, S.2    Sompornpisut, P.3    Perozo, E.4
  • 40
    • 79961124704 scopus 로고    scopus 로고
    • R1 in the Shaker S4 occupies the gating charge transfer center in the resting state
    • Lin, M.C., J.Y. Hsieh, A.F. Mock, and D.M. Papazian. 2011. R1 in the Shaker S4 occupies the gating charge transfer center in the resting state. J. Gen. Physiol. 138:155-163. http://dx.doi.org/10.1085/ jgp.201110642
    • (2011) J. Gen. Physiol. , vol.138 , pp. 155-163
    • Lin, M.C.1    Hsieh, J.Y.2    Mock, A.F.3    Papazian, D.M.4
  • 41
    • 84861880853 scopus 로고    scopus 로고
    • Disease-related cardiac troponins alter thin filament Ca2+ association and dissociation rates
    • Liu, B., S.B. Tikunova, K.P. Kline, J.K. Siddiqui, and J.P. Davis. 2012. Disease-related cardiac troponins alter thin filament Ca2+ association and dissociation rates. PLoS ONE. 7:e38259. http://dx.doi .org/10.1371/journal.pone.0038259
    • (2012) PLoS ONE. , vol.7
    • Liu, B.1    Tikunova, S.B.2    Kline, K.P.3    Siddiqui, J.K.4    Davis, J.P.5
  • 43
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell, A.D., Jr., M. Feig, and C.L. Brooks III. 2004. Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25:1400-1415. http://dx.doi.org/10.1002/jcc.20065
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • MacKerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 46
    • 79956116043 scopus 로고    scopus 로고
    • SCN5A mutations associate with arrhythmic dilated cardiomyopathy and commonly localize to the voltage-sensing mechanism
    • McNair, W.P., G. Sinagra, M.R. Taylor, A. Di Lenarda, D.A. Ferguson, E.E. Salcedo, D. Slavov, X. Zhu, J.H. Caldwell, and L. Mestroni, and Familial Cardiomyopathy Registry Research Group. 2011. SCN5A mutations associate with arrhythmic dilated cardiomyopathy and commonly localize to the voltage-sensing mechanism. J. Am. Coll. Cardiol. 57:2160-2168. http://dx.doi.org/10.1016/ j.jacc.2010.09.084
    • (2011) J. Am. Coll. Cardiol. , vol.57 , pp. 2160-2168
    • McNair, W.P.1    Sinagra, G.2    Taylor, M.R.3    Di Lenarda, A.4    Ferguson, D.A.5    Salcedo, E.E.6    Slavov, D.7    Zhu, X.8    Caldwell, J.H.9    Mestroni, L.10
  • 47
    • 51649104990 scopus 로고    scopus 로고
    • Gating consequences of charge neutralization of arginine residues in the S4 segment of K(v)7.2, an epilepsy-linked K+ channel subunit
    • Miceli, F., M.V. Soldovieri, C.C. Hernandez, M.S. Shapiro, L. Annunziato, and M. Taglialatela. 2008. Gating consequences of charge neutralization of arginine residues in the S4 segment of K(v)7.2, an epilepsy-linked K+ channel subunit. Biophys. J. 95:2254-2264. http://dx.doi.org/10.1529/biophysj.107.128371
    • (2008) Biophys. J. , vol.95 , pp. 2254-2264
    • Miceli, F.1    Soldovieri, M.V.2    Hernandez, C.C.3    Shapiro, M.S.4    Annunziato, L.5    Taglialatela, M.6
  • 48
    • 84858769963 scopus 로고    scopus 로고
    • Gating currents from Kv7 channels carrying neuronal hyperexcitability mutations in the voltage-sensing domain
    • Miceli, F., E. Vargas, F. Bezanilla, and M. Taglialatela. 2012. Gating currents from Kv7 channels carrying neuronal hyperexcitability mutations in the voltage-sensing domain. Biophys. J. 102:1372- 1382. http://dx.doi.org/10.1016/j.bpj.2012.02.004
    • (2012) Biophys. J. , vol.102 , pp. 1372- 1382
    • Miceli, F.1    Vargas, E.2    Bezanilla, F.3    Taglialatela, M.4
  • 49
    • 84901059842 scopus 로고    scopus 로고
    • Biophysics, pathophysiology, and pharmacology of ion channel gating pores.
    • Moreau, A., P. Gosselin-Badaroudine, and M. Chahine. 2014a. Biophysics, pathophysiology, and pharmacology of ion channel gating pores. Front Pharmacol. 5:53. http://dx.doi.org/10.3389/ fphar.2014.00053
    • (2014) Front Pharmacol. , vol.5 , pp. 53
    • Moreau, A.1    Gosselin-Badaroudine, P.2    Chahine, M.3
  • 50
    • 84910137181 scopus 로고    scopus 로고
    • Molecular biology and biophysical properties of ion channel gating pores.
    • Moreau, A., P. Gosselin-Badaroudine, and M. Chahine. 2014b. Molecular biology and biophysical properties of ion channel gating pores. Q. Rev. Biophys. 47:364-388. http://dx.doi.org/10 .1017/S0033583514000109
    • (2014) Q. Rev. Biophys. , vol.47 , pp. 364-388
    • Moreau, A.1    Gosselin-Badaroudine, P.2    Chahine, M.3
  • 51
    • 84866637503 scopus 로고    scopus 로고
    • Escape capture bigeminy: Phenotypic marker of cardiac sodium channel voltage sensor mutation R222Q
    • Nair, K., R. Pekhletski, L. Harris, M. Care, C. Morel, T. Farid, P.H. Backx, E. Szabo, and K. Nanthakumar. 2012. Escape capture bigeminy: Phenotypic marker of cardiac sodium channel voltage sensor mutation R222Q. Heart Rhythm. 9:1681-1688. http:// dx.doi.org/10.1016/j.hrthm.2012.06.029
    • (2012) Heart Rhythm. , vol.9 , pp. 1681-1688
    • Nair, K.1    Pekhletski, R.2    Harris, L.3    Care, M.4    Morel, C.5    Farid, T.6    Backx, P.H.7    Szabo, E.8    Nanthakumar, K.9
  • 52
    • 79951782054 scopus 로고    scopus 로고
    • An atypical phenotype of hypokalemic periodic paralysis caused by a mutation in the sodium channel gene SCN4A
    • Park, Y.H., and J.B. Kim. 2010. An atypical phenotype of hypokalemic periodic paralysis caused by a mutation in the sodium channel gene SCN4A. Korean J Pediatr. 53:909-912. http://dx.doi .org/10.3345/kjp.2010.53.10.909
    • (2010) Korean J Pediatr. , vol.53 , pp. 909-912
    • Park, Y.H.1    Kim, J.B.2
  • 53
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., T. Scheuer, N. Zheng, and W.A. Catterall. 2011. The crystal structure of a voltage-gated sodium channel. Nature. 475:353-358. http://dx.doi.org/10.1038/nature10238
    • (2011) Nature. , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 56
    • 84890903987 scopus 로고    scopus 로고
    • Targeting sodium channels in cardiac arrhythmia
    • Remme, C.A., and A.A. Wilde. 2014. Targeting sodium channels in cardiac arrhythmia. Curr. Opin. Pharmacol. 15:53-60. http:// dx.doi.org/10.1016/j.coph.2013.11.014
    • (2014) Curr. Opin. Pharmacol. , vol.15 , pp. 53-60
    • Remme, C.A.1    Wilde, A.A.2
  • 57
    • 67649547603 scopus 로고    scopus 로고
    • Sodium channel mutations and arrhythmias
    • Ruan, Y., N. Liu, and S.G. Priori. 2009. Sodium channel mutations and arrhythmias. Nat. Rev. Cardiol. 6:337-348. http://dx.doi.org/ 10.1038/nrcardio.2009.44
    • (2009) Nat. Rev. Cardiol. , vol.6 , pp. 337-348
    • Ruan, Y.1    Liu, N.2    Priori, S.G.3
  • 58
    • 84867669798 scopus 로고    scopus 로고
    • The free energy barrier for arginine gating charge translation is altered by mutations in the voltage sensor domain
    • Schwaiger, C.S., S.I. Börjesson, B. Hess, B. Wallner, F. Elinder, and E. Lindahl. 2012. The free energy barrier for arginine gating charge translation is altered by mutations in the voltage sensor domain. PLoS ONE. 7:e45880. http://dx.doi.org/10.1371/journal .pone.0045880
    • (2012) PLoS ONE. , vol.7
    • Schwaiger, C.S.1    Börjesson, S.I.2    Hess, B.3    Wallner, B.4    Elinder, F.5    Lindahl, E.6
  • 59
    • 33847344389 scopus 로고    scopus 로고
    • Gating pore current in an inherited ion channelopathy
    • Sokolov, S., T. Scheuer, and W.A. Catterall. 2007. Gating pore current in an inherited ion channelopathy. Nature. 446:76-78. http://dx.doi.org/10.1038/nature05598
    • (2007) Nature. , vol.446 , pp. 76-78
    • Sokolov, S.1    Scheuer, T.2    Catterall, W.A.3
  • 60
    • 58149395036 scopus 로고    scopus 로고
    • Depolarizationactivated gating pore current conducted by mutant sodium channels in potassium-sensitive normokalemic periodic paralysis
    • Sokolov, S., T. Scheuer, and W.A. Catterall. 2008. Depolarizationactivated gating pore current conducted by mutant sodium channels in potassium-sensitive normokalemic periodic paralysis. Proc. Natl. Acad. Sci. USA. 105:19980-19985. http://dx.doi.org/10 .1073/pnas.0810562105
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 19980-19985
    • Sokolov, S.1    Scheuer, T.2    Catterall, W.A.3
  • 61
    • 34347211819 scopus 로고    scopus 로고
    • A Na+ channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore
    • Struyk, A.F., and S.C. Cannon. 2007. A Na+ channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore. J. Gen. Physiol. 130:11-20. http://dx.doi.org/10.1085/ jgp.200709755
    • (2007) J. Gen. Physiol. , vol.130 , pp. 11-20
    • Struyk, A.F.1    Cannon, S.C.2
  • 62
    • 77950488909 scopus 로고    scopus 로고
    • A gating charge transfer center in voltage sensors
    • Tao, X., A. Lee, W. Limapichat, D.A. Dougherty, and R. MacKinnon. 2010. A gating charge transfer center in voltage sensors. Science. 328:67-73. http://dx.doi.org/10.1126/science.1185954
    • (2010) Science. , vol.328 , pp. 67-73
    • Tao, X.1    Lee, A.2    Limapichat, W.3    Dougherty, D.A.4    MacKinnon, R.5
  • 63
    • 13244272072 scopus 로고    scopus 로고
    • Voltage-sensing arginines in a potassium channel permeate and occlude cationselective pores
    • Tombola, F., M.M. Pathak, and E.Y. Isacoff. 2005. Voltage-sensing arginines in a potassium channel permeate and occlude cationselective pores. Neuron. 45:379-388. http://dx.doi.org/10.1016/ j.neuron.2004.12.047
    • (2005) Neuron. , vol.45 , pp. 379-388
    • Tombola, F.1    Pathak, M.M.2    Isacoff, E.Y.3
  • 64
    • 33751192493 scopus 로고    scopus 로고
    • How does voltage open an ion channel?
    • Tombola, F., M.M. Pathak, and E.Y. Isacoff. 2006. How does voltage open an ion channel? Annu. Rev. Cell Dev. Biol. 22:23-52. http:// dx.doi.org/10.1146/annurev.cellbio.21.020404.145837
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 23-52
    • Tombola, F.1    Pathak, M.M.2    Isacoff, E.Y.3
  • 65
    • 33846688821 scopus 로고    scopus 로고
    • The twisted ion-permeation pathway of a resting voltage-sensing domain
    • Tombola, F., M.M. Pathak, P. Gorostiza, and E.Y. Isacoff. 2007. The twisted ion-permeation pathway of a resting voltage-sensing domain. Nature. 445:546-549. http://dx.doi.org/10.1038/ nature05396
    • (2007) Nature. , vol.445 , pp. 546-549
    • Tombola, F.1    Pathak, M.M.2    Gorostiza, P.3    Isacoff, E.Y.4
  • 66
    • 33646135082 scopus 로고    scopus 로고
    • Environment of the gating charges in the Kv1.2 Shaker potassium channel
    • Treptow, W., and M. Tarek. 2006. Environment of the gating charges in the Kv1.2 Shaker potassium channel. Biophys. J. 90:L64-L66. http://dx.doi.org/10.1529/biophysj.106.080754
    • (2006) Biophys. J. , vol.90 , pp. L64-L66
    • Treptow, W.1    Tarek, M.2
  • 67
    • 84857628246 scopus 로고    scopus 로고
    • Recent advances in the pathogenesis and drug action in periodic paralyses and related channelopathies
    • Tricarico, D., and D.C. Camerino. 2011. Recent advances in the pathogenesis and drug action in periodic paralyses and related channelopathies. Front Pharmacol. 2:8. http://dx.doi.org/10.3389/ fphar.2011.00008
    • (2011) Front Pharmacol. , vol.2 , pp. 8
    • Tricarico, D.1    Camerino, D.C.2
  • 70
    • 80053417931 scopus 로고    scopus 로고
    • A sodium channel knockin mutant (NaV1.4- R669H) mouse model of hypokalemic periodic paralysis
    • Wu, F., W. Mi, D.K. Burns, Y. Fu, H.F. Gray, A.F. Struyk, and S.C. Cannon. 2011. A sodium channel knockin mutant (NaV1.4- R669H) mouse model of hypokalemic periodic paralysis. J. Clin. Invest. 121:4082-4094. http://dx.doi.org/10.1172/JCI57398
    • (2011) J. Clin. Invest. , vol.121 , pp. 4082-4094
    • Wu, F.1    Mi, W.2    Burns, D.K.3    Fu, Y.4    Gray, H.F.5    Struyk, A.F.6    Cannon, S.C.7


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