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Volumn 72, Issue 19, 2015, Pages 3677-3693

Structure of potassium channels

Author keywords

Conductivity; Gating; RCK; Selectivity; Sensor domain

Indexed keywords

DIMER; GUANINE NUCLEOTIDE BINDING PROTEIN; INWARDLY RECTIFYING POTASSIUM CHANNEL; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR2.2; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR3.1; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR3.2; LIGAND GATED POTASSIUM CHANNEL; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; POTASSIUM CHANNEL; POTASSIUM ION; POTASSIUM PROTON EXCHANGE PROTEIN; PROTEIN TYROSINE KINASE A; TANDEM PORE DOMAIN POTASSIUM CHANNEL; TWIK RELATED ARACHIDONIC ACID ACTIVATED POTASSIUM CHANNEL; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84941421455     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-1948-5     Document Type: Review
Times cited : (209)

References (134)
  • 1
    • 22244458104 scopus 로고    scopus 로고
    • Prokaryotic K(+) channels: From crystal structures to diversity
    • 10.1016/j.femsre.2005.03.003 1:CAS:528:DC%2BD2MXhtFSisLnE
    • Kuo MM, Haynes WJ, Loukin SH, Kung C, Saimi Y (2005) Prokaryotic K(+) channels: from crystal structures to diversity. FEMS Microbiol Rev 29(5):961-985. doi: 10.1016/j.femsre.2005.03.003
    • (2005) FEMS Microbiol Rev , vol.29 , Issue.5 , pp. 961-985
    • Kuo, M.M.1    Haynes, W.J.2    Loukin, S.H.3    Kung, C.4    Saimi, Y.5
  • 3
    • 77951079450 scopus 로고    scopus 로고
    • + channels
    • 10.1152/physrev.00020.2009 1:CAS:528:DC%2BC3cXht1erurnF
    • + channels. Physiol Rev 90(2):755-796. doi: 10.1152/physrev.00020.2009
    • (2010) Physiol Rev , vol.90 , Issue.2 , pp. 755-796
    • Pongs, O.1    Schwarz, J.R.2
  • 4
    • 74949143771 scopus 로고    scopus 로고
    • Inwardly rectifying potassium channels: Their structure, function, and physiological roles
    • 10.1152/physrev.00021.2009 1:CAS:528:DC%2BC3cXitFGgsLk%3D
    • Hibino H, Inanobe A, Furutani K, Murakami S, Findlay I, Kurachi Y (2010) Inwardly rectifying potassium channels: their structure, function, and physiological roles. Physiol Rev 90(1):291-366. doi: 10.1152/physrev.00021.2009
    • (2010) Physiol Rev , vol.90 , Issue.1 , pp. 291-366
    • Hibino, H.1    Inanobe, A.2    Furutani, K.3    Murakami, S.4    Findlay, I.5    Kurachi, Y.6
  • 5
    • 77951041210 scopus 로고    scopus 로고
    • + currents: Two-pore domain potassium channels
    • 10.1152/physrev.00029.2009 1:CAS:528:DC%2BC3cXht1erurnO
    • + currents: two-pore domain potassium channels. Physiol Rev 90(2):559-605. doi: 10.1152/physrev.00029.2009
    • (2010) Physiol Rev , vol.90 , Issue.2 , pp. 559-605
    • Enyedi, P.1    Czirjak, G.2
  • 6
    • 84908363276 scopus 로고    scopus 로고
    • Regulation of BK channels by auxiliary gamma subunits
    • 10.3389/fphys.2014.00401
    • Zhang J, Yan J (2014) Regulation of BK channels by auxiliary gamma subunits. Front Physiol 5:401. doi: 10.3389/fphys.2014.00401
    • (2014) Front Physiol , vol.5 , pp. 401
    • Zhang, J.1    Yan, J.2
  • 7
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • 10.1016/S0014-5793(03)01104-9 1:CAS:528:DC%2BD3sXptVWgtbo%3D
    • MacKinnon R (2003) Potassium channels. FEBS Lett 555(1):62-65. doi: 10.1016/S0014-5793(03)01104-9
    • (2003) FEBS Lett , vol.555 , Issue.1 , pp. 62-65
    • MacKinnon, R.1
  • 10
    • 0035499447 scopus 로고    scopus 로고
    • + selectivity filter
    • 10.1038/35102000 1:STN:280:DC%2BD3MnktVWmuw%3D%3D
    • + selectivity filter. Nature 414(6859):37-42. doi: 10.1038/35102000
    • (2001) Nature , vol.414 , Issue.6859 , pp. 37-42
    • Morais-Cabral, J.H.1    Zhou, Y.2    MacKinnon, R.3
  • 11
    • 0035499892 scopus 로고    scopus 로고
    • + channel-Fab complex at 2.0 A resolution
    • 10.1038/35102009 1:CAS:528:DC%2BD3MXot1Wqsbg%3D
    • + channel-Fab complex at 2.0 A resolution. Nature 414(6859):43-48. doi: 10.1038/35102009
    • (2001) Nature , vol.414 , Issue.6859 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 13
    • 79956123183 scopus 로고    scopus 로고
    • Structural studies of ion selectivity in tetrameric cation channels
    • 10.1085/jgp.201010546 1:CAS:528:DC%2BC3MXntlygsLc%3D
    • Alam A, Jiang Y (2011) Structural studies of ion selectivity in tetrameric cation channels. J Gen Physiol 137(5):397-403. doi: 10.1085/jgp.201010546
    • (2011) J Gen Physiol , vol.137 , Issue.5 , pp. 397-403
    • Alam, A.1    Jiang, Y.2
  • 14
    • 71449094441 scopus 로고    scopus 로고
    • Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore
    • 10.1038/nsmb.1703 1:CAS:528:DC%2BD1MXhsVylsb%2FO
    • Thompson AN, Kim I, Panosian TD, Iverson TM, Allen TW, Nimigean CM (2009) Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore. Nat Struct Mol Biol 16(12):1317-1324. doi: 10.1038/nsmb.1703
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.12 , pp. 1317-1324
    • Thompson, A.N.1    Kim, I.2    Panosian, T.D.3    Iverson, T.M.4    Allen, T.W.5    Nimigean, C.M.6
  • 15
    • 0142185496 scopus 로고    scopus 로고
    • + selectivity filter: Charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates
    • 10.1016/j.jmb.2003.09.022 1:CAS:528:DC%2BD3sXosVygu7s%3D
    • + selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates. J Mol Biol 333(5):965-975. doi: 10.1016/j.jmb.2003.09.022
    • (2003) J Mol Biol , vol.333 , Issue.5 , pp. 965-975
    • Zhou, Y.1    MacKinnon, R.2
  • 16
    • 1942425489 scopus 로고    scopus 로고
    • A mutant KcsA K(+) channel with altered conduction properties and selectivity filter ion distribution
    • 10.1016/j.jmb.2004.03.020 1:CAS:528:DC%2BD2cXjtFOgsrw%3D
    • Zhou M, MacKinnon R (2004) A mutant KcsA K(+) channel with altered conduction properties and selectivity filter ion distribution. J Mol Biol 338(4):839-846. doi: 10.1016/j.jmb.2004.03.020
    • (2004) J Mol Biol , vol.338 , Issue.4 , pp. 839-846
    • Zhou, M.1    MacKinnon, R.2
  • 17
    • 79958031754 scopus 로고    scopus 로고
    • + -channels
    • 10.1016/j.jmb.2011.04.043 1:CAS:528:DC%2BC3MXntFSrtb4%3D
    • + -channels. J Mol Biol 409(5):867-878. doi: 10.1016/j.jmb.2011.04.043
    • (2011) J Mol Biol , vol.409 , Issue.5 , pp. 867-878
    • Furini, S.1    Domene, C.2
  • 20
    • 33750968787 scopus 로고    scopus 로고
    • + channel locked in the conductive conformation
    • 10.1126/science.1133415 1:CAS:528:DC%2BD28XhtFyqtLjL
    • + channel locked in the conductive conformation. Science 314(5801):1004-1007. doi: 10.1126/science.1133415
    • (2006) Science , vol.314 , Issue.5801 , pp. 1004-1007
    • Valiyaveetil, F.I.1    Leonetti, M.2    Muir, T.W.3    MacKinnon, R.4
  • 21
    • 33745041507 scopus 로고    scopus 로고
    • Molecular determinants of gating at the potassium-channel selectivity filter
    • 10.1038/nsmb1069 1:CAS:528:DC%2BD28Xjs1Ort70%3D
    • Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E (2006) Molecular determinants of gating at the potassium-channel selectivity filter. Nat Struct Mol Biol 13(4):311-318. doi: 10.1038/nsmb1069
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.4 , pp. 311-318
    • Cordero-Morales, J.F.1    Cuello, L.G.2    Zhao, Y.3    Jogini, V.4    Cortes, D.M.5    Roux, B.6    Perozo, E.7
  • 22
    • 79955124042 scopus 로고    scopus 로고
    • Mechanism for selectivity-inactivation coupling in KcsA potassium channels
    • 10.1073/pnas.1014186108 1:CAS:528:DC%2BC3MXkslOmtL8%3D
    • Cheng WW, McCoy JG, Thompson AN, Nichols CG, Nimigean CM (2011) Mechanism for selectivity-inactivation coupling in KcsA potassium channels. Proc Natl Acad Sci USA 108(13):5272-5277. doi: 10.1073/pnas.1014186108
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.13 , pp. 5272-5277
    • Cheng, W.W.1    McCoy, J.G.2    Thompson, A.N.3    Nichols, C.G.4    Nimigean, C.M.5
  • 23
    • 84857539138 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the TrkH membrane protein
    • 10.1021/bi201586n 1:CAS:528:DC%2BC38XhvFKmtr0%3D
    • Domene C, Furini S (2012) Molecular dynamics simulations of the TrkH membrane protein. Biochemistry 51(8):1559-1565. doi: 10.1021/bi201586n
    • (2012) Biochemistry , vol.51 , Issue.8 , pp. 1559-1565
    • Domene, C.1    Furini, S.2
  • 24
    • 77955423895 scopus 로고    scopus 로고
    • + channel pore
    • 10.1038/nsmb.1865 1:CAS:528:DC%2BC3cXpsFWltbs%3D
    • + channel pore. Nat Struct Mol Biol 17(8):1019-1023. doi: 10.1038/nsmb.1865
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.8 , pp. 1019-1023
    • Ye, S.1    Li, Y.2    Jiang, Y.3
  • 25
    • 70349602525 scopus 로고    scopus 로고
    • Atypical mechanism of conduction in potassium channels
    • 10.1073/pnas.0903226106 1:CAS:528:DC%2BD1MXht1OjsbjP
    • Furini S, Domene C (2009) Atypical mechanism of conduction in potassium channels. Proc Natl Acad Sci USA 106(38):16074-16077. doi: 10.1073/pnas.0903226106
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.38 , pp. 16074-16077
    • Furini, S.1    Domene, C.2
  • 27
    • 79551660280 scopus 로고    scopus 로고
    • Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites
    • 10.1073/pnas.1013636108 1:CAS:528:DC%2BC3MXosFeltw%3D%3D
    • Derebe MG, Sauer DB, Zeng W, Alam A, Shi N, Jiang Y (2011) Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites. Proc Natl Acad Sci USA 108(2):598-602. doi: 10.1073/pnas.1013636108
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.2 , pp. 598-602
    • Derebe, M.G.1    Sauer, D.B.2    Zeng, W.3    Alam, A.4    Shi, N.5    Jiang, Y.6
  • 29
    • 0033516590 scopus 로고    scopus 로고
    • + channel: Electrostatic stabilization of monovalent cations
    • 10.1126/science.285.5424.100 1:CAS:528:DyaK1MXksVCqt7o%3D
    • + channel: electrostatic stabilization of monovalent cations. Science 285(5424):100-102. doi: 10.1126/science.285.5424.100
    • (1999) Science , vol.285 , Issue.5424 , pp. 100-102
    • Roux, B.1    MacKinnon, R.2
  • 30
    • 38149012053 scopus 로고    scopus 로고
    • Role of the intracellular cavity in potassium channel conductivity
    • 10.1021/jp0747813 1:CAS:528:DC%2BD2sXhtlaktb%2FI
    • Furini S, Zerbetto F, Cavalcanti S (2007) Role of the intracellular cavity in potassium channel conductivity. J Phys Chem B 111(50):13993-14000. doi: 10.1021/jp0747813
    • (2007) J Phys Chem B , vol.111 , Issue.50 , pp. 13993-14000
    • Furini, S.1    Zerbetto, F.2    Cavalcanti, S.3
  • 32
    • 77950913923 scopus 로고    scopus 로고
    • Structural basis underlying the dual gate properties of KcsA
    • 10.1073/pnas.0911270107 1:CAS:528:DC%2BC3cXkslynur8%3D
    • Imai S, Osawa M, Takeuchi K, Shimada I (2010) Structural basis underlying the dual gate properties of KcsA. Proc Natl Acad Sci USA 107(14):6216-6221. doi: 10.1073/pnas.0911270107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.14 , pp. 6216-6221
    • Imai, S.1    Osawa, M.2    Takeuchi, K.3    Shimada, I.4
  • 33
    • 58149262941 scopus 로고    scopus 로고
    • + channel gates underlies distinct roles in electrical signaling
    • 10.1038/nsmb.1525 1:CAS:528:DC%2BD1cXhsFajtbfI
    • + channel gates underlies distinct roles in electrical signaling. Nat Struct Mol Biol 16(1):71-79. doi: 10.1038/nsmb.1525
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.1 , pp. 71-79
    • Ben-Abu, Y.1    Zhou, Y.2    Zilberberg, N.3    Yifrach, O.4
  • 36
    • 84855467714 scopus 로고    scopus 로고
    • Structural correlates of selectivity and inactivation in potassium channels
    • 10.1016/j.bbamem.2011.09.007
    • McCoy JG, Nimigean CM (2012) Structural correlates of selectivity and inactivation in potassium channels. Biochim Biophys Acta 2:272-285. doi: 10.1016/j.bbamem.2011.09.007
    • (2012) Biochim Biophys Acta , vol.2 , pp. 272-285
    • McCoy, J.G.1    Nimigean, C.M.2
  • 37
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • 10.1038/nature12823 1:CAS:528:DC%2BC3sXhvVyisL%2FI
    • Cao E, Liao M, Cheng Y, Julius D (2013) TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504(7478):113-118. doi: 10.1038/nature12823
    • (2013) Nature , vol.504 , Issue.7478 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 38
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • 10.1038/417523a 1:CAS:528:DC%2BD38XktVeht7k%3D
    • Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (2002) The open pore conformation of potassium channels. Nature 417(6888):523-526. doi: 10.1038/417523a
    • (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
  • 39
    • 33751192493 scopus 로고    scopus 로고
    • How does voltage open an ion channel?
    • 10.1146/annurev.cellbio.21.020404.145837 1:CAS:528:DC%2BD28Xht1yjs7rF
    • Tombola F, Pathak MM, Isacoff EY (2006) How does voltage open an ion channel? Annu Rev Cell Dev Biol 22:23-52. doi: 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
  • 40
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • 10.1126/science.1116270 1:CAS:528:DC%2BD2MXmvFSks7s%3D
    • Long SB, Campbell EB, Mackinnon R (2005) Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309(5736):903-908. doi: 10.1126/science.1116270
    • (2005) Science , vol.309 , Issue.5736 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 41
    • 78650973241 scopus 로고    scopus 로고
    • Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel
    • 10.1038/nsmb.1966
    • Wang DT, Hill AP, Mann SA, Tan PS, Vandenberg JI (2011) Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel. Nat Struct Mol Biol 18(1):35-41. doi: 10.1038/nsmb.1966
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.1 , pp. 35-41
    • Wang, D.T.1    Hill, A.P.2    Mann, S.A.3    Tan, P.S.4    Vandenberg, J.I.5
  • 42
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • 10.1038/35079500 1:CAS:528:DC%2BD3MXksFOqs7o%3D
    • Zhou M, Morais-Cabral JH, Mann S, MacKinnon R (2001) Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature 411(6838):657-661. doi: 10.1038/35079500
    • (2001) Nature , vol.411 , Issue.6838 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 43
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • 10.1126/science.2122519 1:CAS:528:DyaK3cXmt1Cls70%3D
    • Hoshi T, Zagotta WN, Aldrich RW (1990) Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250(4980):533-538. doi: 10.1126/science.2122519
    • (1990) Science , vol.250 , Issue.4980 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 44
    • 80054974935 scopus 로고    scopus 로고
    • Electrostatic interaction between inactivation ball and T1-S1 linker region of Kv1.4 channel
    • 10.1016/j.bbamem.2011.09.028 1:CAS:528:DC%2BC3MXhsFOhu77L
    • Fan Z, Ji X, Fu M, Zhang W, Zhang D, Xiao Z (2012) Electrostatic interaction between inactivation ball and T1-S1 linker region of Kv1.4 channel. Biochim Biophys Acta 1818(1):55-63. doi: 10.1016/j.bbamem.2011.09.028
    • (2012) Biochim Biophys Acta , vol.1818 , Issue.1 , pp. 55-63
    • Fan, Z.1    Ji, X.2    Fu, M.3    Zhang, W.4    Zhang, D.5    Xiao, Z.6
  • 45
    • 77954485089 scopus 로고    scopus 로고
    • Structural mechanism of C-type inactivation in K(+) channels
    • 10.1038/nature09153 1:CAS:528:DC%2BC3cXosVKhsbc%3D
    • Cuello LG, Jogini V, Cortes DM, Perozo E (2010) Structural mechanism of C-type inactivation in K(+) channels. Nature 466(7303):203-208. doi: 10.1038/nature09153
    • (2010) Nature , vol.466 , Issue.7303 , pp. 203-208
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Perozo, E.4
  • 46
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • 10.1038/nature00978 1:CAS:528:DC%2BD38Xmslahtbs%3D
    • Yellen G (2002) The voltage-gated potassium channels and their relatives. Nature 419(6902):35-42. doi: 10.1038/nature00978
    • (2002) Nature , vol.419 , Issue.6902 , pp. 35-42
    • Yellen, G.1
  • 48
    • 41449090448 scopus 로고    scopus 로고
    • Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening
    • 10.1529/biophysj.107.117507 1:CAS:528:DC%2BD1cXit1yqtb8%3D
    • Marius P, Zagnoni M, Sandison ME, East JM, Morgan H, Lee AG (2008) Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening. Biophys J 94(5):1689-1698. doi: 10.1529/biophysj.107.117507
    • (2008) Biophys J , vol.94 , Issue.5 , pp. 1689-1698
    • Marius, P.1    Zagnoni, M.2    Sandison, M.E.3    East, J.M.4    Morgan, H.5    Lee, A.G.6
  • 49
    • 0032031204 scopus 로고    scopus 로고
    • Voltage-gated ion channels and electrical excitability
    • 10.1016/S0896-6273(00)80981-2 1:CAS:528:DyaK1cXit1Gmsro%3D
    • Armstrong CM, Hille B (1998) Voltage-gated ion channels and electrical excitability. Neuron 20(3):371-380. doi: 10.1016/S0896-6273(00)80981-2
    • (1998) Neuron , vol.20 , Issue.3 , pp. 371-380
    • Armstrong, C.M.1    Hille, B.2
  • 50
    • 34248995257 scopus 로고    scopus 로고
    • The action potential in mammalian central neurons
    • 10.1038/nrn2148 1:CAS:528:DC%2BD2sXlsVSktb0%3D
    • Bean BP (2007) The action potential in mammalian central neurons. Nat Rev Neurosci 8(6):451-465. doi: 10.1038/nrn2148
    • (2007) Nat Rev Neurosci , vol.8 , Issue.6 , pp. 451-465
    • Bean, B.P.1
  • 51
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • 10.1113/jphysiol.1952.sp004764 1:STN:280:DyaG3s%2FhsFGjug%3D%3D
    • Hodgkin AL, Huxley AF (1952) A quantitative description of membrane current and its application to conduction and excitation in nerve. J Physiol 117(4):500-544. doi: 10.1113/jphysiol.1952.sp004764
    • (1952) J Physiol , vol.117 , Issue.4 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 52
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • 10.1038/nature07620 1:CAS:528:DC%2BD1cXhsFWmsLnE
    • Swartz KJ (2008) Sensing voltage across lipid membranes. Nature 456(7224):891-897. doi: 10.1038/nature07620
    • (2008) Nature , vol.456 , Issue.7224 , pp. 891-897
    • Swartz, K.J.1
  • 53
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • 10.1038/nature06265 1:CAS:528:DC%2BD2sXhtlajs7%2FN
    • + channel in a lipid membrane-like environment. Nature 450(7168):376-382. doi: 10.1038/nature06265
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 54
    • 23244456428 scopus 로고    scopus 로고
    • + channel
    • 10.1126/science.1116269 1:CAS:528:DC%2BD2MXmvFSks7o%3D
    • + channel. Science 309(5736):897-903. doi: 10.1126/science.1116269
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 55
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • 10.1038/35101535 1:CAS:528:DC%2BD3MXotFyksbo%3D
    • Lu Z, Klem AM, Ramu Y (2001) Ion conduction pore is conserved among potassium channels. Nature 413(6858):809-813. doi: 10.1038/35101535
    • (2001) Nature , vol.413 , Issue.6858 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 56
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • 10.1038/nature06266 1:CAS:528:DC%2BD2sXhtlajs77F
    • Alabi AA, Bahamonde MI, Jung HJ, Kim JI, Swartz KJ (2007) Portability of paddle motif function and pharmacology in voltage sensors. Nature 450(7168):370-375. doi: 10.1038/nature06266
    • (2007) Nature , vol.450 , Issue.7168 , pp. 370-375
    • Alabi, A.A.1    Bahamonde, M.I.2    Jung, H.J.3    Kim, J.I.4    Swartz, K.J.5
  • 57
    • 77955626630 scopus 로고    scopus 로고
    • + channel with a miniature engineered voltage sensor
    • 10.1016/j.cell.2010.07.013 1:CAS:528:DC%2BC3cXhtVKhurzP
    • + channel with a miniature engineered voltage sensor. Cell 142(4):580-589. doi: 10.1016/j.cell.2010.07.013
    • (2010) Cell , vol.142 , Issue.4 , pp. 580-589
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 58
    • 78049359992 scopus 로고    scopus 로고
    • Signaling complexes of voltage-gated sodium and calcium channels
    • 10.1016/j.neulet.2010.08.085 1:CAS:528:DC%2BC3cXhtlens7nP
    • Catterall WA (2010) Signaling complexes of voltage-gated sodium and calcium channels. Neurosci Lett 486(2):107-116. doi: 10.1016/j.neulet.2010.08.085
    • (2010) Neurosci Lett , vol.486 , Issue.2 , pp. 107-116
    • Catterall, W.A.1
  • 59
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • 10.1126/science.1122352 1:CAS:528:DC%2BD28XjvVGktbg%3D
    • Sasaki M, Takagi M, Okamura Y (2006) A voltage sensor-domain protein is a voltage-gated proton channel. Science 312(5773):589-592. doi: 10.1126/science.1122352
    • (2006) Science , vol.312 , Issue.5773 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 60
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • 10.1038/nature04700 1:CAS:528:DC%2BD28XjvVGltb0%3D
    • Ramsey IS, Moran MM, Chong JA, Clapham DE (2006) A voltage-gated proton-selective channel lacking the pore domain. Nature 440(7088):1213-1216. doi: 10.1038/nature04700
    • (2006) Nature , vol.440 , Issue.7088 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 61
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • 10.1038/nature03650 1:CAS:528:DC%2BD2MXls1OntLc%3D
    • Murata Y, Iwasaki H, Sasaki M, Inaba K, Okamura Y (2005) Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435(7046):1239-1243. doi: 10.1038/nature03650
    • (2005) Nature , vol.435 , Issue.7046 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 62
    • 40349085541 scopus 로고    scopus 로고
    • Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel
    • 10.1073/pnas.0711533105 1:CAS:528:DC%2BD1cXhvFCit7Y%3D
    • Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH (2008) Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel. Proc Natl Acad Sci USA 105(5):1511-1515. doi: 10.1073/pnas.0711533105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.5 , pp. 1511-1515
    • Clayton, G.M.1    Altieri, S.2    Heginbotham, L.3    Unger, V.M.4    Morais-Cabral, J.H.5
  • 63
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement
    • 10.1073/pnas.1000142107 1:CAS:528:DC%2BC3cXot1ekt70%3D
    • Chen X, Wang Q, Ni F, Ma J (2010) Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement. Proc Natl Acad Sci USA 107(25):11352-11357. doi: 10.1073/pnas.1000142107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.25 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ni, F.3    Ma, J.4
  • 64
    • 27344442574 scopus 로고    scopus 로고
    • + channel and its dependence on the lipid membrane
    • 10.1073/pnas.0507651102 1:CAS:528:DC%2BD2MXht1ShtrvI
    • + channel and its dependence on the lipid membrane. Proc Natl Acad Sci USA 102(43):15441-15446. doi: 10.1073/pnas.0507651102
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.43 , pp. 15441-15446
    • Lee, S.Y.1    Lee, A.2    Chen, J.3    MacKinnon, R.4
  • 65
    • 66149157329 scopus 로고    scopus 로고
    • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels
    • 10.1371/journal.pbio.1000047
    • Lee SY, Banerjee A, MacKinnon R (2009) Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels. PLoS Biol 7(3):e47. doi: 10.1371/journal.pbio.1000047
    • (2009) PLoS Biol , vol.7 , Issue.3 , pp. e47
    • Lee, S.Y.1    Banerjee, A.2    MacKinnon, R.3
  • 66
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • 10.1016/S0896-6273(00)80143-9 1:CAS:528:DyaK28XjvFaks7c%3D
    • + channel. Neuron 16(6):1169-1177. doi: 10.1016/S0896-6273(00)80143-9
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 68
    • 46149091062 scopus 로고    scopus 로고
    • + channels
    • 10.1016/j.neuron.2008.05.006 1:CAS:528:DC%2BD1cXoslyjurk%3D
    • + channels. Neuron 59(1):98-109. doi: 10.1016/j.neuron.2008.05.006
    • (2008) Neuron , vol.59 , Issue.1 , pp. 98-109
    • Posson, D.J.1    Selvin, P.R.2
  • 69
    • 34748848687 scopus 로고    scopus 로고
    • Closing in on the resting state of the Shaker K(+) channel
    • 10.1016/j.neuron.2007.09.023 1:CAS:528:DC%2BD2sXht1WksrzI
    • Pathak MM, Yarov-Yarovoy V, Agarwal G, Roux B, Barth P, Kohout S, Tombola F, Isacoff EY (2007) Closing in on the resting state of the Shaker K(+) channel. Neuron 56(1):124-140. doi: 10.1016/j.neuron.2007.09.023
    • (2007) Neuron , vol.56 , Issue.1 , pp. 124-140
    • Pathak, M.M.1    Yarov-Yarovoy, V.2    Agarwal, G.3    Roux, B.4    Barth, P.5    Kohout, S.6    Tombola, F.7    Isacoff, E.Y.8
  • 70
    • 77957924708 scopus 로고    scopus 로고
    • Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP
    • 10.1016/j.jmb.2010.09.012 1:CAS:528:DC%2BC3cXhtlShurnO
    • Butterwick JA, MacKinnon R (2010) Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP. J Mol Biol 403(4):591-606. doi: 10.1016/j.jmb.2010.09.012
    • (2010) J Mol Biol , vol.403 , Issue.4 , pp. 591-606
    • Butterwick, J.A.1    MacKinnon, R.2
  • 71
    • 33748103925 scopus 로고    scopus 로고
    • + channel from Listeria monocytogenes
    • 10.1085/jgp.200609572 1:CAS:528:DC%2BD28XhtVWksr%2FJ
    • + channel from Listeria monocytogenes. J Gen Physiol 128(3):283-292. doi: 10.1085/jgp.200609572
    • (2006) J Gen Physiol , vol.128 , Issue.3 , pp. 283-292
    • Santos, J.S.1    Lundby, A.2    Zazueta, C.3    Montal, M.4
  • 72
    • 11144221751 scopus 로고    scopus 로고
    • Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment
    • 10.1073/pnas.0408270101 1:CAS:528:DC%2BD2MXjtVSlsg%3D%3D
    • Zhao Y, Scheuer T, Catterall WA (2004) Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment. Proc Natl Acad Sci USA 101(51):17873-17878. doi: 10.1073/pnas.0408270101
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.51 , pp. 17873-17878
    • Zhao, Y.1    Scheuer, T.2    Catterall, W.A.3
  • 73
    • 0037381334 scopus 로고    scopus 로고
    • Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel
    • 10.1038/nn1028 1:CAS:528:DC%2BD3sXitlequ7s%3D
    • Sesti F, Rajan S, Gonzalez-Colaso R, Nikolaeva N, Goldstein SA (2003) Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal voltage-gated potassium channel. Nat Neurosci 6(4):353-361. doi: 10.1038/nn1028
    • (2003) Nat Neurosci , vol.6 , Issue.4 , pp. 353-361
    • Sesti, F.1    Rajan, S.2    Gonzalez-Colaso, R.3    Nikolaeva, N.4    Goldstein, S.A.5
  • 74
    • 13244272072 scopus 로고    scopus 로고
    • Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores
    • 10.1016/j.neuron.2004.12.047 1:CAS:528:DC%2BD2MXhs1Wntr8%3D
    • Tombola F, Pathak MM, Isacoff EY (2005) Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores. Neuron 45(3):379-388. doi: 10.1016/j.neuron.2004.12.047
    • (2005) Neuron , vol.45 , Issue.3 , pp. 379-388
    • Tombola, F.1    Pathak, M.M.2    Isacoff, E.Y.3
  • 75
    • 22544439334 scopus 로고    scopus 로고
    • Ion permeation through a voltage- sensitive gating pore in brain sodium channels having voltage sensor mutations
    • 10.1016/j.neuron.2005.06.012 1:CAS:528:DC%2BD2MXntVSmsb0%3D
    • Sokolov S, Scheuer T, Catterall WA (2005) Ion permeation through a voltage- sensitive gating pore in brain sodium channels having voltage sensor mutations. Neuron 47(2):183-189. doi: 10.1016/j.neuron.2005.06.012
    • (2005) Neuron , vol.47 , Issue.2 , pp. 183-189
    • Sokolov, S.1    Scheuer, T.2    Catterall, W.A.3
  • 76
    • 0035039731 scopus 로고    scopus 로고
    • + channel
    • 10.1085/jgp.117.5.469 1:CAS:528:DC%2BD3MXktVaktbc%3D
    • + channel. J Gen Physiol 117(5):469-490. doi: 10.1085/jgp.117.5.469
    • (2001) J Gen Physiol , vol.117 , Issue.5 , pp. 469-490
    • Starace, D.M.1    Bezanilla, F.2
  • 77
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • 10.1038/nature02270 1:CAS:528:DC%2BD2cXpsFWgsg%3D%3D
    • Starace DM, Bezanilla F (2004) A proton pore in a potassium channel voltage sensor reveals a focused electric field. Nature 427(6974):548-553. doi: 10.1038/nature02270
    • (2004) Nature , vol.427 , Issue.6974 , pp. 548-553
    • Starace, D.M.1    Bezanilla, F.2
  • 78
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • 10.1016/j.neuron.2010.08.021 1:CAS:528:DC%2BC3cXht1Wisr3P
    • Catterall WA (2010) Ion channel voltage sensors: structure, function, and pathophysiology. Neuron 67(6):915-928. doi: 10.1016/j.neuron.2010.08.021
    • (2010) Neuron , vol.67 , Issue.6 , pp. 915-928
    • Catterall, W.A.1
  • 79
    • 78650055985 scopus 로고    scopus 로고
    • 3(10) helices in channels and other membrane proteins
    • 10.1085/jgp.201010508 1:CAS:528:DC%2BC3MXmtFan
    • Vieira-Pires RS, Morais-Cabral JH (2010) 3(10) helices in channels and other membrane proteins. J Gen Physiol 136(6):585-592. doi: 10.1085/jgp.201010508
    • (2010) J Gen Physiol , vol.136 , Issue.6 , pp. 585-592
    • Vieira-Pires, R.S.1    Morais-Cabral, J.H.2
  • 80
    • 84855998904 scopus 로고    scopus 로고
    • Structural basis for gating charge movement in the voltage sensor of a sodium channel
    • 10.1073/pnas.1118434109 1:CAS:528:DC%2BC38XhtFyku70%3D
    • Yarov-Yarovoy V, DeCaen PG, Westenbroek RE, Pan CY, Scheuer T, Baker D, Catterall WA (2012) Structural basis for gating charge movement in the voltage sensor of a sodium channel. Proc Natl Acad Sci USA 109(2):E93-E102. doi: 10.1073/pnas.1118434109
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.2 , pp. E93-E102
    • Yarov-Yarovoy, V.1    DeCaen, P.G.2    Westenbroek, R.E.3    Pan, C.Y.4    Scheuer, T.5    Baker, D.6    Catterall, W.A.7
  • 81
    • 77950488909 scopus 로고    scopus 로고
    • A gating charge transfer center in voltage sensors
    • 10.1126/science.1185954 1:CAS:528:DC%2BC3cXjvFKltrk%3D
    • Tao X, Lee A, Limapichat W, Dougherty DA, MacKinnon R (2010) A gating charge transfer center in voltage sensors. Science 328(5974):67-73. doi: 10.1126/science.1185954
    • (2010) Science , vol.328 , Issue.5974 , pp. 67-73
    • Tao, X.1    Lee, A.2    Limapichat, W.3    Dougherty, D.A.4    MacKinnon, R.5
  • 84
    • 79953236295 scopus 로고    scopus 로고
    • Lipid-dependent gating of a voltage-gated potassium channel
    • 10.1038/ncomms1254 1:CAS:528:DC%2BC3MXkt12iurs%3D
    • Zheng H, Liu W, Anderson LY, Jiang QX (2011) Lipid-dependent gating of a voltage-gated potassium channel. Nat Commun 2:250. doi: 10.1038/ncomms1254
    • (2011) Nat Commun , vol.2 , pp. 250
    • Zheng, H.1    Liu, W.2    Anderson, L.Y.3    Jiang, Q.X.4
  • 85
    • 0042071600 scopus 로고    scopus 로고
    • Sulphonylurea action revisited: The post-cloning era
    • 10.1007/s00125-003-1143-3 1:STN:280:DC%2BD3szmtlSgsA%3D%3D
    • Gribble FM, Reimann F (2003) Sulphonylurea action revisited: the post-cloning era. Diab tologia 46(7):875-891. doi: 10.1007/s00125-003-1143-3
    • (2003) Diab Tologia , vol.46 , Issue.7 , pp. 875-891
    • Gribble, F.M.1    Reimann, F.2
  • 87
    • 34548386717 scopus 로고    scopus 로고
    • Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
    • 10.1038/sj.emboj.7601828 1:CAS:528:DC%2BD2sXpvFWhsbw%3D
    • Nishida M, Cadene M, Chait BT, MacKinnon R (2007) Crystal structure of a Kir3.1-prokaryotic Kir channel chimera. EMBO J 26(17):4005-4015. doi: 10.1038/sj.emboj.7601828
    • (2007) EMBO J , vol.26 , Issue.17 , pp. 4005-4015
    • Nishida, M.1    Cadene, M.2    Chait, B.T.3    MacKinnon, R.4
  • 88
    • 72949091450 scopus 로고    scopus 로고
    • + channel Kir2.2 at 3.1 A resolution
    • 10.1126/science.1180310 1:CAS:528:DC%2BD1MXhsFGmsL%2FP
    • + channel Kir2.2 at 3.1 A resolution. Science 326(5960):1668-1674. doi: 10.1126/science.1180310
    • (2009) Science , vol.326 , Issue.5960 , pp. 1668-1674
    • Tao, X.1    Avalos, J.L.2    Chen, J.3    MacKinnon, R.4
  • 89
    • 80053485088 scopus 로고    scopus 로고
    • + channel and gating regulation by G proteins, PIP2, and sodium
    • 10.1016/j.cell.2011.07.046 1:CAS:528:DC%2BC3MXht1GrsLjK
    • + channel and gating regulation by G proteins, PIP2, and sodium. Cell 147(1):199-208. doi: 10.1016/j.cell.2011.07.046
    • (2011) Cell , vol.147 , Issue.1 , pp. 199-208
    • Whorton, M.R.1    MacKinnon, R.2
  • 90
    • 84856691589 scopus 로고    scopus 로고
    • Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating
    • 10.1038/nsmb.2208 1:CAS:528:DC%2BC38XlsF2lug%3D%3D
    • Bavro VN, De Zorzi R, Schmidt MR, Muniz JR, Zubcevic L, Sansom MS, Venien-Bryan C, Tucker SJ (2012) Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating. Nat Struct Mol Biol 19(2):158-163. doi: 10.1038/nsmb.2208
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.2 , pp. 158-163
    • Bavro, V.N.1    De Zorzi, R.2    Schmidt, M.R.3    Muniz, J.R.4    Zubcevic, L.5    Sansom, M.S.6    Venien-Bryan, C.7    Tucker, S.J.8
  • 91
    • 84878996278 scopus 로고    scopus 로고
    • X-ray structure of the mammalian GIRK2-betagamma G-protein complex
    • 10.1038/nature12241 1:CAS:528:DC%2BC3sXovVWitb0%3D
    • Whorton MR, MacKinnon R (2013) X-ray structure of the mammalian GIRK2-betagamma G-protein complex. Nature 498(7453):190-197. doi: 10.1038/nature12241
    • (2013) Nature , vol.498 , Issue.7453 , pp. 190-197
    • Whorton, M.R.1    MacKinnon, R.2
  • 93
    • 80053131218 scopus 로고    scopus 로고
    • + channel Kir2.2
    • 10.1038/nature10370 1:CAS:528:DC%2BC3MXhtFersLnF
    • + channel Kir2.2. Nature 477(7365):495-498. doi: 10.1038/nature10370
    • (2011) Nature , vol.477 , Issue.7365 , pp. 495-498
    • Hansen, S.B.1    Tao, X.2    MacKinnon, R.3
  • 94
    • 80052858808 scopus 로고    scopus 로고
    • + channels: Differential role of the pore-helix glutamate in stabilizing the channel pore
    • 10.1016/j.bbrc.2011.08.062 1:CAS:528:DC%2BC3MXhtF2gs7vN
    • + channels: differential role of the pore-helix glutamate in stabilizing the channel pore. Biochem Biophys Res Commun 413(1):1-4. doi: 10.1016/j.bbrc.2011.08.062
    • (2011) Biochem Biophys Res Commun , vol.413 , Issue.1 , pp. 1-4
    • Raja, M.1
  • 95
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • 10.1038/nn1411 1:CAS:528:DC%2BD2MXhslyqsbo%3D
    • Pegan S, Arrabit C, Zhou W, Kwiatkowski W, Collins A, Slesinger PA, Choe S (2005) Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nat Neurosci 8(3):279-287. doi: 10.1038/nn1411
    • (2005) Nat Neurosci , vol.8 , Issue.3 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6    Choe, S.7
  • 96
    • 71449120188 scopus 로고    scopus 로고
    • Physical determinants of strong voltage sensitivity of K(+) channel block
    • 10.1038/nsmb.1717 1:CAS:528:DC%2BD1MXhsVyls7fP
    • Xu Y, Shin HG, Szep S, Lu Z (2009) Physical determinants of strong voltage sensitivity of K(+) channel block. Nat Struct Mol Biol 16(12):1252-1258. doi: 10.1038/nsmb.1717
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.12 , pp. 1252-1258
    • Xu, Y.1    Shin, H.G.2    Szep, S.3    Lu, Z.4
  • 97
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • 10.1016/j.cell.2010.05.003 1:CAS:528:DC%2BC3cXnvValtLw%3D
    • Clarke OB, Caputo AT, Hill AP, Vandenberg JI, Smith BJ, Gulbis JM (2010) Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell 141(6):1018-1029. doi: 10.1016/j.cell.2010.05.003
    • (2010) Cell , vol.141 , Issue.6 , pp. 1018-1029
    • Clarke, O.B.1    Caputo, A.T.2    Hill, A.P.3    Vandenberg, J.I.4    Smith, B.J.5    Gulbis, J.M.6
  • 98
    • 48249116482 scopus 로고    scopus 로고
    • PIP2 is a necessary cofactor for ion channel function: How and why?
    • 10.1146/annurev.biophys.37.032807.125859 1:CAS:528:DC%2BD1cXnsVGltbk%3D
    • Suh BC, Hille B (2008) PIP2 is a necessary cofactor for ion channel function: how and why? Annu Rev Biophys 37:175-195. doi: 10.1146/annurev.biophys.37.032807.125859
    • (2008) Annu Rev Biophys , vol.37 , pp. 175-195
    • Suh, B.C.1    Hille, B.2
  • 99
    • 77953903075 scopus 로고    scopus 로고
    • Lipids driving protein structure? Evolutionary adaptations in Kir channels
    • 10.4161/chan.4.3.12129
    • D'Avanzo N, Cheng WW, Wang S, Enkvetchakul D, Nichols CG (2010) Lipids driving protein structure? Evolutionary adaptations in Kir channels. Channels 4(3):139-141. doi: 10.4161/chan.4.3.12129
    • (2010) Channels , vol.4 , Issue.3 , pp. 139-141
    • D'Avanzo, N.1    Cheng, W.W.2    Wang, S.3    Enkvetchakul, D.4    Nichols, C.G.5
  • 101
    • 0032526428 scopus 로고    scopus 로고
    • + channel stimulated by arachidonic acid and polyunsaturated fatty acids
    • 10.1093/emboj/17.12.3297 1:CAS:528:DyaK1cXksFClt7g%3D
    • + channel stimulated by arachidonic acid and polyunsaturated fatty acids. EMBO J 17(12):3297-3308. doi: 10.1093/emboj/17.12.3297
    • (1998) EMBO J , vol.17 , Issue.12 , pp. 3297-3308
    • Fink, M.1    Lesage, F.2    Duprat, F.3    Heurteaux, C.4    Reyes, R.5    Fosset, M.6    Lazdunski, M.7
  • 102
    • 0037185379 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids induce ischemic and epileptic tolerance
    • 10.1016/S0306-4522(01)00473-0 1:CAS:528:DC%2BD38XktVKmuw%3D%3D
    • Blondeau N, Widmann C, Lazdunski M, Heurteaux C (2002) Polyunsaturated fatty acids induce ischemic and epileptic tolerance. Neuroscience 109(2):231-241. doi: 10.1016/S0306-4522(01)00473-0
    • (2002) Neuroscience , vol.109 , Issue.2 , pp. 231-241
    • Blondeau, N.1    Widmann, C.2    Lazdunski, M.3    Heurteaux, C.4
  • 104
    • 84926368897 scopus 로고    scopus 로고
    • Transmembrane helix straightening and buckling underlies activation of mechanosensitive and thermosensitive K(2P) channels
    • 10.1016/j.neuron.2014.11.017 1:CAS:528:DC%2BC2cXitFCrtLzN
    • Lolicato M, Riegelhaupt PM, Arrigoni C, Clark KA, Minor DL Jr (2014) Transmembrane helix straightening and buckling underlies activation of mechanosensitive and thermosensitive K(2P) channels. Neuron 84(6):1198-1212. doi: 10.1016/j.neuron.2014.11.017
    • (2014) Neuron , vol.84 , Issue.6 , pp. 1198-1212
    • Lolicato, M.1    Riegelhaupt, P.M.2    Arrigoni, C.3    Clark, K.A.4    Minor, D.L.5
  • 107
    • 84856297467 scopus 로고    scopus 로고
    • Crystal structure of the human two-pore domain potassium channel K2P1
    • 10.1126/science.1213274 1:CAS:528:DC%2BC38XhtFajtr0%3D
    • Miller AN, Long SB (2012) Crystal structure of the human two-pore domain potassium channel K2P1. Science 335(6067):432-436. doi: 10.1126/science.1213274
    • (2012) Science , vol.335 , Issue.6067 , pp. 432-436
    • Miller, A.N.1    Long, S.B.2
  • 108
    • 84856244292 scopus 로고    scopus 로고
    • + ion channel
    • 10.1126/science.1213808 1:CAS:528:DC%2BC38XhtFajtro%3D
    • + ion channel. Science 335(6067):436-441. doi: 10.1126/science.1213808
    • (2012) Science , vol.335 , Issue.6067 , pp. 436-441
    • Brohawn, S.G.1    Del Marmol, J.2    MacKinnon, R.3
  • 110
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • 10.1038/417515a 1:CAS:528:DC%2BD38XktVeht7g%3D
    • Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (2002) Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417(6888):515-522. doi: 10.1038/417515a
    • (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
  • 112
    • 33748622291 scopus 로고    scopus 로고
    • + channels
    • 10.1016/j.cell.2006.08.029 1:CAS:528:DC%2BD28XhtVCnsrvN
    • + channels. Cell 126(6):1161-1173. doi: 10.1016/j.cell.2006.08.029
    • (2006) Cell , vol.126 , Issue.6 , pp. 1161-1173
    • Ye, S.1    Li, Y.2    Chen, L.3    Jiang, Y.4
  • 113
    • 77954659083 scopus 로고    scopus 로고
    • + channel
    • 10.1038/nature09252 1:CAS:528:DC%2BC3cXnvVShu7o%3D
    • + channel. Nature 466(7304):393-397. doi: 10.1038/nature09252
    • (2010) Nature , vol.466 , Issue.7304 , pp. 393-397
    • Wu, Y.1    Yang, Y.2    Ye, S.3    Jiang, Y.4
  • 115
    • 77954591491 scopus 로고    scopus 로고
    • 2+-activation apparatus at 3.0 A resolution
    • 10.1126/science.1190414 1:CAS:528:DC%2BC3cXosVWgu7o%3D
    • 2+-activation apparatus at 3.0 A resolution. Science 329(5988):182-186. doi: 10.1126/science.1190414
    • (2010) Science , vol.329 , Issue.5988 , pp. 182-186
    • Yuan, P.1    Leonetti, M.D.2    Pico, A.R.3    Hsiung, Y.4    MacKinnon, R.5
  • 116
    • 33748604768 scopus 로고    scopus 로고
    • + transporter: Multiple conformations of an octameric ring
    • 10.1016/j.cell.2006.08.028 1:CAS:528:DC%2BD28XhtVCnsrvM
    • + transporter: multiple conformations of an octameric ring. Cell 126(6):1147-1159. doi: 10.1016/j.cell.2006.08.028
    • (2006) Cell , vol.126 , Issue.6 , pp. 1147-1159
    • Albright, R.A.1    Ibar, J.L.2    Kim, C.U.3    Gruner, S.M.4    Morais-Cabral, J.H.5
  • 117
    • 0037077136 scopus 로고    scopus 로고
    • A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch
    • 10.1016/S0092-8674(02)00768-7 1:CAS:528:DC%2BD38XkvV2ju7o%3D
    • Roosild TP, Miller S, Booth IR, Choe S (2002) A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch. Cell 109(6):781-791. doi: 10.1016/S0092-8674(02)00768-7
    • (2002) Cell , vol.109 , Issue.6 , pp. 781-791
    • Roosild, T.P.1    Miller, S.2    Booth, I.R.3    Choe, S.4
  • 118
    • 70249124205 scopus 로고    scopus 로고
    • Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
    • 10.1038/nature08291 1:CAS:528:DC%2BD1MXhtVKhs73E
    • Wang L, Sigworth FJ (2009) Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 461(7261):292-295. doi: 10.1038/nature08291
    • (2009) Nature , vol.461 , Issue.7261 , pp. 292-295
    • Wang, L.1    Sigworth, F.J.2
  • 120
    • 0035054180 scopus 로고    scopus 로고
    • + channel and demonstration of its presence in the human BK channel
    • 10.1016/S0896-6273(01)00236-7 1:CAS:528:DC%2BD3MXis1KjsbY%3D
    • + channel and demonstration of its presence in the human BK channel. Neuron 29(3):593-601. doi: 10.1016/S0896-6273(01)00236-7
    • (2001) Neuron , vol.29 , Issue.3 , pp. 593-601
    • Jiang, Y.1    Pico, A.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 121
    • 70349451964 scopus 로고    scopus 로고
    • Assembly of Kch, a putative potassium channel from Escherichia coli
    • 10.1016/j.jsb.2009.07.018
    • Lundback AK, Muller SA, Engel A, Hebert H (2009) Assembly of Kch, a putative potassium channel from Escherichia coli. J Struct Biol 168(2):288-293. doi: 10.1016/j.jsb.2009.07.018
    • (2009) J Struct Biol , vol.168 , Issue.2 , pp. 288-293
    • Lundback, A.K.1    Muller, S.A.2    Engel, A.3    Hebert, H.4
  • 122
    • 0037966580 scopus 로고    scopus 로고
    • + sensitivity in E. Coli
    • 10.1016/S0014-5793(03)00706-3 1:CAS:528:DC%2BD3sXlsVahsrw%3D
    • + sensitivity in E. coli. FEBS Lett 547(1-3):165-169. doi: 10.1016/S0014-5793(03)00706-3
    • (2003) FEBS Lett , vol.547 , Issue.1-3 , pp. 165-169
    • Hellmer, J.1    Zeilinger, C.2
  • 123
    • 11844269841 scopus 로고    scopus 로고
    • + channel RCK domain with charged membrane surfaces
    • 10.1021/bi048390f 1:CAS:528:DC%2BD2cXhtVKgtrbM
    • + channel RCK domain with charged membrane surfaces. Biochemistry 44(1):62-71. doi: 10.1021/bi048390f
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 62-71
    • Ptak, C.P.1    Cuello, L.G.2    Perozo, E.3
  • 124
    • 84876208373 scopus 로고    scopus 로고
    • Gating of the TrkH ion channel by its associated RCK protein TrkA
    • 10.1038/nature12056 1:CAS:528:DC%2BC3sXmtV2nuro%3D
    • Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M (2013) Gating of the TrkH ion channel by its associated RCK protein TrkA. Nature 496(7445):317-322. doi: 10.1038/nature12056
    • (2013) Nature , vol.496 , Issue.7445 , pp. 317-322
    • Cao, Y.1    Pan, Y.2    Huang, H.3    Jin, X.4    Levin, E.J.5    Kloss, B.6    Zhou, M.7
  • 128
    • 84887960452 scopus 로고    scopus 로고
    • The projection structure of Kch, a putative potassium channel in Escherichia coli, by electron crystallography
    • 10.1016/j.bbamem.2013.09.006 1:CAS:528:DC%2BC3sXhvFOltbbN
    • Kuang Q, Purhonen P, Jegerschold C, Hebert H (2014) The projection structure of Kch, a putative potassium channel in Escherichia coli, by electron crystallography. Biochim Biophys Acta 1838(1):237-243. doi: 10.1016/j.bbamem.2013.09.006
    • (2014) Biochim Biophys Acta , vol.1838 , Issue.1 , pp. 237-243
    • Kuang, Q.1    Purhonen, P.2    Jegerschold, C.3    Hebert, H.4
  • 129
    • 84920999760 scopus 로고    scopus 로고
    • Free RCK Arrangement in Kch, a Putative Escherichia coli Potassium Channel, as Suggested by Electron Crystallography
    • 10.1016/j.str.2014.10.018 1:CAS:528:DC%2BC2cXitFCrtLnK
    • Kuang Q, Purhonen P, Jegerschold C, Koeck PJ, Hebert H (2015) Free RCK Arrangement in Kch, a Putative Escherichia coli Potassium Channel, as Suggested by Electron Crystallography. Structure 23(1):199-205. doi: 10.1016/j.str.2014.10.018
    • (2015) Structure , vol.23 , Issue.1 , pp. 199-205
    • Kuang, Q.1    Purhonen, P.2    Jegerschold, C.3    Koeck, P.J.4    Hebert, H.5
  • 130
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • 10.1002/jcc.20084 1:CAS:528:DC%2BD2cXmvVOhsbs%3D
    • Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612. doi: 10.1002/jcc.20084
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3    Couch, G.S.4    Greenblatt, D.M.5    Meng, E.C.6    Ferrin, T.E.7
  • 131
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • 10.1038/nature10238 1:CAS:528:DC%2BC3MXos1OmsLs%3D
    • Payandeh J, Scheuer T, Zheng N, Catterall WA (2011) The crystal structure of a voltage-gated sodium channel. Nature 475(7356):353-358. doi: 10.1038/nature10238
    • (2011) Nature , vol.475 , Issue.7356 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 133
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • 10.1038/nature12822 1:CAS:528:DC%2BC3sXhvVyis77N
    • Liao M, Cao E, Julius D, Cheng Y (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504(7478):107-112. doi: 10.1038/nature12822
    • (2013) Nature , vol.504 , Issue.7478 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 134
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • 10.1038/nature11077 1:CAS:528:DC%2BC38Xot1Cnurc%3D
    • Payandeh J, Gamal El-Din TM, Scheuer T, Zheng N, Catterall WA (2012) Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 486(7401):135-139. doi: 10.1038/nature11077
    • (2012) Nature , vol.486 , Issue.7401 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5


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