메뉴 건너뛰기




Volumn 50, Issue 32, 2011, Pages 6742-6752

NaChBac: The long lost sodium channel ancestor

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS HALODURANS; CHANNELOPATHIES; ESSENTIAL ELEMENTS; EXCITABLE CELLS; FUNCTIONAL CHARACTERIZATION; FUNCTIONAL DEMANDS; GLYCOSYLATED; HETEROLOGOUS EXPRESSION; MAMMALIAN SYSTEMS; MEMBRANE PROTEINS; MUSCULAR CONTRACTION; NEURONAL SIGNALING; SODIUM CHANNEL; STRUCTURAL ORGANIZATION; STRUCTURE-FUNCTION STUDIES; VOLTAGE GATED ION CHANNELS;

EID: 80051495437     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200942y     Document Type: Review
Times cited : (56)

References (81)
  • 2
    • 0031896768 scopus 로고    scopus 로고
    • Structure and function of voltage-gated sodium channels
    • DOI 10.1111/j.1469-7793.1998.647bp.x
    • Marban, E., Yamagishi, T., and Tomaselli, G. F. (1998) Structure and function of voltage-gated sodium channels J. Physiol. 508, 647-657 (Pubitemid 28220721)
    • (1998) Journal of Physiology , vol.508 , Issue.3 , pp. 647-657
    • Marban, E.1    Yamagishi, T.2    Tomaselli, G.F.3
  • 3
    • 0033694833 scopus 로고    scopus 로고
    • From ionic currents to molecular mechanisms: The structure and function of voltage-gated sodium channels
    • Catterall, W. A. (2000) From ionic currents to molecular mechanisms: The structure and function of voltage-gated sodium channels Neuron 26, 13-25
    • (2000) Neuron , vol.26 , pp. 13-25
    • Catterall, W.A.1
  • 4
    • 0037022783 scopus 로고    scopus 로고
    • Structure and function of voltage-dependent ion channel regulatory β subunits
    • DOI 10.1021/bi0119565
    • Hanlon, M. R. and Wallace, B. A. (2002) Structure and function of voltage-dependent ion channel regulatory β subunits Biochemistry 41, 2886-2894 (Pubitemid 34184619)
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 2886-2894
    • Hanlon, M.R.1    Wallace, B.A.2
  • 5
    • 0035931906 scopus 로고    scopus 로고
    • The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities
    • DOI 10.1038/35059098
    • Sato, C., Ueno, Y., Asai, K., Takahashi, K., Sato, M., Engel, A., and Fujiyoshi, Y. (2001) The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities Nature 409, 1047-1051 (Pubitemid 32204057)
    • (2001) Nature , vol.409 , Issue.6823 , pp. 1047-1051
    • Sato, C.1    Ueno, Y.2    Asai, K.3    Takahashi, K.4    Sato, M.5    Engel, A.6    Fujiyoshi, Y.7
  • 6
    • 1342282941 scopus 로고    scopus 로고
    • The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: Comparison with the skeletal muscle form reveals a common architectural motif
    • DOI 10.1074/jbc.M308057200
    • Wang, M. C., Collins, R. F., Ford, R. C., Berrow, N. S., Dolphin, A. C., and Kitmitto, A. (2004) The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: Comparison with the skeletal muscle form reveals a common architectural motif J. Biol. Chem. 279, 7159-7168 (Pubitemid 38248863)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 7159-7168
    • Wang, M.-C.1    Collins, R.F.2    Ford, R.C.3    Berrow, N.S.4    Dolphin, A.C.5    Kitmitto, A.6
  • 9
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • DOI 10.1038/417515a
    • Jiang, Y. X., Lee, A., Chen, J. Y., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) Crystal structure and mechanism of a calcium-gated potassium channel Nature 417, 515-522 (Pubitemid 34595912)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 10
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • DOI 10.1038/417523a
    • Jiang, Y. X., Lee, A., Chen, J. Y., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) The open pore conformation of potassium channels Nature 417, 523-526 (Pubitemid 34595913)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 523-526
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 14
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • + channel in a lipid membrane-like environment Nature 450, 376-382 (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 16
    • 5644258235 scopus 로고    scopus 로고
    • + channel in a lipid bilayer
    • DOI 10.1126/science.1101373
    • + channel in a lipid bilayer Science 306, 491-495 (Pubitemid 39372450)
    • (2004) Science , vol.306 , Issue.5695 , pp. 491-495
    • Cuello, L.G.1    Cortes, D.M.2    Perozo, E.3
  • 17
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • DOI 10.1126/science.1116270
    • Long, S. B., Campbell, E. B., and Mackinnon, R. (2005) Voltage sensor of Kv1.2: Structural basis of electromechanical coupling Science 309, 903-908 (Pubitemid 41099920)
    • (2005) Science , vol.309 , Issue.5736 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 20
    • 56049083760 scopus 로고    scopus 로고
    • Models of voltage-dependent conformational changes in NaChBac channels
    • Shafrir, Y., Durell, S. R., and Guy, H. R. (2008) Models of voltage-dependent conformational changes in NaChBac channels Biophys. J. 95, 3663-3676
    • (2008) Biophys. J. , vol.95 , pp. 3663-3676
    • Shafrir, Y.1    Durell, S.R.2    Guy, H.R.3
  • 21
    • 34247880407 scopus 로고    scopus 로고
    • Acidic residues on the voltage-sensor domain determine the activation of the NaChBac sodium channel
    • DOI 10.1529/biophysj.106.090464
    • Blanchet, J., Pilote, S., and Chahine, M. (2007) Acidic residues on the voltage-sensor domain determine the activation of the NaChBac sodium channel Biophys. J. 92, 3513-3523 (Pubitemid 46698641)
    • (2007) Biophysical Journal , vol.92 , Issue.10 , pp. 3513-3523
    • Blanchet, J.1    Pilote, S.2    Chahine, M.3
  • 22
    • 1842422868 scopus 로고    scopus 로고
    • + channels: A molecular switch for electrical signaling
    • DOI 10.1016/S0896-6273(04)00116-3, PII S0896627304001163
    • + channels: A molecular switch for electrical signaling Neuron 41, 859-865 (Pubitemid 38429730)
    • (2004) Neuron , vol.41 , Issue.6 , pp. 859-865
    • Zhao, Y.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Catterall, W.A.4
  • 24
    • 0034682616 scopus 로고    scopus 로고
    • + channel pore
    • DOI 10.1021/bi000486w
    • Lipkind, G. M. and Fozzard, H. A. (2000) KcsA crystal structure as framework for a molecular model of the Na channel pore Biochemistry 39, 8161-8170 (Pubitemid 30460965)
    • (2000) Biochemistry , vol.39 , Issue.28 , pp. 8161-8170
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 25
    • 11244296111 scopus 로고    scopus 로고
    • Modeling P-loops domain of sodium channel: Homology with potassium channels and interaction with ligands
    • DOI 10.1529/biophysj.104.048173
    • Tikhonov, D. B. and Zhorov, B. S. (2005) Modeling P-loops domain of sodium channel: Homology with potassium channels and interaction with ligands Biophys. J. 88, 184-197 (Pubitemid 40070668)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 184-197
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 26
    • 0030663654 scopus 로고    scopus 로고
    • Prokaryotes offer hope for potassium channel structural studies
    • DOI 10.1038/nsb1197-877
    • MacKinnon, R. and Doyle, D. A. (1997) Prokaryotes offer hope for potassium channel structural studies Nat. Struct. Biol. 4, 877-879 (Pubitemid 27479434)
    • (1997) Nature Structural Biology , vol.4 , Issue.11 , pp. 877-879
    • MacKinnon, R.1    Doyle, D.A.2
  • 27
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • DOI 10.1126/science.1065635
    • Ren, D., Navarro, B., Xu, H., Yue, L., Shi, Q., and Clapham, D. E. (2001) A prokaryotic voltage-gated sodium channel Science 294, 2372-2375 (Pubitemid 33140564)
    • (2001) Science , vol.294 , Issue.5550 , pp. 2372-2375
    • Ren, D.1    Navarro, B.2    Xu, H.3    Yue, L.4    Shi, Q.5    Clapham, D.E.6
  • 28
    • 77950463390 scopus 로고    scopus 로고
    • Comparative study of the gating motif and C-type inactivation in prokaryotic voltage-gated sodium channels
    • Irie, K., Kitagawa, K., Nagura, H., Imai, T., Shimomura, T., and Fujiyoshi, Y. (2010) Comparative study of the gating motif and C-type inactivation in prokaryotic voltage-gated sodium channels J. Biol. Chem. 285, 3685-3694
    • (2010) J. Biol. Chem. , vol.285 , pp. 3685-3694
    • Irie, K.1    Kitagawa, K.2    Nagura, H.3    Imai, T.4    Shimomura, T.5    Fujiyoshi, Y.6
  • 31
    • 77956294944 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly
    • Powl, A. M., O'Reilly, A. O., Miles, A. J., and Wallace, B. A. (2010) Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly Proc. Natl. Acad. Sci. U.S.A. 107, 14064-14069
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14064-14069
    • Powl, A.M.1    O'Reilly, A.O.2    Miles, A.J.3    Wallace, B.A.4
  • 32
    • 79955549892 scopus 로고    scopus 로고
    • Simplified bacterial "pore" provides insight into the assembly, stability and structure of sodium channels
    • McCusker, E. C., D'Avanzo, N., Nichols, C. G., and Wallace, B. A. (2011) Simplified bacterial "pore" provides insight into the assembly, stability and structure of sodium channels J. Biol. Chem. 286, 16386-16391
    • (2011) J. Biol. Chem. , vol.286 , pp. 16386-16391
    • McCusker, E.C.1    D'Avanzo, N.2    Nichols, C.G.3    Wallace, B.A.4
  • 33
    • 65549103287 scopus 로고    scopus 로고
    • Thermal and chemical unfolding and refolding of a eukaryotic sodium channel
    • Charalambous, K., O'Reilly, A. O., Bullough, P. A., and Wallace, B. A. (2009) Thermal and chemical unfolding and refolding of a eukaryotic sodium channel Biochim. Biophys. Acta 1788, 1279-1286
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1279-1286
    • Charalambous, K.1    O'Reilly, A.O.2    Bullough, P.A.3    Wallace, B.A.4
  • 35
    • 57049128880 scopus 로고    scopus 로고
    • G219S mutagenesis as a means of stabilizing conformational flexibility in the bacterial sodium channel NaChBac
    • O'Reilly, A. O., Charalambous, K., Nurani, G., Powl, A. M., and Wallace, B. A. (2008) G219S mutagenesis as a means of stabilizing conformational flexibility in the bacterial sodium channel NaChBac Mol. Membr. Biol. 25, 670-676
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 670-676
    • O'Reilly, A.O.1    Charalambous, K.2    Nurani, G.3    Powl, A.M.4    Wallace, B.A.5
  • 36
    • 78650589362 scopus 로고    scopus 로고
    • Integration and recording of a reconstituted voltage-gated sodium channel in planar lipid bilayers
    • Studer, A., Demarche, S., Langenegger, D., and Tiefenauer, L. (2011) Integration and recording of a reconstituted voltage-gated sodium channel in planar lipid bilayers Biosens. Bioelectron. 26, 1924-1928
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 1924-1928
    • Studer, A.1    Demarche, S.2    Langenegger, D.3    Tiefenauer, L.4
  • 37
    • 5144229327 scopus 로고    scopus 로고
    • Gating of the bacterial sodium channel, NaChBac: Voltage-dependent charge movement and gating currents
    • DOI 10.1085/jgp.200409139
    • Kuzmenkin, A., Bezanilla, F., and Correa, A. M. (2004) Gating of the bacterial sodium channel, NaChBac: Voltage-dependent charge movement and gating currents J. Gen. Physiol. 124, 349-356 (Pubitemid 39346639)
    • (2004) Journal of General Physiology , vol.124 , Issue.4 , pp. 349-356
    • Kuzmenkin, A.1    Bezanilla, F.2    Correa, A.M.3
  • 39
    • 79958139475 scopus 로고    scopus 로고
    • A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy
    • Abdul-Gader, A., Miles, A. J., and Wallace, B. A. (2011) A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy Bioinformatics 27, 1630-1636
    • (2011) Bioinformatics , vol.27 , pp. 1630-1636
    • Abdul-Gader, A.1    Miles, A.J.2    Wallace, B.A.3
  • 40
    • 77955269299 scopus 로고    scopus 로고
    • The C-terminal coiled-coil of the bacterial voltage-gated sodium channel NaChBac is not essential for tetramer formation, but stabilizes subunit-to-subunit interactions
    • Mio, K., Mio, M., Arisaka, F., Sato, M., and Sato, C. (2010) The C-terminal coiled-coil of the bacterial voltage-gated sodium channel NaChBac is not essential for tetramer formation, but stabilizes subunit-to-subunit interactions Prog. Biophys. Mol. Biol. 103, 111-121
    • (2010) Prog. Biophys. Mol. Biol. , vol.103 , pp. 111-121
    • Mio, K.1    Mio, M.2    Arisaka, F.3    Sato, M.4    Sato, C.5
  • 42
    • 0024368695 scopus 로고
    • Structural parts involved in activation and inactivation of the sodium channel
    • DOI 10.1038/339597a0
    • Stuhmer, W., Conti, F., Suzuki, H., Wang, X. D., Noda, M., Yahagi, N., Kubo, H., and Numa, S. (1989) Structural parts involved in activation and inactivation of the sodium channel Nature 339, 597-603 (Pubitemid 19174342)
    • (1989) Nature , vol.339 , Issue.6226 , pp. 597-603
    • Stuhmer, W.1    Conti, F.2    Suzuki, H.3    Wang, X.4    Noda, M.5    Yagagi, N.6    Kubo, H.7    Numa, S.8
  • 44
    • 54449100445 scopus 로고    scopus 로고
    • Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation
    • DeCaen, P. G., Yarov-Yarovoy, V., Zhao, Y., Scheuer, T., and Catterall, W. A. (2008) Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation Proc. Natl. Acad. Sci. U.S.A. 105, 15142-15147
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15142-15147
    • Decaen, P.G.1    Yarov-Yarovoy, V.2    Zhao, Y.3    Scheuer, T.4    Catterall, W.A.5
  • 45
    • 79953185756 scopus 로고    scopus 로고
    • Arrangement and mobility of the voltage sensor domain in prokaryotic voltage-gated sodium channels
    • Shimomura, M., Irie, K., Nagura, H., Imai, T., and Fujiyoshi, Y. (2011) Arrangement and mobility of the voltage sensor domain in prokaryotic voltage-gated sodium channels J. Biol. Chem. 286, 7409-7417
    • (2011) J. Biol. Chem. , vol.286 , pp. 7409-7417
    • Shimomura, M.1    Irie, K.2    Nagura, H.3    Imai, T.4    Fujiyoshi, Y.5
  • 46
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., Scheuer, T., Zheng, N., and Catterall, W. A. (2011) The crystal structure of a voltage-gated sodium channel Nature 475, 353-358
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 47
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • DOI 10.1038/nature03650
    • Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K., and Okamura, Y. (2005) Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor Nature 435, 1239-1243 (Pubitemid 40943089)
    • (2005) Nature , vol.435 , Issue.7046 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 48
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • Sasaki, M., Takagi, M., and Okamura, Y. (2006) A voltage sensor-domain protein is a voltage-gated proton channel Science 312, 589-592
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 49
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • DOI 10.1038/35101535
    • Lu, Z., Klem, A. M., and Ramu, Y. (2001) Ion conduction pore is conserved among potassium channels Nature 413, 809-813 (Pubitemid 33026842)
    • (2001) Nature , vol.413 , Issue.6858 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 50
    • 40049094627 scopus 로고    scopus 로고
    • Structural Dynamics of an Isolated Voltage-Sensor Domain in a Lipid Bilayer
    • DOI 10.1016/j.str.2007.12.015, PII S096921260800021X
    • Chakrapani, S., Cuello, L. G., Cortes, D. M., and Perozo, E. (2008) Structural dynamics of an isolated voltage-sensor domain in a lipid bilayer Structure 16, 398-409 (Pubitemid 351324110)
    • (2008) Structure , vol.16 , Issue.3 , pp. 398-409
    • Chakrapani, S.1    Cuello, L.G.2    Cortes, D.M.3    Perozo, E.4
  • 51
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80143-9
    • + channel Neuron 16, 1169-1177 (Pubitemid 26227238)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 53
    • 0032031204 scopus 로고    scopus 로고
    • Voltage-gated ion channels and electrical excitability
    • DOI 10.1016/S0896-6273(00)80981-2
    • Armstrong, C. M. and Hille, B. (1998) Voltage-gated ion channels and electrical excitability Neuron 20, 371-380 (Pubitemid 28153071)
    • (1998) Neuron , vol.20 , Issue.3 , pp. 371-380
    • Armstrong, C.M.1    Hille, B.2
  • 54
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • Heinemann, S. H., Terlau, H., Stuhmer, W., Imoto, K., and Numa, S. (1992) Calcium channel characteristics conferred on the sodium channel by single mutations Nature 356, 441-443
    • (1992) Nature , vol.356 , pp. 441-443
    • Heinemann, S.H.1    Terlau, H.2    Stuhmer, W.3    Imoto, K.4    Numa, S.5
  • 56
    • 0036899251 scopus 로고    scopus 로고
    • The cation selectivity filter of the bacterial sodium channel, NaChBac
    • DOI 10.1085/jgp.20028699
    • Yue, L., Navarro, B., Ren, D., Ramos, A., and Clapham, D. E. (2002) The cation selectivity filter of the bacterial sodium channel, NaChBac J. Gen. Physiol. 120, 845-853 (Pubitemid 35435016)
    • (2002) Journal of General Physiology , vol.120 , Issue.6 , pp. 845-853
    • Yue, L.1    Navarro, B.2    Ren, D.3    Ramos, A.4    Clapham, D.E.5
  • 58
    • 0034702931 scopus 로고    scopus 로고
    • Molecular pharmacology of the sodium channel mutation D1790G linked to the long-QT syndrome
    • Abriel, H., Wehrens, X. H., Benhorin, J., Kerem, B., and Kass, R. S. (2000) Molecular pharmacology of the sodium channel mutation D1790G linked to the long-QT syndrome Circulation 102, 921-925
    • (2000) Circulation , vol.102 , pp. 921-925
    • Abriel, H.1    Wehrens, X.H.2    Benhorin, J.3    Kerem, B.4    Kass, R.S.5
  • 59
    • 0037066036 scopus 로고    scopus 로고
    • + channel mutation that causes both Brugada and long-QT syndrome phenotypes: A simulation study of mechanism
    • DOI 10.1161/hc1002.105183
    • + channel mutation that causes both Brugada and long-QT syndrome phenotypes: A simulation study of mechanism Circulation 105, 1208-1213 (Pubitemid 34225822)
    • (2002) Circulation , vol.105 , Issue.10 , pp. 1208-1213
    • Clancy, C.E.1    Rudy, Y.2
  • 60
    • 0344672944 scopus 로고    scopus 로고
    • Mutations of sodium channel α subunit type 1 (SCN1A) in intractable childhood epilepsies with frequent generalized tonic-clonic seizures
    • DOI 10.1093/brain/awg053
    • Fujiwara, T., Sugawara, T., Mazaki-Miyazaki, E., Takahashi, Y., Fukushima, K., Watanabe, M., Hara, K., Morikawa, T., Yagi, K., Yamakawa, K., and Inoue, Y. (2003) Mutations of sodium channel α subunit type 1 (SCN1A) in intractable childhood epilepsies with frequent generalized tonic-clonic seizures Brain 126, 531-546 (Pubitemid 36240855)
    • (2003) Brain , vol.126 , Issue.3 , pp. 531-546
    • Fujiwara, T.1    Sugawara, T.2    Mazaki-Miyazaki, E.3    Takahashi, Y.4    Fukushima, K.5    Watanabe, M.6    Hara, K.7    Morikawa, T.8    Yagi, K.9    Yamakawa, K.10    Inoue, Y.11
  • 61
    • 65249136569 scopus 로고    scopus 로고
    • Solution NMR structure of the C-terminal EF-hand domain of human cardiac sodium channel NaV1.5
    • Chagot, B., Potet, F., Balser, J. R., and Chazin, W. J. (2009) Solution NMR structure of the C-terminal EF-hand domain of human cardiac sodium channel NaV1.5 J. Biol. Chem. 284, 6436-6445
    • (2009) J. Biol. Chem. , vol.284 , pp. 6436-6445
    • Chagot, B.1    Potet, F.2    Balser, J.R.3    Chazin, W.J.4
  • 63
    • 0037415755 scopus 로고    scopus 로고
    • C-terminal domains implicated in the functional surface expression of potassium channels
    • DOI 10.1093/emboj/cdg035
    • Jenke, M., Sanchez, A., Monje, F., Stuhmer, W., Weseloh, R. M., and Pardo, L. A. (2003) C-terminal domains implicated in the functional surface expression of potassium channels EMBO J. 22, 395-403 (Pubitemid 36193585)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 395-403
    • Jenke, M.1    Sanchez, A.2    Monje, F.3    Stuhmer, W.4    Weseloh, R.M.5    Pardo, L.A.6
  • 64
    • 0030606298 scopus 로고    scopus 로고
    • Regions responsible for the assembly of inwardly rectifying potassium channels
    • DOI 10.1016/S0092-8674(00)81993-5
    • Tinker, A., Jan, Y. N., and Jan, L. Y. (1996) Regions responsible for the assembly of inwardly rectifying potassium channels Cell 87, 857-868 (Pubitemid 26404285)
    • (1996) Cell , vol.87 , Issue.5 , pp. 857-868
    • Tinker, A.1    Jan, Y.N.2    Jan, L.Y.3
  • 65
    • 0026045545 scopus 로고
    • + channel behaves like an open-channel blocker
    • + channel behaves like an open-channel blocker Neuron 7, 743-753
    • (1991) Neuron , vol.7 , pp. 743-753
    • Demo, S.D.1    Yellen, G.2
  • 66
    • 23244467740 scopus 로고    scopus 로고
    • The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel
    • DOI 10.1529/biophysj.104.056994
    • Pavlov, E., Bladen, C., Winkfein, R., Diao, C., Dhaliwal, P., and French, R. J. (2005) The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel Biophys. J. 89, 232-242 (Pubitemid 41098278)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 232-242
    • Pavlov, E.1    Bladen, C.2    Winkfein, R.3    Diao, C.4    Dhaliwal, P.5    French, R.J.6
  • 67
  • 69
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestele, S. and Catterall, W. A. (2000) Molecular mechanisms of neurotoxin action on voltage-gated sodium channels Biochimie 82, 883-892
    • (2000) Biochimie , vol.82 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 70
    • 33846513431 scopus 로고    scopus 로고
    • Voltage-gated ion channels and gating modifier toxins
    • DOI 10.1016/j.toxicon.2006.09.022, PII S0041010106003461
    • Catterall, W. A., Cestele, S., Yarov-Yarovoy, V., Yu, F. H., Konoki, K., and Scheuer, T. (2007) Voltage-gated ion channels and gating modifier toxins Toxicon 49, 124-141 (Pubitemid 46151715)
    • (2007) Toxicon , vol.49 , Issue.2 , pp. 124-141
    • Catterall, W.A.1    Cestele, S.2    Yarov-Yarovoy, V.3    Yu, F.H.4    Konoki, K.5    Scheuer, T.6
  • 71
    • 0026490286 scopus 로고
    • Cellular and molecular biology of voltage-gated sodium channels
    • Catterall, W. A. (1992) Cellular and molecular biology of voltage-gated sodium channels Physiol. Rev. 72, S15-S48
    • (1992) Physiol. Rev. , vol.72
    • Catterall, W.A.1
  • 75
    • 0024810050 scopus 로고
    • The sharpey-schafer lecture. Ionic channels: Evolutionary origins and modern roles
    • Hille, B. (1989) The Sharpey-Schafer Lecture. Ionic channels: Evolutionary origins and modern roles Q. J. Exp. Physiol. Cogn. Med. Sci. 74, 785-804 (Pubitemid 20078487)
    • (1989) Quarterly Journal of Experimental Physiology , vol.74 , Issue.6 , pp. 785-804
    • Hille, B.1
  • 76
    • 0030977971 scopus 로고    scopus 로고
    • Fast and slow activation kinetics of voltage-gated sodium channels in molluscan neurons
    • Gilly, W. F., Gillette, R., and McFarlane, M. (1997) Fast and slow activation kinetics of voltage-gated sodium channels in molluscan neurons J. Neurophysiol. 77, 2373-2384 (Pubitemid 27209210)
    • (1997) Journal of Neurophysiology , vol.77 , Issue.5 , pp. 2373-2384
    • Gilly, W.F.1    Gillette, R.2    McFarlane, M.3
  • 79
    • 29844456883 scopus 로고    scopus 로고
    • International Union of Pharmacology. L. Nomenclature and structure-function relationships of CatSper and two-pore channels
    • DOI 10.1124/pr.57.4.7
    • Clapham, D. E. and Garbers, D. L. (2005) International Union of Pharmacology. L. Nomenclature and structure-function relationships of CatSper and two-pore channels Pharm. Rev. 57, 451-454 (Pubitemid 43036434)
    • (2005) Pharmacological Reviews , vol.57 , Issue.4 , pp. 451-454
    • Clapham, D.E.1    Garbers, D.L.2
  • 80
    • 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, J. D., Higgins, D. G., and Gibson, T. J. (1994) Clustal-W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22, 4673-4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 81
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes J. Mol. Biol. 305, 567-580 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.