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Volumn 355, Issue 6328, 2017, Pages

Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE; VOLTAGE GATED SODIUM CHANNEL; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL ALPHA SUBUNIT;

EID: 85013031896     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aal4326     Document Type: Article
Times cited : (335)

References (105)
  • 1
    • 84944495530 scopus 로고
    • Resting and action potentials in single nerve fibres
    • pmid: 16991677
    • A. L. Hodgkin, A. F. Huxley, Resting and action potentials in single nerve fibres. J. Physiol. 104, 176-195 (1945). doi: 10. 1113/jphysiol. 1945. sp004114; pmid: 16991677
    • (1945) J. Physiol. , vol.104 , pp. 176-195
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 2
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • pmid: 12991237
    • A. L. Hodgkin, A. F. Huxley, A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117, 500-544 (1952). doi: 10. 1113/jphysiol. 1952. sp004764; pmid: 12991237
    • (1952) J. Physiol. , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 4
    • 84977607706 scopus 로고    scopus 로고
    • The hitchhiker's guide to the voltage-gated sodium channel galaxy
    • pmid: 26712848
    • C. A. Ahern, J. Payandeh, F. Bosmans, B. Chanda, The hitchhiker's guide to the voltage-gated sodium channel galaxy. J. Gen. Physiol. 147, 1-24 (2016). doi: 10. 1085/ jgp. 201511492; pmid: 26712848
    • (2016) J. Gen. Physiol. , vol.147 , pp. 1-24
    • Ahern, C.A.1    Payandeh, J.2    Bosmans, F.3    Chanda, B.4
  • 5
    • 84891854608 scopus 로고    scopus 로고
    • Sodium channels, inherited epilepsy, and antiepileptic drugs
    • pmid: 24392695
    • W. A. Catterall, Sodium channels, inherited epilepsy, and antiepileptic drugs. Annu. Rev. Pharmacol. Toxicol. 54, 317-338 (2014). doi: 10. 1146/annurev-pharmtox-011112-140232; pmid: 24392695
    • (2014) Annu. Rev. Pharmacol. Toxicol. , vol.54 , pp. 317-338
    • Catterall, W.A.1
  • 7
    • 84963997524 scopus 로고    scopus 로고
    • Voltage gated sodium channels as drug discovery targets
    • pmid: 26646477
    • S. K. Bagal, B. E. Marron, R. M. Owen, R. I. Storer, N. A. Swain, Voltage gated sodium channels as drug discovery targets. Channels (Austin) 9, 360-366 (2015). doi: 10. 1080/19336950. 2015. 1079674; pmid: 26646477
    • (2015) Channels (Austin) , vol.9 , pp. 360-366
    • Bagal, S.K.1    Marron, B.E.2    Owen, R.M.3    Storer, R.I.4    Swain, N.A.5
  • 8
    • 0021330126 scopus 로고
    • The molecular basis of neuronal excitability
    • pmid: 6320365
    • W. A. Catterall, The molecular basis of neuronal excitability. Science 223, 653-661 (1984). doi: 10. 1126/science. 6320365; pmid: 6320365
    • (1984) Science , vol.223 , pp. 653-661
    • Catterall, W.A.1
  • 9
    • 84922785492 scopus 로고    scopus 로고
    • Sodium channel b subunits: Emerging targets in channelopathies
    • pmid: 25668026
    • H. A. O'Malley, L. L. Isom, Sodium channel b subunits: Emerging targets in channelopathies. Annu. Rev. Physiol. 77, 481-504 (2015). doi: 10. 1146/annurev-physiol-021014-071846; pmid: 25668026
    • (2015) Annu. Rev. Physiol. , vol.77 , pp. 481-504
    • O'Malley, H.A.1    Isom, L.L.2
  • 10
    • 0033636506 scopus 로고    scopus 로고
    • Nomenclature of voltage-gated sodium channels
    • pmid: 11144347
    • A. L. Goldin et al., Nomenclature of voltage-gated sodium channels. Neuron 28, 365-368 (2000). doi: 10. 1016/ S0896-6273(00)00116-1; pmid: 11144347
    • (2000) Neuron , vol.28 , pp. 365-368
    • Goldin, A.L.1
  • 11
    • 0034666838 scopus 로고    scopus 로고
    • Nav2/NaG channel is involved in control of salt-intake behavior in the CNS
    • pmid: 11027237
    • E. Watanabe et al., Nav2/NaG channel is involved in control of salt-intake behavior in the CNS. J. Neurosci. 20, 7743-7751 (2000). pmid: 11027237
    • (2000) J. Neurosci. , vol.20 , pp. 7743-7751
    • Watanabe, E.1
  • 12
    • 0027497515 scopus 로고
    • Molecular evolution of voltage-sensitive ion channel genes: On the origins of electrical excitability
    • pmid: 7680747
    • M. Strong, K. G. Chandy, G. A. Gutman, Molecular evolution of voltage-sensitive ion channel genes: On the origins of electrical excitability. Mol. Biol. Evol. 10, 221-242 (1993). pmid: 7680747
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 221-242
    • Strong, M.1    Chandy, K.G.2    Gutman, G.A.3
  • 13
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K+ channel
    • pmid: 12721618
    • Y. Jiang et al., X-ray structure of a voltage-dependent K+ channel. Nature 423, 33-41 (2003). doi: 10. 1038/ nature01580; pmid: 12721618
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 14
    • 84958214652 scopus 로고    scopus 로고
    • An update on transcriptional and post-translational regulation of brain voltage-gated sodium channels
    • pmid: 26503606
    • D. O. Onwuli, P. Beltran-Alvarez, An update on transcriptional and post-translational regulation of brain voltage-gated sodium channels. Amino Acids 48, 641-651 (2016). doi: 10. 1007/s00726-015-2122-y; pmid: 26503606
    • (2016) Amino Acids , vol.48 , pp. 641-651
    • Onwuli, D.O.1    Beltran-Alvarez, P.2
  • 15
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • pmid: 11743207
    • D. Ren et al., A prokaryotic voltage-gated sodium channel. Science 294, 2372-2375 (2001). doi: 10. 1126/ science. 1065635; pmid: 11743207
    • (2001) Science , vol.294 , pp. 2372-2375
    • Ren, D.1
  • 16
    • 0032478818 scopus 로고    scopus 로고
    • The structure of the potassium channel: Molecular basis of K+ conduction and selectivity
    • pmid: 9525859
    • D. A. Doyle et al., The structure of the potassium channel: Molecular basis of K+ conduction and selectivity. Science 280, 69-77 (1998). doi: 10. 1126/science. 280. 5360. 69; pmid: 9525859
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 17
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • pmid: 21743477
    • J. Payandeh, T. Scheuer, N. Zheng, W. A. Catterall, The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358 (2011). doi: 10. 1038/nature10238; pmid: 21743477
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 18
    • 84950282257 scopus 로고    scopus 로고
    • Structure of the voltage-gated calcium channel Cav1. 1 complex
    • pmid: 26680202
    • J. Wu et al., Structure of the voltage-gated calcium channel Cav1. 1 complex. Science 350, aad2395 (2015). doi: 10. 1126/ science. aad2395; pmid: 26680202
    • (2015) Science , vol.350 , pp. aad2395
    • Wu, J.1
  • 19
    • 0036899251 scopus 로고    scopus 로고
    • The cation selectivity filter of the bacterial sodium channel
    • pmid: 12451053
    • L. Yue, B. Navarro, D. Ren, A. Ramos, D. E. Clapham, The cation selectivity filter of the bacterial sodium channel, NaChBac. J. Gen. Physiol. 120, 845-853 (2002). doi: 10. 1085/jgp. 20028699; pmid: 12451053
    • (2002) NaChBac. J. Gen. Physiol. , vol.120 , pp. 845-853
    • Yue, L.1    Navarro, B.2    Ren, D.3    Ramos, A.4    Clapham, D.E.5
  • 20
    • 0027340610 scopus 로고
    • Molecular determinants of Ca2+ selectivity and ion permeation in L-type Ca2+ channels
    • pmid: 8232554
    • J. Yang, P. T. Ellinor, W. A. Sather, J. F. Zhang, R. W. Tsien, Molecular determinants of Ca2+ selectivity and ion permeation in L-type Ca2+ channels. Nature 366, 158-161 (1993). doi: 10. 1038/366158a0; pmid: 8232554
    • (1993) Nature , vol.366 , pp. 158-161
    • Yang, J.1    Ellinor, P.T.2    Sather, W.A.3    Zhang, J.F.4    Tsien, R.W.5
  • 21
    • 0028973249 scopus 로고
    • Ca2+ channel selectivity at a single locus for high-affinity Ca2+ interactions
    • pmid: 7576655
    • P. T. Ellinor, J. Yang, W. A. Sather, J. F. Zhang, R. W. Tsien, Ca2+ channel selectivity at a single locus for high-affinity Ca2+ interactions. Neuron 15, 1121-1132 (1995). doi: 10. 1016/ 0896-6273(95)90100-0; pmid: 7576655
    • (1995) Neuron , vol.15 , pp. 1121-1132
    • Ellinor, P.T.1    Yang, J.2    Sather, W.A.3    Zhang, J.F.4    Tsien, R.W.5
  • 22
    • 0029754658 scopus 로고    scopus 로고
    • On the structural basis for ionic selectivity among Na+, K+, and Ca2+ in the voltage-gated sodium channel
    • pmid: 8968582
    • I. Favre, E. Moczydlowski, L. Schild, On the structural basis for ionic selectivity among Na+, K+, and Ca2+ in the voltage-gated sodium channel. Biophys. J. 71, 3110-3125 (1996). doi: 10. 1016/S0006-3495(96)79505-X; pmid: 8968582
    • (1996) Biophys. J. , vol.71 , pp. 3110-3125
    • Favre, I.1    Moczydlowski, E.2    Schild, L.3
  • 23
    • 0030777655 scopus 로고    scopus 로고
    • On the structural basis for size-selective permeation of organic cations through the voltage-gated sodium channel. Effect of alanine mutations at the DEKA locus on selectivity, inhibition by Ca2+ and H+, and molecular sieving
    • pmid: 9382897
    • Y. M. Sun, I. Favre, L. Schild, E. Moczydlowski, On the structural basis for size-selective permeation of organic cations through the voltage-gated sodium channel. Effect of alanine mutations at the DEKA locus on selectivity, inhibition by Ca2+ and H+, and molecular sieving. J. Gen. Physiol. 110, 693-715 (1997). doi: 10. 1085/ jgp. 110. 6. 693; pmid: 9382897
    • (1997) J. Gen. Physiol. , vol.110 , pp. 693-715
    • Sun, Y.M.1    Favre, I.2    Schild, L.3    Moczydlowski, E.4
  • 24
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • pmid: 4824995
    • C. M. Armstrong, F. Bezanilla, Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol. 63, 533-552 (1974). doi: 10. 1085/jgp. 63. 5. 533; pmid: 4824995
    • (1974) J. Gen. Physiol. , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Bezanilla, F.2
  • 25
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • pmid: 1553560
    • N. E. Schoppa, K. McCormack, M. A. Tanouye, F. J. Sigworth, The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255, 1712-1715 (1992). doi: 10. 1126/science. 1553560; pmid: 1553560
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 26
    • 0030175867 scopus 로고    scopus 로고
    • Voltagesensing residues in the S2 and S4 segments of the Shaker K+ channel
    • pmid: 8663992
    • S. A. Seoh, D. Sigg, D. M. Papazian, F. Bezanilla, Voltagesensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron 16, 1159-1167 (1996). doi: 10. 1016/ S0896-6273(00)80142-7; pmid: 8663992
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 27
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4 segment to gating charge in the Shaker K+ channel
    • pmid: 8663993
    • S. K. Aggarwal, R. MacKinnon, Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16, 1169-1177 (1996). doi: 10. 1016/S0896-6273(00)80143-9; pmid: 8663993
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 28
    • 54449100445 scopus 로고    scopus 로고
    • Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation
    • pmid: 18809926
    • P. G. DeCaen, V. Yarov-Yarovoy, Y. Zhao, T. Scheuer, W. A. Catterall, Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation. Proc. Natl. Acad. Sci. U. S. A. 105, 15142-15147 (2008). doi: 10. 1073/pnas. 0806486105; pmid: 18809926
    • (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
  • 29
    • 76049115811 scopus 로고    scopus 로고
    • Sequential formation of ion pairs during activation of a sodium channel voltage sensor
    • pmid: 20007787
    • P. G. DeCaen, V. Yarov-Yarovoy, E. M. Sharp, T. Scheuer, W. A. Catterall, Sequential formation of ion pairs during activation of a sodium channel voltage sensor. Proc. Natl. Acad. Sci. U. S. A. 106, 22498-22503 (2009). doi: 10. 1073/ pnas. 0912307106; pmid: 20007787
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 22498-22503
    • DeCaen, P.G.1    Yarov-Yarovoy, V.2    Sharp, E.M.3    Scheuer, T.4    Catterall, W.A.5
  • 30
    • 84861952634 scopus 로고    scopus 로고
    • Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel
    • pmid: 22678295
    • X. Zhang et al., Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel. Nature 486, 130-134 (2012). pmid: 22678295
    • (2012) Nature , vol.486 , pp. 130-134
    • Zhang, X.1
  • 31
    • 77950488909 scopus 로고    scopus 로고
    • A gating charge transfer center in voltage sensors
    • pmid: 20360102
    • X. Tao, A. Lee, W. Limapichat, D. A. Dougherty, R. MacKinnon, A gating charge transfer center in voltage sensors. Science 328, 67-73 (2010). doi: 10. 1126/science. 1185954; pmid: 20360102
    • (2010) Science , vol.328 , pp. 67-73
    • Tao, X.1    Lee, A.2    Limapichat, W.3    Dougherty, D.A.4    MacKinnon, R.5
  • 32
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1. 2: Structural basis of electromechanical coupling
    • pmid: 16002579
    • S. B. Long, E. B. Campbell, R. Mackinnon, Voltage sensor of Kv1. 2: Structural basis of electromechanical coupling. Science 309, 903-908 (2005). doi: 10. 1126/science. 1116270; pmid: 16002579
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 33
    • 84981510441 scopus 로고    scopus 로고
    • Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism
    • pmid: 27516594
    • J. R. Whicher, R. MacKinnon, Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism. Science 353, 664-669 (2016). doi: 10. 1126/science. aaf8070; pmid: 27516594
    • (2016) Science , vol.353 , pp. 664-669
    • Whicher, J.R.1    MacKinnon, R.2
  • 34
    • 85009210607 scopus 로고    scopus 로고
    • Structures of the human HCN1 hyperpolarization-activated channel
    • pmid: 28086084
    • C. H. Lee, R. MacKinnon, Structures of the human HCN1 hyperpolarization-activated channel. Cell 168, 111-120. e11 (2017). doi: 10. 1016/j. cell. 2016. 12. 023; pmid: 28086084
    • (2017) Cell , vol.168 , pp. 111-120e11
    • Lee, C.H.1    MacKinnon, R.2
  • 35
    • 85016153996 scopus 로고    scopus 로고
    • Structural basis for gating the high-conductance Ca2+-activated K+ channel
    • pmid: 27974801
    • R. K. Hite, X. Tao, R. MacKinnon, Structural basis for gating the high-conductance Ca2+-activated K+ channel. Nature 541, 52-57 (2017). doi: 10. 1038/nature20775; pmid: 27974801
    • (2017) Nature , vol.541 , pp. 52-57
    • Hite, R.K.1    Tao, X.2    MacKinnon, R.3
  • 36
    • 85016153637 scopus 로고    scopus 로고
    • Structure of a eukaryotic cyclic-nucleotide-gated channel
    • pmid: 28099415
    • M. Li et al., Structure of a eukaryotic cyclic-nucleotide-gated channel. Nature 542, 60-65 (2017). doi: 10. 1038/ nature20819; pmid: 28099415
    • (2017) Nature , vol.542 , pp. 60-65
    • Li, M.1
  • 37
    • 0023784649 scopus 로고
    • Identification of an intracellular peptide segment involved in sodium channel inactivation
    • pmid: 2458625
    • P. M. Vassilev, T. Scheuer, W. A. Catterall, Identification of an intracellular peptide segment involved in sodium channel inactivation. Science 241, 1658-1661 (1988). doi: 10. 1126/science. 2458625; pmid: 2458625
    • (1988) Science , vol.241 , pp. 1658-1661
    • Vassilev, P.M.1    Scheuer, T.2    Catterall, A.W.3
  • 38
    • 25444498065 scopus 로고    scopus 로고
    • Sodium channel inactivation: Molecular determinants and modulation
    • pmid: 16183913
    • W. Ulbricht, Sodium channel inactivation: Molecular determinants and modulation. Physiol. Rev. 85, 1271-1301 (2005). doi: 10. 1152/physrev. 00024. 2004; pmid: 16183913
    • (2005) Physiol. Rev. , vol.85 , pp. 1271-1301
    • Ulbricht, W.1
  • 39
    • 0028297301 scopus 로고
    • An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding
    • pmid: 8038379
    • G. Yellen, D. Sodickson, T. Y. Chen, M. E. Jurman, An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding. Biophys. J. 66, 1068-1075 (1994). doi: 10. 1016/ S0006-3495(94)80888-4; pmid: 8038379
    • (1994) Biophys. J. , vol.66 , pp. 1068-1075
    • Yellen, G.1    Sodickson, D.2    Chen, T.Y.3    Jurman, M.E.4
  • 40
    • 0028822993 scopus 로고
    • Cooperative subunit interactions in C-type inactivation of K channels
    • pmid: 8599651
    • E. M. Ogielska et al., Cooperative subunit interactions in C-type inactivation of K channels. Biophys. J. 69, 2449-2457 (1995). doi: 10. 1016/S0006-3495(95)80114-1; pmid: 8599651
    • (1995) Biophys. J. , vol.69 , pp. 2449-2457
    • Ogielska, E.M.1
  • 41
    • 0032982292 scopus 로고    scopus 로고
    • Ultra-slow inactivation in m1 Na+ channels is produced by a structural rearrangement of the outer vestibule
    • pmid: 10049317
    • H. Todt, S. C. Dudley Jr., J. W. Kyle, R. J. French, H. A. Fozzard, Ultra-slow inactivation in m1 Na+ channels is produced by a structural rearrangement of the outer vestibule. Biophys. J. 76, 1335-1345 (1999). doi: 10. 1016/ S0006-3495(99)77296-6; pmid: 10049317
    • (1999) Biophys. J. , vol.76 , pp. 1335-1345
    • Todt, H.1    Dudley, S.C.2    Kyle, J.W.3    French, R.J.4    Fozzard, H.A.5
  • 42
    • 23244467740 scopus 로고    scopus 로고
    • The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel
    • pmid: 15849254
    • E. Pavlov et al., The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel. Biophys. J. 89, 232-242 (2005). doi: 10. 1529/biophysj. 104. 056994; pmid: 15849254
    • (2005) Biophys. J. , vol.89 , pp. 232-242
    • Pavlov, E.1
  • 43
    • 77954485089 scopus 로고    scopus 로고
    • Structural mechanism of C-type inactivation in K+ channels
    • pmid: 20613835
    • L. G. Cuello, V. Jogini, D. M. Cortes, E. Perozo, Structural mechanism of C-type inactivation in K+ channels. Nature 466, 203-208 (2010). doi: 10. 1038/nature09153; pmid: 20613835
    • (2010) Nature , vol.466 , pp. 203-208
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Perozo, E.4
  • 44
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • pmid: 18004376
    • S. B. Long, X. Tao, E. B. Campbell, R. MacKinnon, Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450, 376-382 (2007). doi: 10. 1038/nature06265; pmid: 18004376
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 45
    • 84869478035 scopus 로고    scopus 로고
    • Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing
    • pmid: 23033078
    • E. C. McCusker et al., Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing. Nat. Commun. 3, 1102 (2012). doi: 10. 1038/ ncomms2077; pmid: 23033078
    • (2012) Nat. Commun. , vol.3 , pp. 1102
    • McCusker, E.C.1
  • 46
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • pmid: 24305160
    • M. Liao, E. Cao, D. Julius, Y. Cheng, Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013). doi: 10. 1038/nature12822; pmid: 24305160
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 47
    • 84904560883 scopus 로고    scopus 로고
    • Three-dimensional structure of human g-secretase
    • pmid: 25043039
    • P. Lu et al., Three-dimensional structure of human g-secretase. Nature 512, 166-170 (2014). doi: 10. 1038/ nature13567; pmid: 25043039
    • (2014) Nature , vol.512 , pp. 166-170
    • Lu, P.1
  • 48
    • 84942474131 scopus 로고    scopus 로고
    • Structure of a yeast spliceosome at 3. 6-angstrom resolution
    • pmid: 26292707
    • C. Yan et al., Structure of a yeast spliceosome at 3. 6-angstrom resolution. Science 349, 1182-1191 (2015). doi: 10. 1126/science. aac7629; pmid: 26292707
    • (2015) Science , vol.349 , pp. 1182-1191
    • Yan, C.1
  • 49
    • 84986575661 scopus 로고    scopus 로고
    • Structure of the voltage-gated calcium channel Cav1. 1 at 3. 6 Å resolution
    • pmid: 27580036
    • J. Wu et al., Structure of the voltage-gated calcium channel Cav1. 1 at 3. 6 Å resolution. Nature 537, 191-196 (2016). doi: 10. 1038/nature19321; pmid: 27580036
    • (2016) Nature , vol.537 , pp. 191-196
    • Wu, J.1
  • 50
    • 85011294805 scopus 로고    scopus 로고
    • Structure-based assessment of disease-related mutations in human voltage-gated sodium channels
    • W. Huang, M. Liu, F. S. Yan, N. Yan, Structure-based assessment of disease-related mutations in human voltage-gated sodium channels. Protein Cell 2017, s13238-017-0372-z (2017). doi: 10. 1007/s13238-017-0372-z
    • (2017) Protein Cell , vol.2017 , pp. s13238017-0372z
    • Huang, W.1    Liu, M.2    Yan, F.S.3    Yan, N.4
  • 51
    • 84928027320 scopus 로고    scopus 로고
    • Benchmarking the stability of human detergent-solubilised voltage-gated sodium channels for structural studies using eel as a reference
    • pmid: 25838126
    • D. Slowik, R. Henderson, Benchmarking the stability of human detergent-solubilised voltage-gated sodium channels for structural studies using eel as a reference. Biochim. Biophys. Acta 1848, 1545-1551 (2015). doi: 10. 1016/ j. bbamem. 2015. 03. 021; pmid: 25838126
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1545-1551
    • Slowik, D.1    Henderson, R.2
  • 52
    • 33847348405 scopus 로고    scopus 로고
    • Insect sodium channels and insecticide resistance
    • pmid: 17206406
    • K. Dong, Insect sodium channels and insecticide resistance. Invert. Neurosci. 7, 17-30 (2007). doi: 10. 1007/ s10158-006-0036-9; pmid: 17206406
    • (2007) Invert. Neurosci. , vol.7 , pp. 17-30
    • Dong, K.1
  • 53
    • 0029091192 scopus 로고
    • Cloning and functional analysis of TipE, a novel membrane protein that enhances Drosophila para sodium channel function
    • pmid: 7553842
    • G. Feng, P. Deák, M. Chopra, L. M. Hall, Cloning and functional analysis of TipE, a novel membrane protein that enhances Drosophila para sodium channel function. Cell 82, 1001-1011 (1995). doi: 10. 1016/0092-8674(95)90279-1; pmid: 7553842
    • (1995) Cell , vol.82 , pp. 1001-1011
    • Feng, G.1    Deák, P.2    Chopra, M.3    Hall, L.M.4
  • 54
    • 70450224251 scopus 로고    scopus 로고
    • The discovery of a novel sodium channel in the cockroach Periplaneta americana: Evidence for an early duplication of the para-like gene
    • pmid: 19800971
    • B. Moignot, C. Lemaire, S. Quinchard, B. Lapied, C. Legros, The discovery of a novel sodium channel in the cockroach Periplaneta americana: Evidence for an early duplication of the para-like gene. Insect Biochem. Mol. Biol. 39, 814-823 (2009). doi: 10. 1016/j. ibmb. 2009. 09. 006; pmid: 19800971
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , pp. 814-823
    • Moignot, B.1    Lemaire, C.2    Quinchard, S.3    Lapied, B.4    Legros, C.5
  • 55
    • 0026483172 scopus 로고
    • A cluster of hydrophobic amino acid residues required for fast Na+-channel inactivation
    • pmid: 1332060
    • J. W. West et al., A cluster of hydrophobic amino acid residues required for fast Na+-channel inactivation. Proc. Natl. Acad. Sci. U. S. A. 89, 10910-10914 (1992). doi: 10. 1073/ pnas. 89. 22. 10910; pmid: 1332060
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10910-10914
    • West, J.W.1
  • 56
    • 84992597299 scopus 로고    scopus 로고
    • The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs
    • pmid: 27768895
    • P. S. Shen et al., The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs. Cell 167, 763-773. e11 (2016). doi: 10. 1016/j. cell. 2016. 09. 048; pmid: 27768895
    • (2016) Cell , vol.167 , pp. 763-773e11
    • Shen, P.S.1
  • 57
    • 84881573183 scopus 로고    scopus 로고
    • Intron retention in mRNA encoding ancillary subunit of insect voltage-gated sodium channel modulates channel expression, gating regulation and drug sensitivity
    • pmid: 23967047
    • C. M. Bourdin et al., Intron retention in mRNA encoding ancillary subunit of insect voltage-gated sodium channel modulates channel expression, gating regulation and drug sensitivity. PLOS ONE 8, e67290 (2013). doi: 10. 1371/ journal. pone. 0067290; pmid: 23967047
    • (2013) PLOS ONE , vol.8 , pp. e67290
    • Bourdin, C.M.1
  • 58
    • 84893077319 scopus 로고    scopus 로고
    • Sodium channel selectivity and conduction: Prokaryotes have devised their own molecular strategy
    • pmid: 24420772
    • R. K. Finol-Urdaneta et al., Sodium channel selectivity and conduction: Prokaryotes have devised their own molecular strategy. J. Gen. Physiol. 143, 157-171 (2014). doi: 10. 1085/ jgp. 201311037; pmid: 24420772
    • (2014) J. Gen. Physiol. , vol.143 , pp. 157-171
    • Finol-Urdaneta, R.K.1
  • 59
    • 0015166645 scopus 로고
    • The permeability of the sodium channel to organic cations in myelinated nerve
    • pmid: 5315827
    • B. Hille, The permeability of the sodium channel to organic cations in myelinated nerve. J. Gen. Physiol. 58, 599-619 (1971). doi: 10. 1085/jgp. 58. 6. 599; pmid: 5315827
    • (1971) J. Gen. Physiol. , vol.58 , pp. 599-619
    • Hille, B.1
  • 60
    • 84961262752 scopus 로고    scopus 로고
    • Binary architecture of the Nav1. 2-b2 signaling complex
    • pmid: 26894959 10. 7554/eLife. 10960
    • S. Das, J. Gilchrist, F. Bosmans, F. Van Petegem, Binary architecture of the Nav1. 2-b2 signaling complex. eLife 5, 10. 7554/eLife. 10960 (2016). doi: 10. 7554/eLife. 10960; pmid: 26894959
    • (2016) ELife , vol.5
    • Das, S.1    Gilchrist, J.2    Bosmans, F.3    Van Petegem, F.4
  • 61
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • pmid: 4700900
    • C. M. Armstrong, F. Bezanilla, Currents related to movement of the gating particles of the sodium channels. Nature 242, 459-461 (1973). doi: 10. 1038/242459a0; pmid: 4700900
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 62
    • 0024368695 scopus 로고
    • Structural parts involved in activation and inactivation of the sodium channel
    • pmid: 2543931
    • W. Stühmer et al., Structural parts involved in activation and inactivation of the sodium channel. Nature 339, 597-603 (1989). doi: 10. 1038/339597a0; pmid: 2543931
    • (1989) Nature , vol.339 , pp. 597-603
    • Stühmer, W.1
  • 63
    • 0008453646 scopus 로고
    • Inhibition of inactivation of single sodium channels by a site-directed antibody
    • pmid: 2554301
    • P. Vassilev, T. Scheuer, W. A. Catterall, Inhibition of inactivation of single sodium channels by a site-directed antibody. Proc. Natl. Acad. Sci. U. S. A. 86, 8147-8151 (1989). doi: 10. 1073/pnas. 86. 20. 8147; pmid: 2554301
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 8147-8151
    • Vassilev, P.1    Scheuer, T.2    Catterall, W.A.3
  • 64
    • 0039552118 scopus 로고    scopus 로고
    • Solution structure of the sodium channel inactivation gate
    • pmid: 9893979
    • C. A. Rohl et al., Solution structure of the sodium channel inactivation gate. Biochemistry 38, 855-861 (1999). doi: 10. 1021/bi9823380; pmid: 9893979
    • (1999) Biochemistry , vol.38 , pp. 855-861
    • Rohl, C.A.1
  • 65
    • 84863534231 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin
    • pmid: 22705208
    • C. Wang, B. C. Chung, H. Yan, S. Y. Lee, G. S. Pitt, Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure 20, 1167-1176 (2012). doi: 10. 1016/ j. str. 2012. 05. 001; pmid: 22705208
    • (2012) Structure , vol.20 , pp. 1167-1176
    • Wang, C.1    Chung, B.C.2    Yan, H.3    Lee, S.Y.4    Pitt, G.S.5
  • 66
    • 84883277214 scopus 로고    scopus 로고
    • Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels
    • pmid: 23858005
    • D. L. Capes, M. P. Goldschen-Ohm, M. Arcisio-Miranda, F. Bezanilla, B. Chanda, Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels. J. Gen. Physiol. 142, 101-112 (2013). doi: 10. 1085/jgp. 201310998; pmid: 23858005
    • (2013) J. Gen. Physiol. , vol.142 , pp. 101-112
    • Capes, D.L.1    Goldschen-Ohm, M.P.2    Arcisio-Miranda, M.3    Bezanilla, F.4    Chanda, B.5
  • 67
    • 0036846886 scopus 로고    scopus 로고
    • Tracking voltage-dependent conformational changes in skeletal muscle sodium channel during activation
    • pmid: 12407076
    • B. Chanda, F. Bezanilla, Tracking voltage-dependent conformational changes in skeletal muscle sodium channel during activation. J. Gen. Physiol. 120, 629-645 (2002). doi: 10. 1085/jgp. 20028679; pmid: 12407076
    • (2002) J. Gen. Physiol. , vol.120 , pp. 629-645
    • Chanda, B.1    Bezanilla, F.2
  • 68
    • 84879190086 scopus 로고    scopus 로고
    • Multiple pore conformations driven by asynchronous movements of voltage sensors in a eukaryotic sodium channel
    • pmid: 23322038
    • M. P. Goldschen-Ohm, D. L. Capes, K. M. Oelstrom, B. Chanda, Multiple pore conformations driven by asynchronous movements of voltage sensors in a eukaryotic sodium channel. Nat. Commun. 4, 1350 (2013). doi: 10. 1038/ ncomms2356; pmid: 23322038
    • (2013) Nat. Commun. , vol.4 , pp. 1350
    • Goldschen-Ohm, M.P.1    Capes, D.L.2    Oelstrom, K.M.3    Chanda, B.4
  • 69
    • 0842326191 scopus 로고    scopus 로고
    • The Na+ channel inactivation gate is a molecular complex: A novel role of the COOH-terminal domain
    • pmid: 14744988
    • H. K. Motoike et al., The Na+ channel inactivation gate is a molecular complex: A novel role of the COOH-terminal domain. J. Gen. Physiol. 123, 155-165 (2004). doi: 10. 1085/ jgp. 200308929; pmid: 14744988
    • (2004) J. Gen. Physiol. , vol.123 , pp. 155-165
    • Motoike, H.K.1
  • 70
    • 33646009667 scopus 로고    scopus 로고
    • Sodium channel inactivation in heart: A novel role of the carboxy-terminal domain
    • pmid: 16686678
    • R. S. Kass, Sodium channel inactivation in heart: A novel role of the carboxy-terminal domain. J. Cardiovasc. Electrophysiol. 17 (suppl. 1), S21-S25 (2006). doi: 10. 1111/ j. 1540-8167. 2006. 00381. x; pmid: 16686678
    • (2006) J. Cardiovasc. Electrophysiol. , vol.17 , pp. S21-S25
    • Kass, R.S.1
  • 71
    • 84950257999 scopus 로고    scopus 로고
    • Structural basis of Nav1. 7 inhibition by an isoform-selective small-molecule antagonist
    • pmid: 26680203
    • S. Ahuja et al., Structural basis of Nav1. 7 inhibition by an isoform-selective small-molecule antagonist. Science 350, aac5464 (2015). doi: 10. 1126/science. aac5464; pmid: 26680203
    • (2015) Science , vol.350 , pp. aac5464
    • Ahuja, S.1
  • 72
    • 0342547301 scopus 로고    scopus 로고
    • A mutation in segment I-S6 alters slow inactivation of sodium channels
    • pmid: 9083667
    • S. Y. Wang, G. K. Wang, A mutation in segment I-S6 alters slow inactivation of sodium channels. Biophys. J. 72, 1633-1640 (1997). doi: 10. 1016/S0006-3495(97)78809-X; pmid: 9083667
    • (1997) Biophys. J. , vol.72 , pp. 1633-1640
    • Wang, S.Y.1    Wang, G.K.2
  • 73
    • 0037144493 scopus 로고    scopus 로고
    • Role of amino acid residues in transmembrane segments IS6 and IIS6 of the Na+ channel alpha subunit in voltage-dependent gating and drug block
    • pmid: 12130650
    • V. Yarov-Yarovoy et al., Role of amino acid residues in transmembrane segments IS6 and IIS6 of the Na+ channel alpha subunit in voltage-dependent gating and drug block. J. Biol. Chem. 277, 35393-35401 (2002). doi: 10. 1074/ jbc. M206126200; pmid: 12130650
    • (2002) J. Biol. Chem. , vol.277 , pp. 35393-35401
    • Yarov-Yarovoy, V.1
  • 74
    • 31444454845 scopus 로고    scopus 로고
    • Neuromodulation of Na+ channel slow inactivation via cAMP-dependent protein kinase and protein kinase C
    • pmid: 16446144
    • Y. Chen, F. H. Yu, D. J. Surmeier, T. Scheuer, W. A. Catterall, Neuromodulation of Na+ channel slow inactivation via cAMP-dependent protein kinase and protein kinase C. Neuron 49, 409-420 (2006). doi: 10. 1016/j. neuron. 2006. 01. 009; pmid: 16446144
    • (2006) Neuron , vol.49 , pp. 409-420
    • Chen, Y.1    Yu, F.H.2    Surmeier, D.J.3    Scheuer, T.4    Catterall, W.A.5
  • 75
    • 27844589940 scopus 로고    scopus 로고
    • Molecular modeling of local anesthetic drug binding by voltage-gated sodium channels
    • pmid: 16174788
    • G. M. Lipkind, H. A. Fozzard, Molecular modeling of local anesthetic drug binding by voltage-gated sodium channels. Mol. Pharmacol. 68, 1611-1622 (2005). pmid: 16174788
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1611-1622
    • Lipkind, G.M.1    Fozzard, H.A.2
  • 76
    • 37849001772 scopus 로고    scopus 로고
    • Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels
    • pmid: 17967784
    • C. A. Ahern, A. L. Eastwood, D. A. Dougherty, R. Horn, Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels. Circ. Res. 102, 86-94 (2008). doi: 10. 1161/ CIRCRESAHA. 107. 160663; pmid: 17967784
    • (2008) Circ. Res. , vol.102 , pp. 86-94
    • Ahern, C.A.1    Eastwood, A.L.2    Dougherty, D.A.3    Horn, R.4
  • 77
    • 0347089037 scopus 로고    scopus 로고
    • Electroporation and RNA interference in the rodent retina in vivo and in vitro
    • pmid: 14603031
    • T. Matsuda, C. L. Cepko, Electroporation and RNA interference in the rodent retina in vivo and in vitro. Proc. Natl. Acad. Sci. U. S. A. 101, 16-22 (2004). doi: 10. 1073/ pnas. 2235688100; pmid: 14603031
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16-22
    • Matsuda, T.1    Cepko, C.L.2
  • 78
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • pmid: 23644547
    • X. Li et al., Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013). doi: 10. 1038/ nmeth. 2472; pmid: 23644547
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 79
    • 84992578098 scopus 로고    scopus 로고
    • Anisotropic correction of beam-induced motion for improved single-particle electron cryo-microscopy
    • S. Zheng, E. Palovcak, J.-P. Armache, Y. Cheng, D. Agard, Anisotropic correction of beam-induced motion for improved single-particle electron cryo-microscopy. bioRxiv, 10. 1101/ 061960 (2016). https: //doi. org/10. 1101/061960
    • (2016) BioRxiv
    • Zheng, S.1    Palovcak, E.2    Armache, J.-P.3    Cheng, Y.4    Agard, D.5
  • 80
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2. 6 Å reconstruction of rotavirus VP6
    • pmid: 26023829
    • T. Grant, N. Grigorieff, Measuring the optimal exposure for single particle cryo-EM using a 2. 6 Å reconstruction of rotavirus VP6. eLife 4, e06980 (2015). doi: 10. 7554/ eLife. 06980; pmid: 26023829
    • (2015) ELife , vol.4 , pp. e06980
    • Grant, T.1    Grigorieff, N.2
  • 81
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: Real-time CTF determination and correction
    • pmid: 26592709
    • K. Zhang, Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1-12 (2016). doi: 10. 1016/ j. jsb. 2015. 11. 003; pmid: 26592709
    • (2016) J. Struct. Biol. , vol.193 , pp. 1-12
    • Zhang, K.1
  • 82
    • 84922727036 scopus 로고    scopus 로고
    • Semi-automated selection of cryo-EM particles in RELION-1. 3
    • pmid: 25486611
    • S. H. Scheres, Semi-automated selection of cryo-EM particles in RELION-1. 3. J. Struct. Biol. 189, 114-122 (2015). doi: 10. 1016/j. jsb. 2014. 11. 010; pmid: 25486611
    • (2015) J. Struct. Biol. , vol.189 , pp. 114-122
    • Scheres, S.H.1
  • 83
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • pmid: 22100448
    • S. H. Scheres, A Bayesian view on cryo-EM structure determination. J. Mol. Biol. 415, 406-418 (2012). doi: 10. 1016/j. jmb. 2011. 11. 010; pmid: 22100448
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.1
  • 84
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • pmid: 23000701
    • S. H. Scheres, RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012). doi: 10. 1016/j. jsb. 2012. 09. 006; pmid: 23000701
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 85
    • 85009208040 scopus 로고    scopus 로고
    • Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
    • 10. 7554/eLife. 18722 pmid: 27845625
    • D. Kimanius, B. O. Forsberg, S. H. Scheres, E. Lindahl, Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2. eLife 5, 10. 7554/ eLife. 18722 (2016). doi: 10. 7554/eLife. 18722; pmid: 27845625
    • (2016) ELife , vol.5
    • Kimanius, D.1    Forsberg, B.O.2    Scheres, S.H.3    Lindahl, E.4
  • 86
    • 84946481951 scopus 로고    scopus 로고
    • Automatic estimation and correction of anisotropic magnification distortion in electron microscopes
    • pmid: 26278979
    • T. Grant, N. Grigorieff, Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J. Struct. Biol. 192, 204-208 (2015). doi: 10. 1016/j. jsb. 2015. 08. 006; pmid: 26278979
    • (2015) J. Struct. Biol. , vol.192 , pp. 204-208
    • Grant, T.1    Grigorieff, N.2
  • 87
    • 84969961924 scopus 로고    scopus 로고
    • Structural insights into the Niemann-Pick C1 (NPC1)-mediated cholesterol transfer and Ebola infection
    • pmid: 27238017
    • X. Gong et al., Structural insights into the Niemann-Pick C1 (NPC1)-mediated cholesterol transfer and Ebola infection. Cell 165, 1467-1478 (2016). doi: 10. 1016/j. cell. 2016. 05. 022; pmid: 27238017
    • (2016) Cell , vol.165 , pp. 1467-1478
    • Gong, X.1
  • 88
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • pmid: 14568533
    • P. B. Rosenthal, R. Henderson, Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003). doi: 10. 1016/j. jmb. 2003. 07. 013; pmid: 14568533
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 89
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • pmid: 23872039
    • S. Chen et al., High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013). doi: 10. 1016/ j. ultramic. 2013. 06. 004; pmid: 23872039
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 90
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • N. Stein, CHAINSAW: A program for mutating pdb files used as templates in molecular replacement. J. Appl. Cryst. 41, 641-643 (2008). doi: 10. 1107/S0021889808006985
    • (2008) J. Appl. Cryst. , vol.41 , pp. 641-643
    • Stein, N.1
  • 92
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • pmid: 20124702
    • P. D. Adams et al., PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010). doi: 10. 1107/S0907444909052925; pmid: 20124702
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 93
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • pmid: 21460454
    • G. N. Murshudov et al., REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011). doi: 10. 1107/ S0907444911001314; pmid: 21460454
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 94
    • 84907007915 scopus 로고    scopus 로고
    • Conformation-independent structural comparison of macromolecules with ProSMART
    • pmid: 25195761
    • R. A. Nicholls, M. Fischer, S. McNicholas, G. N. Murshudov, Conformation-independent structural comparison of macromolecules with ProSMART. Acta Crystallogr. D Biol. Crystallogr. 70, 2487-2499 (2014). doi: 10. 1107/ S1399004714016241; pmid: 25195761
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 2487-2499
    • Nicholls, R.A.1    Fischer, M.2    McNicholas, S.3    Murshudov, G.N.4
  • 95
    • 84897000112 scopus 로고    scopus 로고
    • Structure of the yeast mitochondrial large ribosomal subunit
    • pmid: 24675956
    • A. Amunts et al., Structure of the yeast mitochondrial large ribosomal subunit. Science 343, 1485-1489 (2014). doi: 10. 1126/science. 1249410; pmid: 24675956
    • (2014) Science , vol.343 , pp. 1485-1489
    • Amunts, A.1
  • 96
    • 57049150788 scopus 로고    scopus 로고
    • The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures
    • Database pmid: 18971256
    • O. Goldenberg, E. Erez, G. Nimrod, N. Ben-Tal, The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures. Nucleic Acids Res. 37 (Database), D323-D327 (2009). doi: 10. 1093/nar/gkn822; pmid: 18971256
    • (2009) Nucleic Acids Res. , vol.37 , pp. D323-D327
    • Goldenberg, O.1    Erez, E.2    Nimrod, G.3    Ben-Tal, N.4
  • 97
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • pmid: 15264254
    • E. F. Pettersen et al., UCSF Chimera-A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004). doi: 10. 1002/jcc. 20084; pmid: 15264254
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 99
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • 376 pmid: 9195488
    • O. S. Smart, J. G. Neduvelil, X. Wang, B. A. Wallace, M. S. Sansom, HOLE: A program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354-360, 376 (1996). doi: 10. 1016/S0263-7855(97)00009-X; pmid: 9195488
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 100
    • 84904815625 scopus 로고    scopus 로고
    • SWISS-MODEL: Modelling protein tertiary and quaternary structure using evolutionary information
    • pmid: 24782522
    • M. Biasini et al., SWISS-MODEL: Modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42 (W1), W252-W258 (2014). doi: 10. 1093/nar/gku340; pmid: 24782522
    • (2014) Nucleic Acids Res. , vol.42 , Issue.W1 , pp. W252-W258
    • Biasini, M.1
  • 101
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • pmid: 16301204
    • K. Arnold, L. Bordoli, J. Kopp, T. Schwede, The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201 (2006). doi: 10. 1093/bioinformatics/bti770; pmid: 16301204
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 102
    • 69249212321 scopus 로고    scopus 로고
    • Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective
    • N. Guex, M. C. Peitsch, T. Schwede, Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective. Electrophoresis 30 (suppl. 1), S162-S173 (2009). doi: 10. 1002/ elps. 200900140; pmid: 19517507
    • (2009) Electrophoresis , vol.30 , pp. S162-S173
    • Guex, N.1    Peitsch, M.C.2    Schwede, T.3
  • 103
    • 58149193233 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository and associated resources
    • Database pmid: 18931379
    • F. Kiefer, K. Arnold, M. Künzli, L. Bordoli, T. Schwede, The SWISS-MODEL Repository and associated resources. Nucleic Acids Res. 37 (Database), D387-D392 (2009). doi: 10. 1093/ nar/gkn750; pmid: 18931379
    • (2009) Nucleic Acids Res. , vol.37 , pp. D387-D392
    • Kiefer, F.1    Arnold, K.2    Künzli, M.3    Bordoli, L.4    Schwede, T.5
  • 104
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • pmid: 9757107
    • A. T. Brünger et al., Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998). doi: 10. 1107/S0907444998003254; pmid: 9757107
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 105
    • 37049014272 scopus 로고    scopus 로고
    • Version 1. 2 of the crystallography and NMR system
    • pmid: 18007608
    • A. T. Brunger, Version 1. 2 of the crystallography and NMR system. Nat. Protoc. 2, 2728-2733 (2007). doi: 10. 1038/ nprot. 2007. 406; pmid: 18007608
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


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