메뉴 건너뛰기




Volumn 3 MAR, Issue , 2012, Pages

Cytoplasmic domains and voltage-dependent potassium channel gating

Author keywords

Activation deactivation gating; Cytoplasmic domains; Inactivation gating; Potassium channel; Structure function relationships; Voltage dependent gating

Indexed keywords

CALMODULIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; DELAYED RECTIFIER POTASSIUM CHANNEL; POTASSIUM CHANNEL; POTASSIUM CHANNEL HERG; POTASSIUM CHANNEL KCNQ; SHAKER POTASSIUM CHANNEL; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT POTASSIUM CHANNEL; VOLTAGE GATED CALCIUM CHANNEL;

EID: 84866053486     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2012.00049     Document Type: Article
Times cited : (42)

References (253)
  • 1
    • 44049102683 scopus 로고    scopus 로고
    • Single particle image reconstruction of the human recombinant Kv2 1 channel
    • Adair, B., Nunn, R., Lewis, S., Dukes, I, Philipson, L., and Yeager, M. (2008). Single particle image reconstruction of the human recombinant Kv2.1 channel. Biophys. J. 94, 2106-2114.
    • (2008) Biophys. J. , vol.94 , pp. 2106-2114
    • Adair, B.1    Nunn, R.2    Lewis, S.3    Dukes, I.4    Philipson, L.5    Yeager, M.6
  • 5
    • 43849103812 scopus 로고    scopus 로고
    • Thermodynamic and kinetic properties of amino-terminal and S4-S5 loop HERG channel mutants under steady-state conditions
    • Alonso-Ron, C., de la Peña, P., Miranda, P., Domínguez, P., and Barros, F. (2008). Thermodynamic and kinetic properties of amino-terminal and S4-S5 loop HERG channel mutants under steady-state conditions. Biophys. J. 94, 3893-3911.
    • (2008) Biophys. J. , vol.94 , pp. 3893-3911
    • Alonso-Ron, C.1    de la Peña, P.2    Miranda, P.3    Domínguez, P.4    Barros, F.5
  • 6
    • 67349135030 scopus 로고    scopus 로고
    • Role of intracellular domains in the function of the herg potassium channel
    • Al-Owais, M., Bracey, K., and Wray, D. (2009). Role of intracellular domains in the function of the herg potassium channel. Eur. Biophys. J. 38, 569-576.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 569-576
    • Al-Owais, M.1    Bracey, K.2    Wray, D.3
  • 8
    • 0026597932 scopus 로고
    • Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae
    • Anderson,J. A.,Huprikar,S. S.,Kochian, L. V., Lucas, W. J., and Gaber, R. F. (1992). Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae. Proc. Natl.Acad. Sci. U.S.A. 89, 3736-3740.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3736-3740
    • Anderson, J.A.1    Huprikar, S.S.2    Kochian, L.V.3    Lucas, W.J.4    Gaber, R.F.5
  • 12
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons
    • Armstrong, C. M. (1971). Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons. J. Gen. Physiol. 58, 413-437.
    • (1971) J. Gen. Physiol. , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 13
    • 0017743723 scopus 로고
    • Inactivation of the sodium channel II. Gating current experiments
    • Armstrong, C. M., and Bezanilla, F. (1977). Inactivation of the sodium channel. II. Gating current experiments. J. Gen. Physiol. 70, 567-590.
    • (1977) J. Gen. Physiol. , vol.70 , pp. 567-590
    • Armstrong, C.M.1    Bezanilla, F.2
  • 14
    • 0015902531 scopus 로고
    • Destruction of sodium conductance inactivation in squid axons perfused with pronase
    • Armstrong, C. M., Bezanilla, F., and Rojas, E. (1973). Destruction of sodium conductance inactivation in squid axons perfused with pronase. J. Gen. Physiol. 62, 375-391.
    • (1973) J. Gen. Physiol. , vol.62 , pp. 375-391
    • Armstrong, C.M.1    Bezanilla, F.2    Rojas, E.3
  • 15
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft, F. M. (2006). From molecule to malady. Nature 440, 440-447.
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 16
    • 78650589673 scopus 로고    scopus 로고
    • Eag and HERG potassium channels as novel therapeutic targets in cancer
    • Asher, V., Sowter, H., Shaw, R., Bali, A., and Khan, R. (2010). Eag and HERG potassium channels as novel therapeutic targets in cancer. World J. Surg. Oncol. 8, 113.
    • (2010) World J. Surg. Oncol. , vol.8 , pp. 113
    • Asher, V.1    Sowter, H.2    Shaw, R.3    Bali, A.4    Khan, R.5
  • 18
    • 79952419012 scopus 로고    scopus 로고
    • Mass spectrometry-based phosphoproteomics reveals multisite phosphorylation of mammalian brain voltage-gated sodium and potassium channels
    • Baek, J.-H., Cerda, O., and Trimmer, J. S. (2011). Mass spectrometry-based phosphoproteomics reveals multisite phosphorylation of mammalian brain voltage-gated sodium and potassium channels. Semin. Cell Dev. Biol. 22, 153-159.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 153-159
    • Baek, J.-H.1    Cerda, O.2    Trimmer, J.S.3
  • 19
    • 32344440232 scopus 로고    scopus 로고
    • NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain
    • Baker,K.A.,Hilty,C.,Peti,W.,Prince,A., Pfaffinger, P. J., Wider, G., Wüthrich, K., and Choe, S. (2006). NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain. Biochemistry 45, 1663-1672.
    • (2006) Biochemistry , vol.45 , pp. 1663-1672
    • Baker, K.A.1    Hilty, C.2    Peti, W.3    Prince, A.4    Pfaffinger, P.J.5    Wider, G.6    Wüthrich, K.7    Choe, S.8
  • 22
    • 62349098199 scopus 로고    scopus 로고
    • Dynamic coupling of voltage sensor and gate involved in closed-state inactivation of Kv4 2 channels
    • Barghaan, J., and Bähring, R. (2009). Dynamic coupling of voltage sensor and gate involved in closed-state inactivation of Kv4.2 channels. J. Gen. Physiol. 133, 205-224.
    • (2009) J. Gen. Physiol. , vol.133 , pp. 205-224
    • Barghaan, J.1    Bähring, R.2
  • 23
    • 38949143719 scopus 로고    scopus 로고
    • Role of N-terminal domain and accessory subunits in controlling deactivation-inactivation coupling of Kv4 2 channels
    • Barghaan, J., Tozakidou, M., Ehmke, H., and Bähring, R. (2008). Role of N-terminal domain and accessory subunits in controlling deactivation-inactivation coupling of Kv4.2 channels. Biophys. J. 94, 1276-1294.
    • (2008) Biophys. J. , vol.94 , pp. 1276-1294
    • Barghaan, J.1    Tozakidou, M.2    Ehmke, H.3    Bähring, R.4
  • 27
    • 0028195054 scopus 로고
    • + current in resting potential and thyrotropin-releasing hormone-induced changes in cell excitability of GH3 rat anterior pituitary cells
    • + current in resting potential and thyrotropin-releasing hormone-induced changes in cell excitability of GH3 rat anterior pituitary cells. Pflügers Arch. 426, 221-230.
    • (1994) Pflügers Arch , vol.426 , pp. 221-230
    • Barros, F.1    Villalobos, C.2    García-Sancho, J.3    del Camino, D.4    de la Peña, P.5
  • 30
    • 0032929808 scopus 로고    scopus 로고
    • Determinants of potassium channel assembly localized within the cytoplasmic C-terminal domain of Kv2
    • Bentley, G. N., Brooks, M. A., O'Neill, C. A., and Findlay, J. B. (1999). Determinants of potassium channel assembly localized within the cytoplasmic C-terminal domain of Kv2.1. Biochim. Biophys. Acta 1418, 176-184.
    • (1999) 1. Biochim. Biophys. Acta , vol.1418 , pp. 176-184
    • Bentley, G.N.1    Brooks, M.A.2    O'Neill, C.A.3    Findlay, J.B.4
  • 31
    • 39449113300 scopus 로고    scopus 로고
    • + channel-drug interactions by ancillary subunits
    • + channel-drug interactions by ancillary subunits. J. Physiol. 586, 929-950.
    • (2008) J. Physiol. , vol.586 , pp. 929-950
    • Bett, G.C.L.1    Rasmusson, R.L.2
  • 32
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • Bezanilla, F. (2008). How membrane proteins sense voltage. Nat. Rev. Mol. Cell Biol. 9, 323-332.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 323-332
    • Bezanilla, F.1
  • 33
  • 35
    • 36649017644 scopus 로고    scopus 로고
    • Role of the S6 C-terminus in KCNQ1 channel gating
    • Boulet, I. R., Labro, A. J., Raes, A. L., and Snyders, D. J. (2007). Role of the S6 C-terminus in KCNQ1 channel gating. J. Physiol. 585, 325-337.
    • (2007) J. Physiol. , vol.585 , pp. 325-337
    • Boulet, I.R.1    Labro, A.J.2    Raes, A.L.3    Snyders, D.J.4
  • 37
    • 27644491039 scopus 로고    scopus 로고
    • Contribution of N-and C-terminal Kv4.2 channel domains to KChIP interaction
    • Callsen, B., Isbrandt, D., Sauter, K., Hartmann, L. S., Pongs, O., and Bähring, R. (2005). Contribution of N-and C-terminal Kv4.2 channel domains to KChIP interaction. J. Physiol. 568, 397-412.
    • (2005) J. Physiol. , vol.568 , pp. 397-412
    • Callsen, B.1    Isbrandt, D.2    Sauter, K.3    Hartmann, L.S.4    Pongs, O.5    Bähring, R.6
  • 38
    • 78650907529 scopus 로고    scopus 로고
    • Mining recent brain proteomic databases for ion channel phosphosite nuggets
    • Cerda, O., Baek, J.-Y., and Trimmer, J. S. (2010). Mining recent brain proteomic databases for ion channel phosphosite nuggets. J. Gen. Physiol. 137, 3-16.
    • (2010) J. Gen. Physiol. , vol.137 , pp. 3-16
    • Cerda, O.1    Baek, J.-Y.2    Trimmer, J.S.3
  • 39
    • 78049405427 scopus 로고    scopus 로고
    • Analysis and functional implications of phosphorylation of neuronal voltage-gated potassium channels
    • Cerda, O., and Trimmer, J. S. (2010). Analysis and functional implications of phosphorylation of neuronal voltage-gated potassium channels. Neurosci. Lett. 486, 60-67.
    • (2010) Neurosci. Lett. , vol.486 , pp. 60-67
    • Cerda, O.1    Trimmer, J.S.2
  • 41
    • 0033537885 scopus 로고    scopus 로고
    • Long QT syndrome-associated mutations in the Per-Arnt-sim (PAS) domain of HERG potassium channels accelerate deactivation
    • Chen, J., Zou, A., Splawski, I., Keating, M. T., and Sanguinetti, M. C. (1999). Long QT syndrome-associated mutations in the Per-Arnt-sim (PAS) domain of HERG potassium channels accelerate deactivation. J. Biol. Chem. 274, 10113-10118.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10113-10118
    • Chen, J.1    Zou, A.2    Splawski, I.3    Keating, M.T.4    Sanguinetti, M.C.5
  • 44
    • 24044494280 scopus 로고    scopus 로고
    • Kv1 5 surface expression is modulated by retrograde trafficking of newly endocytosed channels by the dynein motor
    • Choi, W. S., Khurana, A., Mathur, R., Viswanathan, V., Steele, D. F., and Fedida, D. (2005). Kv1.5 surface expression is modulated by retrograde trafficking of newly endocytosed channels by the dynein motor. Circ. Res. 97, 363-371.
    • (2005) Circ. Res. , vol.97 , pp. 363-371
    • Choi, W.S.1    Khurana, A.2    Mathur, R.3    Viswanathan, V.4    Steele, D.F.5    Fedida, D.6
  • 46
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • Clarke, O. B., Caputo, A. T., Hill, A. P., Vandenberg, J. I., Smith, B. J., and Gulbis, J. M. (2010). Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell 141, 1018-1029.
    • (2010) Cell , vol.141 , 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
  • 49
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease
    • Cohen, P. (2001). The role of protein phosphorylation in human health and disease. Eur. J. Biochem. 268, 5001-5010.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 50
    • 0028605349 scopus 로고
    • Elimination of rapid potassium channel inactivation by phosphorylation of the inactivation gate
    • Covarrubias, M., Wei, A., Salkoff, L., and Vyas, T. B. (1994). Elimination of rapid potassium channel inactivation by phosphorylation of the inactivation gate. Neuron 13, 1403-1412.
    • (1994) Neuron , vol.13 , pp. 1403-1412
    • Covarrubias, M.1    Wei, A.2    Salkoff, L.3    Vyas, T.B.4
  • 51
    • 79961111359 scopus 로고    scopus 로고
    • Where's the gate? Gating in the deep pore of the BKCa channel
    • Cox, D. H., and Hoshi, T. (2011). Where's the gate? Gating in the deep pore of the BKCa channel. J. Gen. Physiol. 238, 133-136.
    • (2011) J. Gen. Physiol. , vol.238 , pp. 133-136
    • Cox, D.H.1    Hoshi, T.2
  • 53
    • 0035907235 scopus 로고    scopus 로고
    • Analysis of the cyclic nucleotide binding domain on the HERG potassium channel and interactions with KCNE2
    • Cui, J., Kagan, A., Qin, D., Mathew, J., Melman, Y., and McDonald, T. V. (2001). Analysis of the cyclic nucleotide binding domain on the HERG potassium channel and interactions with KCNE2. J. Biol. Chem. 276, 17244-17251.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17244-17251
    • Cui, J.1    Kagan, A.2    Qin, D.3    Mathew, J.4    Melman, Y.5    McDonald, T.V.6
  • 55
    • 0035370622 scopus 로고    scopus 로고
    • A discrete amino terminal domain of Kv1 5 and Kv1. 4 potassium channels interacts with the spectrin repeats of alpha-actinin-2
    • Cukovic, D., Lu, G. W., Wible, B., Steele, D. F., and Fedida, D. (2001). A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2. FEBS Lett. 498, 87-92.
    • (2001) FEBS Lett , vol.498 , pp. 87-92
    • Cukovic, D.1    Lu, G.W.2    Wible, B.3    Steele, D.F.4    Fedida, D.5
  • 58
    • 1842740890 scopus 로고    scopus 로고
    • Voltage-dependent gating of hyperpolarization-activated, cyclic nucleotide-gated pacemaker channels. molecular coupling between the S4-S5 and C-linkers
    • Decher,N.,Chen,J.,and Sanguinetti,M. C. (2004). Voltage-dependent gating of hyperpolarization-activated, cyclic nucleotide-gated pacemaker channels. molecular coupling between the S4-S5 and C-linkers. J. Biol. Chem. 279, 13859-13865.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13859-13865
    • Decher, N.1    Chen, J.2    Sanguinetti, M.C.3
  • 61
    • 0026757484 scopus 로고
    • Okadaic acid and calyculin A enhance the effect of thyrotropinreleasing hormone on GH3 rat anterior pituitary cells excitability
    • Delgado, L. M., de la Peña, P., del Camino, D., and Barros, F. (1992). Okadaic acid and calyculin A enhance the effect of thyrotropinreleasing hormone on GH3 rat anterior pituitary cells excitability. FEBS Lett. 311, 41-45.
    • (1992) FEBS Lett , vol.311 , pp. 41-45
    • Delgado, L.M.1    de la Peña, P.2    del Camino, D.3    Barros, F.4
  • 62
    • 0026045545 scopus 로고
    • + channel behaves like an openchannel blocker
    • + channel behaves like an openchannel blocker. Neuron 7, 743-753.
    • (1991) Neuron , vol.7 , pp. 743-753
    • Demo, S.D.1    Yellen, G.2
  • 63
    • 0037214636 scopus 로고    scopus 로고
    • Effect of S6 tail mutations on charge movement in Shaker potassium channels
    • Ding, S., and Horn, R. (2003). Effect of S6 tail mutations on charge movement in Shaker potassium channels. Biophys. J. 84, 295-305.
    • (2003) Biophys. J. , vol.84 , pp. 295-305
    • Ding, S.1    Horn, R.2
  • 64
    • 0028321838 scopus 로고
    • + channel inactivation gating by the cAMP-dependent protein kinase
    • + channel inactivation gating by the cAMP-dependent protein kinase. Neuron 12, 1097-1109.
    • (1994) Neuron , vol.12 , pp. 1097-1109
    • Drain, P.1    Dubin, A.E.2    Aldrich, R.W.3
  • 67
    • 80054974935 scopus 로고    scopus 로고
    • Electrostatic int. 4 channel
    • Fan, Z., Ji, X., Zhang, D., and Xiao, Z. (2012). Electrostatic interaction between inactivation ball and T1-S1 linker region of Kv1.4 channel. Biochim. Biophys. Acta 1818, 55-63.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 55-63
    • Fan, Z.1    Ji, X.2    Zhang, D.3    Xiao, Z.4
  • 71
    • 4644276334 scopus 로고    scopus 로고
    • Acquired QT interval prolongation and HERG: implications for drug discovery and development
    • Finlayson, K., Witchel, H. J., McCulloch, J., and Sharkey, J. (2004). Acquired QT interval prolongation and HERG: implications for drug discovery and development. Eur. J. Pharmacol. 500, 129-142.
    • (2004) Eur. J. Pharmacol. , vol.500 , pp. 129-142
    • Finlayson, K.1    Witchel, H.J.2    McCulloch, J.3    Sharkey, J.4
  • 74
    • 36348965431 scopus 로고    scopus 로고
    • Regulation of ion transport proteins by membrane phosphoinositides
    • Gamper, N., and Shapiro, M. S. (2007). Regulation of ion transport proteins by membrane phosphoinositides. Nat. Rev. Neurosci. 8, 921-934.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 921-934
    • Gamper, N.1    Shapiro, M.S.2
  • 75
    • 64549108500 scopus 로고    scopus 로고
    • Divide and conquer: high resolution structural information on TRP channel fragments
    • Gaudet, R. (2009). Divide and conquer: high resolution structural information on TRP channel fragments. J. Gen. Physiol. 133, 231-237.
    • (2009) J. Gen. Physiol. , vol.133 , pp. 231-237
    • Gaudet, R.1
  • 77
    • 33646814436 scopus 로고    scopus 로고
    • KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin
    • Ghosh, S., Nunziato, D. A., and Pitt, G. S. (2006). KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin. Circ. Res. 98, 1048-1054.
    • (2006) Circ. Res. , vol.98 , pp. 1048-1054
    • Ghosh, S.1    Nunziato, D.A.2    Pitt, G.S.3
  • 79
    • 0037472735 scopus 로고    scopus 로고
    • Relevance of the proximal domain in the aminoterminus of HERG channels for regulation by a phospholipase C-coupled hormone receptor
    • Gómez-Varela, D., Barros, F., Viloria, C. G., Giráldez, T., Manso, D. G., Dupuy, S. G., Miranda, P., and de la Peña, P. (2003). Relevance of the proximal domain in the aminoterminus of HERG channels for regulation by a phospholipase C-coupled hormone receptor. FEBS Lett. 535, 125-130.
    • (2003) FEBS Lett , vol.535 , pp. 125-130
    • Gómez-Varela, D.1    Barros, F.2    Viloria, C.G.3    Giráldez, T.4    Manso, D.G.5    Dupuy, S.G.6    Miranda, P.7    de la Peña, P.8
  • 82
    • 33846694346 scopus 로고    scopus 로고
    • Structure prediction for the down state of a potassium channel voltage sensor
    • Grabe, M., Lai, H. C., Jain, M., Jan,Y. N., and Jan, L. Y. (2007). Structure prediction for the down state of a potassium channel voltage sensor. Nature 445, 550-553.
    • (2007) Nature , vol.445 , pp. 550-553
    • Grabe, M.1    Lai, H.C.2    Jain, M.3    Jan, Y.N.4    Jan, L.Y.5
  • 84
    • 69149108876 scopus 로고    scopus 로고
    • A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels
    • Gustina, A. S., and Trudeau, M. C. (2009). A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels. Proc. Natl.Acad. Sci. U.S.A. 106, 13082-13087.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13082-13087
    • Gustina, A.S.1    Trudeau, M.C.2
  • 85
    • 79952120982 scopus 로고    scopus 로고
    • hERG potassium channel gating is mediated by N-and C-terminal region interactions
    • Gustina, A. S., and Trudeau, M. C. (2011). hERG potassium channel gating is mediated by N-and C-terminal region interactions. J. Gen. Physiol. 137, 315-325.
    • (2011) J. Gen. Physiol. , vol.137 , pp. 315-325
    • Gustina, A.S.1    Trudeau, M.C.2
  • 88
    • 44149126774 scopus 로고    scopus 로고
    • The C-terminus of Kv7 channels: a multifunctional module
    • Haitin, Y., and Attali, B. (2008). The C-terminus of Kv7 channels: a multifunctional module. J. Physiol. 586, 1803-1810.
    • (2008) J. Physiol. , vol.586 , pp. 1803-1810
    • Haitin, Y.1    Attali, B.2
  • 91
    • 33744800245 scopus 로고    scopus 로고
    • Modulation of Kv2 1 channel gating and TEA sensitivity by distinct domains of SNAP-25
    • He, Y., Kang, Y., Leung, Y., Xia, F., Gao, X., Xie, H., Gaisano, H. Y., and Tsushima, R. G. (2006). Modulation of Kv2.1 channel gating and TEA sensitivity by distinct domains of SNAP-25. Biochem. J. 396, 363-369.
    • (2006) Biochem. J. , vol.396 , pp. 363-369
    • He, Y.1    Kang, Y.2    Leung, Y.3    Xia, F.4    Gao, X.5    Xie, H.6    Gaisano, H.Y.7    Tsushima, R.G.8
  • 92
    • 45549107093 scopus 로고    scopus 로고
    • Regulation of neural KCNQ channels: signalling pathways, structural motifs and functional implications
    • Hernandez, C. C., Zaika, O., Tolstykh, G. P., and Shapiro, M. S. (2008). Regulation of neural KCNQ channels: signalling pathways, structural motifs and functional implications. J. Physiol. 586, 1811-1821.
    • (2008) J. Physiol. , vol.586 , pp. 1811-1821
    • Hernandez, C.C.1    Zaika, O.2    Tolstykh, G.P.3    Shapiro, M.S.4
  • 93
    • 84866027699 scopus 로고
    • Hille, B. (1992). Ionic Channels of Excitable Membranes. Sunderland, MA: Sinauer.
    • (1992)
    • Hille, B.1
  • 94
    • 0033040717 scopus 로고    scopus 로고
    • N-terminal deletions of rKv1.4 channels affect the voltage dependence of channel availability
    • Höllerer-Beitz, G., Schönherr, R., Koenen, M., and Heinemann, S. H. (1999). N-terminal deletions of rKv1.4 channels affect the voltage dependence of channel availability. Pflügers Arch. 438, 141-146.
    • (1999) Pflügers Arch , vol.438 , pp. 141-146
    • Höllerer-Beitz, G.1    Schönherr, R.2    Koenen, M.3    Heinemann, S.H.4
  • 95
    • 0029783095 scopus 로고    scopus 로고
    • N-type inactivation and the S4-S5 region of the Shaker channel
    • Holmgren, M., Jurman, M. E., and Yellen, G. (1996). N-type inactivation and the S4-S5 region of the Shaker channel. J. Gen. Physiol. 108, 195-206.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 195-206
    • Holmgren, M.1    Jurman, M.E.2    Yellen, G.3
  • 96
    • 0032168179 scopus 로고    scopus 로고
    • + channel can be trapped in the open state by an intersubunit metal bridge
    • + channel can be trapped in the open state by an intersubunit metal bridge. Neuron 21, 617-621.
    • (1998) Neuron , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 97
    • 0030956162 scopus 로고    scopus 로고
    • + channels: evidence for a trap door mechanism of activation gating
    • + channels: evidence for a trap door mechanism of activation gating. J. Gen. Physiol. 109, 527-535.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 527-535
    • Holmgren, M.1    Smith, P.L.2    Yellen, G.3
  • 99
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., Zagotta, W. N., and Aldrich, R. W. (1990). Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250, 533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 100
    • 33847091589 scopus 로고    scopus 로고
    • Structural insight into KCNQ (Kv7) channel assembly and channelopathy
    • Howard, R. J., Clark, K., Holton, J. M., and Minor, D. L. Jr. (2007). Structural insight into KCNQ (Kv7) channel assembly and channelopathy. Neuron 53, 663-675.
    • (2007) Neuron , vol.53 , pp. 663-675
    • Howard, R.J.1    Clark, K.2    Holton, J.M.3    Minor Jr., D.L.4
  • 101
    • 0027146670 scopus 로고
    • Tyrosine kinasedependent suppression of a potassium channel by the G proteincoupled m1 muscarinic acetylcholine receptor
    • Huang, X.-Y., Morielli, A. D., and Peralta, E. G. (1993). Tyrosine kinasedependent suppression of a potassium channel by the G proteincoupled m1 muscarinic acetylcholine receptor. Cell 75,1145-1156.
    • (1993) Cell , vol.75 , pp. 1145-1156
    • Huang, X.-Y.1    Morielli, A.D.2    Peralta, E.G.3
  • 103
    • 0031038307 scopus 로고    scopus 로고
    • + channel inactivation mediated b the concerted action of the cytoplasmic N-and C-terminal domains
    • + channel inactivation mediated b the concerted action of the cytoplasmic N-and C-terminal domains. Biophys. J. 72, 163-174.
    • (1997) Biophys. J. , vol.72 , pp. 163-174
    • Jern, H.H.1    Covarrubias, M.2
  • 105
    • 0031007087 scopus 로고    scopus 로고
    • + channel by β subunit: modulation by a phosphorylation-dependent interaction between the distal C terminus of α subunit and cytoskeleton
    • + channel by β subunit: modulation by a phosphorylation-dependent interaction between the distal C terminus of α subunit and cytoskeleton. J. Bio. Chem. 272, 14021-14024.
    • (1997) J. Bio. Chem. , vol.272 , pp. 14021-14024
    • Jing, J.1    Peretz, T.2    Singer-Lahat, D.3    Chikvashvili, D.4    Thornhill, W.B.5    Lotan, I.6
  • 106
    • 0030176232 scopus 로고    scopus 로고
    • Regulation of potassium channels by protein kinases
    • Jonas, E. A., and Kaczmarek, L. K. (1996). Regulation of potassium channels by protein kinases. Curr. Opin. Neurobiol. 6, 318-323.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 318-323
    • Jonas, E.A.1    Kaczmarek, L.K.2
  • 107
    • 0037968706 scopus 로고    scopus 로고
    • The roles of N-and C-terminal determinants in the activation of the Kv2 1 potassium channel
    • Ju, M., Stevens, L., Leadbitter, E., and Wray, D. (2003). The roles of N-and C-terminal determinants in the activation of the Kv2.1 potassium channel. J. Biol. Chem. 278, 12769-12778.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12769-12778
    • Ju, M.1    Stevens, L.2    Leadbitter, E.3    Wray, D.4
  • 110
    • 0037314677 scopus 로고    scopus 로고
    • Leucine/isoleucine zipper coordination of ion channel macromolecular signaling complexes in the heart: roles in inherited arrhythmias
    • Kass, R. S., Kurokawa, J., Marx, S. O., and Marks, A. R. (2003). Leucine/isoleucine zipper coordination of ion channel macromolecular signaling complexes in the heart: roles in inherited arrhythmias. Trends Cardiovasc. Med. 13, 52-56.
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 52-56
    • Kass, R.S.1    Kurokawa, J.2    Marx, S.O.3    Marks, A.R.4
  • 111
    • 0035936798 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cardiac arrhythmias
    • Keating, M. T., and Sanguinetti, M. C. (2001). Molecular and cellular mechanisms of cardiac arrhythmias. Cell 104, 569-580.
    • (2001) Cell , vol.104 , pp. 569-580
    • Keating, M.T.1    Sanguinetti, M.C.2
  • 112
    • 0034468569 scopus 로고    scopus 로고
    • Regulation of the cardiac repolarizing HERG potassium channel by protein kinase A
    • Kiehn, J. (2000). Regulation of the cardiac repolarizing HERG potassium channel by protein kinase A. Trends Cardiovasc. Med. 10, 205-209.
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 205-209
    • Kiehn, J.1
  • 113
    • 1342333779 scopus 로고    scopus 로고
    • Three-dimensional structure of Ito: Kv4 2-KChIP2 ion channels by electron microscopy at 21 Å resolution
    • Kim, L. A., Furat, J., Gutierrez, D., Butler, M. H., Xu, S., Golstein, S. A. N., and Grigorieff, N. (2004). Three-dimensional structure of Ito: Kv4.2-KChIP2 ion channels by electron microscopy at 21 Å resolution. Neuron 41, 513-519.
    • (2004) Neuron , vol.41 , pp. 513-519
    • Kim, L.A.1    Furat, J.2    Gutierrez, D.3    Butler, M.H.4    Xu, S.5    Golstein, S.A.N.6    Grigorieff, N.7
  • 116
    • 33745838194 scopus 로고    scopus 로고
    • Molecular rearrangements of the Kv2 1 potassium channel termini associated with voltage gating
    • Kobrinsky, E., Stevens, L., Kazmi, Y., and Soldatov, N. M. (2006). Molecular rearrangements of the Kv2.1 potassium channel termini associated with voltage gating. J. Biol. Chem. 281, 19233-19240.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19233-19240
    • Kobrinsky, E.1    Stevens, L.2    Kazmi, Y.3    Soldatov, N.M.4
  • 117
    • 77955731294 scopus 로고    scopus 로고
    • Cysteine 723 in the C-linker segment confers oxidative inhibition of hERG1 potassium channels
    • Kolbe, K., Schönherr, R., Gessner, G., Sahoo, N., Hoshi, T., and Heinemann, S. H. (2010). Cysteine 723 in the C-linker segment confers oxidative inhibition of hERG1 potassium channels. J. Physiol. 588, 2999-3009.
    • (2010) J. Physiol. , vol.588 , pp. 2999-3009
    • Kolbe, K.1    Schönherr, R.2    Gessner, G.3    Sahoo, N.4    Hoshi, T.5    Heinemann, S.H.6
  • 118
    • 0030742577 scopus 로고    scopus 로고
    • + channel, rat Kv1.4, has two potential domains that could produce rapid inactivation
    • + channel, rat Kv1.4, has two potential domains that could produce rapid inactivation. J. Biol. Chem. 272, 19333-19338.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19333-19338
    • Kondoh, S.1    Ishii, K.2    Nakamura, Y.3    Taira, N.4
  • 119
    • 0032580205 scopus 로고    scopus 로고
    • Crystal structure of the tetramerization domain of the Shaker potassium channel
    • Kreusch, A., Pfaffinger, P. J., Stevens, C. F.,and Choe,S. (1998). Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature 392, 945-948.
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 120
    • 11144245528 scopus 로고    scopus 로고
    • KChIP3 rescues the functional expression of Shal channel tetramerization mutants
    • Kunjilwar, K., Strang, C., DeRubeis, D., and Pfaffinger, P. J. (2004). KChIP3 rescues the functional expression of Shal channel tetramerization mutants. J. Biol. Chem. 279, 54542-54551.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54542-54551
    • Kunjilwar, K.1    Strang, C.2    DeRubeis, D.3    Pfaffinger, P.J.4
  • 121
    • 0032538558 scopus 로고    scopus 로고
    • + channel splice variant common in human heart lacks a C-terminal domain required for expression of rapidly activating delayed rectifier current
    • + channel splice variant common in human heart lacks a C-terminal domain required for expression of rapidly activating delayed rectifier current. J. Biol. Chem. 273, 27231-27235.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27231-27235
    • Kupershmidt, S.1    Snyders, D.J.2    Raes, A.3    Roden, D.M.4
  • 122
  • 123
    • 59649096789 scopus 로고    scopus 로고
    • Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by noninteracting residues
    • Labro, A. J., Raes, A. L., Grottesi, A., Van Hoorick, D., Sansom, M. S. P., and Snyders, D. J. (2008). Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by noninteracting residues. J. Gen. Physiol. 132, 667-680.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 667-680
    • Labro, A.J.1    Raes, A.L.2    Grottesi, A.3    Van Hoorick, D.4    Sansom, M.S.P.5    Snyders, D.J.6
  • 126
    • 0028324395 scopus 로고
    • Modulation of ion channels by protein phosphorylation and de phosphorylation
    • Levitan, I. B. (1994). Modulation of ion channels by protein phosphorylation and de phosphorylation. Annu. Rev. Physiol. 56, 193-212.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 193-212
    • Levitan, I.B.1
  • 128
    • 78649713129 scopus 로고    scopus 로고
    • NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker
    • Li, Q., Gayen, S., Chen, A. S., Huang, Q., Raida, M., and Kang, C. (2010). NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker. Biochem. Biophys. Res. Commun. 403, 126-132.
    • (2010) Biochem. Biophys. Res. Commun. , vol.403 , pp. 126-132
    • Li, Q.1    Gayen, S.2    Chen, A.S.3    Huang, Q.4    Raida, M.5    Kang, C.6
  • 129
    • 78651392569 scopus 로고    scopus 로고
    • Intracellular regions of the eag potassium channel play a critical role in generation of voltage-dependent currents
    • Li, Y., Liu, X., Wu, Y., Xu, Z., Li, H., Griffith,L. C.,and Zhou,Y. (2011). Intracellular regions of the eag potassium channel play a critical role in generation of voltage-dependent currents. J. Biol. Chem. 286, 1389-1399.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1389-1399
    • Li, Y.1    Liu, X.2    Wu, Y.3    Xu, Z.4    Li, H.5    Griffith, L.C.6    Zhou, Y.7
  • 130
    • 33646586039 scopus 로고    scopus 로고
    • Voltage-gated potassium channels: regulation by accessory subunits
    • Li, Y., Um, S. Y., and McDonald, T. V. (2006). Voltage-gated potassium channels: regulation by accessory subunits. Neuroscientist. 12, 199-210.
    • (2006) Neuroscientist , vol.12 , pp. 199-210
    • Li, Y.1    Um, S.Y.2    McDonald, T.V.3
  • 131
    • 0038580641 scopus 로고    scopus 로고
    • Negative charges in the transmembrane domains of the HERG K channel are involved in the activation and deactivation gating processes
    • Liu, J., Zhang, M., Jiang, M., and Tseng, G.-N. (2003). Negative charges in the transmembrane domains of the HERG K channel are involved in the activation and deactivation gating processes. J. Gen. Physiol. 121, 599-614.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 599-614
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.-N.4
  • 134
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1 2: structural basis of electromechanical coupling
    • Long, S. B., Campbell, E. B., and Mackinnon, R. (2005b). Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 136
    • 60549089871 scopus 로고    scopus 로고
    • The voltage dependence of hEag currents is not determined solely by membranespanning domains
    • Lörinczi, E., Napp, J., Contreras-Jurado, C., Pardo, L. A., and Stühmer, W. (2009). The voltage dependence of hEag currents is not determined solely by membranespanning domains. Eur. Biophys. J. 38, 279-284.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 279-284
    • Lörinczi, E.1    Napp, J.2    Contreras-Jurado, C.3    Pardo, L.A.4    Stühmer, W.5
  • 140
    • 70350502080 scopus 로고    scopus 로고
    • Rearrangements in the relative orientation of cytoplasmic domains induced by a membraneanchored protein mediate modulations in Kv channel gating
    • Lvov, A., Greitzer, D., Berlin, S., Chikvashvili, D., Tsuk, S., and Lotan, I. (2009). Rearrangements in the relative orientation of cytoplasmic domains induced by a membraneanchored protein mediate modulations in Kv channel gating. J. Biol. Chem. 284, 28276-28291.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28276-28291
    • Lvov, A.1    Greitzer, D.2    Berlin, S.3    Chikvashvili, D.4    Tsuk, S.5    Lotan, I.6
  • 142
    • 0037167878 scopus 로고    scopus 로고
    • Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages
    • Männikkö, R., Elinder, F., and Larsson, H. P. (2002). Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages. Nature 419, 837-841.
    • (2002) Nature , vol.419 , pp. 837-841
    • Männikkö, R.1    Elinder, F.2    Larsson, H.P.3
  • 144
    • 0031835450 scopus 로고    scopus 로고
    • The N-terminus of the K channel KAT1 controls its voltage-dependent gating by altering the membrane electric field
    • Marten, I., and Hoshi, T. (1998). The N-terminus of the K channel KAT1 controls its voltage-dependent gating by altering the membrane electric field. Biophys. J. 74, 2953-2962.
    • (1998) Biophys. J. , vol.74 , pp. 2953-2962
    • Marten, I.1    Hoshi, T.2
  • 145
    • 0037127028 scopus 로고    scopus 로고
    • Requirement of a macromolecular signaling complex for b-adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel
    • Marx, S. O., Kurokawa, J., Reiken, S., Motoike, H., D'Armiento, J., Marks, A. R.,and Kass,R. S. (2002). Requirement of a macromolecular signaling complex for b-adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel. Science 295, 496-499.
    • (2002) Science , vol.295 , pp. 496-499
    • Marx, S.O.1    Kurokawa, J.2    Reiken, S.3    Motoike, H.4    D'Armiento, J.5    Marks, A.R.6    Kass, R.S.7
  • 147
    • 0035425497 scopus 로고    scopus 로고
    • Potassium channels: life in the post-structural world
    • Minor, D. L. Jr. (2001). Potassium channels: life in the post-structural world. Curr. Opin. Struct. Biol. 11, 408-414.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 408-414
    • Minor Jr., D.L.1
  • 148
    • 0034268781 scopus 로고    scopus 로고
    • The polar T1 interface is linked to conformational changes that open the voltagegated potassium channel
    • Minor, D. L., Lin, Y.-F., Mobley, B. C., Avelar, A., Jan, Y. N., Jan, L. Y., and Berger, J. M. (2000). The polar T1 interface is linked to conformational changes that open the voltagegated potassium channel. Cell 102, 657-670.
    • (2000) Cell , vol.102 , pp. 657-670
    • Minor, D.L.1    Lin, Y.-F.2    Mobley, B.C.3    Avelar, A.4    Jan, Y.N.5    Jan, L.Y.6    Berger, J.M.7
  • 151
    • 44949210432 scopus 로고    scopus 로고
    • Interdomain cytoplasmic interactions govern the intracellular trafficking, gating, and modulation of the Kv2 1 channel
    • Mohapatra, D. P., Siino, D. F., and Trimmer, J. S. (2008). Interdomain cytoplasmic interactions govern the intracellular trafficking, gating, and modulation of the Kv2.1 channel. J. Neurosci. 28, 4982-4994.
    • (2008) J. Neurosci. , vol.28 , pp. 4982-4994
    • Mohapatra, D.P.1    Siino, D.F.2    Trimmer, J.S.3
  • 152
    • 32544451419 scopus 로고    scopus 로고
    • The Kv2.1 C terminus can autonomously transfer Kv2.1-like phosphorylation-dependent localization, voltage-dependent gating, and muscarinic modulation to diverse Kv channels
    • Mohapatra, D. P., and Trimmer, J. S. (2006). The Kv2.1 C terminus can autonomously transfer Kv2.1-like phosphorylation-dependent localization, voltage-dependent gating, and muscarinic modulation to diverse Kv channels. J. Neurosci. 26, 685-695.
    • (2006) J. Neurosci. , vol.26 , pp. 685-695
    • Mohapatra, D.P.1    Trimmer, J.S.2
  • 153
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain
    • Morais-Cabral, J. H., Lee, A., Cohen, S. L., Chait, B. T., Li, M., and MacKinnon, R. (1998). Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell 95, 649-655.
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais-Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    MacKinnon, R.6
  • 154
    • 0030729834 scopus 로고    scopus 로고
    • Phosphorylation of the Kv2 1 channel alters voltage-dependent activation
    • Murakoshi,H.,Shi,G.,Scannevin,R. H., and Trimmer, J. S. (1997). Phosphorylation of the Kv2.1 channel alters voltage-dependent activation. Mol. Pharmacol. 52, 821-828.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 821-828
    • Murakoshi, H.1    Shi, G.2    Scannevin, R.H.3    Trimmer, J.S.4
  • 156
    • 79251559440 scopus 로고    scopus 로고
    • The N-terminal tail of hERG contains an amphipathic α-helix that regulates channel deactivation
    • doi:10.1371/journal.pone.0016191
    • Ng, C. A., Hunter, M. J., Perry, M. D., Mobli, M., Ke, Y., Kuchel, P. W., King, G. F., Stock, D., and Vandenberg, J. I. (2011). The N-terminal tail of hERG contains an amphipathic α-helix that regulates channel deactivation. PLoS ONE 6, e16191. doi:10.1371/journal.pone.0016191
    • (2011) PLoS ONE , vol.6
    • Ng, C.A.1    Hunter, M.J.2    Perry, M.D.3    Mobli, M.4    Ke, Y.5    Kuchel, P.W.6    King, G.F.7    Stock, D.8    Vandenberg, J.I.9
  • 157
    • 68949118408 scopus 로고    scopus 로고
    • Coupling of S4 helix translocation and S6 gating analyzed by molecular-dynamics simulations and mutated Kv channels
    • Nishizawa, M., and Nishizawa, K. (2009). Coupling of S4 helix translocation and S6 gating analyzed by molecular-dynamics simulations and mutated Kv channels. Biophys. J. 97, 90-100.
    • (2009) Biophys. J. , vol.97 , pp. 90-100
    • Nishizawa, M.1    Nishizawa, K.2
  • 158
    • 77952403905 scopus 로고    scopus 로고
    • Potassium channel gating: not an open and shut case
    • Norton, R. S., and Gulbis, J. M. (2010). Potassium channel gating: not an open and shut case. Proc. Natl. Acad. Sci. U.S.A. 107, 7623-7624.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 7623-7624
    • Norton, R.S.1    Gulbis, J.M.2
  • 160
    • 0034100735 scopus 로고    scopus 로고
    • HERG-like potassium current regulates the resting membrane potential in glomus cells of the rabbit carotid body
    • Overholt, J. L., Ficker, E., Yang, T., Shams, H., Bright, G. R., and Prabhakar, N. R. (2000). HERG-like potassium current regulates the resting membrane potential in glomus cells of the rabbit carotid body. J. Neurophysiol. 83, 1150-1157.
    • (2000) J. Neurophysiol. , vol.83 , pp. 1150-1157
    • Overholt, J.L.1    Ficker, E.2    Yang, T.3    Shams, H.4    Bright, G.R.5    Prabhakar, N.R.6
  • 161
  • 162
    • 17644388821 scopus 로고    scopus 로고
    • Impaired KCNQ1-KCNE1 and Phosphatidylinositol-4 5-bisphosphate interaction underlies the long QT syndrome
    • Park, K. H., Piron, J., Dahimene, S., Merot, J., Baro, I., Escande, D., and Loussouarn, G. (2005). Impaired KCNQ1-KCNE1 and Phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome. Circ. Res. 96, 730-739.
    • (2005) Circ. Res. , vol.96 , pp. 730-739
    • Park, K.H.1    Piron, J.2    Dahimene, S.3    Merot, J.4    Baro, I.5    Escande, D.6    Loussouarn, G.7
  • 163
    • 36749003075 scopus 로고    scopus 로고
    • Proteomic analysis of Kv2 1 channel phosphorylation sites determining cell background specific differences in function
    • Park, K.-S., Mohapatra, D. P., and Trimmer, J. S. (2007). Proteomic analysis of Kv2.1 channel phosphorylation sites determining cell background specific differences in function. Channels 1, 59-61.
    • (2007) Channels , vol.1 , pp. 59-61
    • Park, K.-S.1    Mohapatra, D.P.2    Trimmer, J.S.3
  • 164
    • 40349089867 scopus 로고    scopus 로고
    • Potassium channel phosphorylation in excitable cells: providing dynamic functional variability to a diverse family of ion channels
    • Park, K.-S., Yang, J.-W., Seikel, E., and Trimmer, J. S. (2008). Potassium channel phosphorylation in excitable cells: providing dynamic functional variability to a diverse family of ion channels. Physiology 23, 49-57.
    • (2008) Physiology , vol.23 , pp. 49-57
    • Park, K.-S.1    Yang, J.-W.2    Seikel, E.3    Trimmer, J.S.4
  • 165
    • 0031306025 scopus 로고    scopus 로고
    • Contribution of the NH2 terminus of Kv2 1 to channel activation
    • Pascual, J. M., Shieh, C.-C. Kirsch, G. E., and Brown, A. M. (1997). Contribution of the NH2 terminus of Kv2.1 to channel activation. Am. J. Physiol. 273, C1849-C1858.
    • (1997) Am. J. Physiol. , vol.273
    • Pascual, J.M.1    Shieh, C.-C.2    Kirsch, G.E.3    Brown, A.M.4
  • 167
    • 33750594842 scopus 로고    scopus 로고
    • Three-dimensional structure of the KchIP1-Kv4 3 T1 complex reveals a cross-shaped octamer
    • Pioletti, M., Findeisen, F., Hura, G. L., and Minor, D. L. Jr. (2006). Three-dimensional structure of the KchIP1-Kv4.3 T1 complex reveals a cross-shaped octamer. Nat. Struct. Mol. Biol. 13, 987-995.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 987-995
    • Pioletti, M.1    Findeisen, F.2    Hura, G.L.3    Minor Jr., D.L.4
  • 168
  • 169
    • 60549107301 scopus 로고    scopus 로고
    • The domain and conformational organization in potassium voltage-gated ion channels
    • Pischalnikova, A. V., and Sokolova, O. S. (2009). The domain and conformational organization in potassium voltage-gated ion channels. J. Neuroimmune Pharmacol. 4, 71-82.
    • (2009) J. Neuroimmune Pharmacol. , vol.4 , pp. 71-82
    • Pischalnikova, A.V.1    Sokolova, O.S.2
  • 172
    • 33748125213 scopus 로고    scopus 로고
    • Reversal of HCN channel voltage dependence via bridging of the S4-S5 linker and post-S6
    • Prole, D.L., and Yellen,G. (2006). Reversal of HCN channel voltage dependence via bridging of the S4-S5 linker and post-S6. J. Gen. Physiol. 128, 273-282.
    • (2006) J. Gen. Physiol. , vol.128 , pp. 273-282
    • Prole, D.L.1    Yellen, G.2
  • 174
    • 0344492207 scopus 로고    scopus 로고
    • Relationships between preclinical cardiac electrophysiology, clinical QT interval prolongation and torsade de pointes for a broad range of drugs: evidence for a provisional safety margin in drug development
    • Redfern, W. S., Carlsson, L., Davis, A. S., Lynch, W. G., MacKenzie, I., Palethorpe, S., Siegl, P. K. S., Strang, I., Sullivan, A. T., Wallis, R., Camm, A. J., and Hammond, T. G. (2002). Relationships between preclinical cardiac electrophysiology, clinical QT interval prolongation and torsade de pointes for a broad range of drugs: evidence for a provisional safety margin in drug development. Cardiovasc. Res. 58, 32-45.
    • (2002) Cardiovasc. Res. , vol.58 , pp. 32-45
    • Redfern, W.S.1    Carlsson, L.2    Davis, A.S.3    Lynch, W.G.4    MacKenzie, I.5    Palethorpe, S.6    Siegl, P.K.S.7    Strang, I.8    Sullivan, A.T.9    Wallis, R.10    Camm, A.J.11    Hammond, T.G.12
  • 175
    • 23644450590 scopus 로고    scopus 로고
    • Genetics of acquired long QT syndrome
    • Roden, D. M., and Viswanathan, P. C. (2005). Genetics of acquired long QT syndrome. J. Clin. Invest. 115, 2025-2032.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2025-2032
    • Roden, D.M.1    Viswanathan, P.C.2
  • 176
    • 0032556879 scopus 로고    scopus 로고
    • NIP domain prevents N-type inactivation in voltage-gated potassium channels
    • Roeper, J., Sewing, S., Zhang, Y., Sommer, T., Wanner, S. G., and Pongs, O. (1998). NIP domain prevents N-type inactivation in voltage-gated potassium channels. Nature 391, 390-393.
    • (1998) Nature , vol.391 , pp. 390-393
    • Roeper, J.1    Sewing, S.2    Zhang, Y.3    Sommer, T.4    Wanner, S.G.5    Pongs, O.6
  • 179
    • 0025925342 scopus 로고
    • Cloned neuronal IK(A) channels reopen during recovery from inactivation
    • Ruppersberg, J. P., Frank, R., Pongs, O., and Stocker, M. (1991). Cloned neuronal IK(A) channels reopen during recovery from inactivation. Nature 353, 657-660.
    • (1991) Nature , vol.353 , pp. 657-660
    • Ruppersberg, J.P.1    Frank, R.2    Pongs, O.3    Stocker, M.4
  • 180
    • 33845383109 scopus 로고    scopus 로고
    • Modulation of HERG gating by a charge cluster in the N-terminal proximal domain
    • Saenen, J. B., Labro, A. J., Raes, A., and Snyders, D. J. (2006). Modulation of HERG gating by a charge cluster in the N-terminal proximal domain. Biophys. J. 91, 4381-4391.
    • (2006) Biophys. J. , vol.91 , pp. 4381-4391
    • Saenen, J.B.1    Labro, A.J.2    Raes, A.3    Snyders, D.J.4
  • 181
    • 0029002969 scopus 로고
    • A mechanistic link between an inherited and an acquired cardiac arrhythmia
    • Sanguinetti, M. C, Jiang, C, Curran, M. E., and Keating, M. T. (1995). A mechanistic link between an inherited and an acquired cardiac arrhythmia. Cell 81, 299-307.
    • (1995) Cell , vol.81 , pp. 299-307
    • Sanguinetti, M.C.1    Jiang, C.2    Curran, M.E.3    Keating, M.T.4
  • 182
    • 28544432686 scopus 로고    scopus 로고
    • N type rapid inactivation in human Kv1 4 channels: functional role of a putative C-terminal helx
    • Sankaranarayanan, K.,Varshney,A., and Mathew, M. K. (2005). N type rapid inactivation in human Kv1.4 channels: functional role of a putative C-terminal helx. Mol. Membr. Biol. 22, 389-400.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 389-400
    • Sankaranarayanan, K.1    Varshney, A.2    Mathew, M.K.3
  • 185
  • 186
    • 0030054878 scopus 로고    scopus 로고
    • Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel
    • Schönherr, R., and Heinemann, S. H. (1996). Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel. J. Physiol. 493, 635-642.
    • (1996) J. Physiol. , vol.493 , pp. 635-642
    • Schönherr, R.1    Heinemann, S.H.2
  • 189
    • 0032476018 scopus 로고    scopus 로고
    • Subunit folding and assembly steps are interspersed during Shaker potassium channel biogenesis
    • Schulteis, C. T., Nagaya, N., and Papazian, D. M. (1998). Subunit folding and assembly steps are interspersed during Shaker potassium channel biogenesis. J. Biol. Chem. 273, 26210-26217.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26210-26217
    • Schulteis, C.T.1    Nagaya, N.2    Papazian, D.M.3
  • 190
    • 79955011398 scopus 로고    scopus 로고
    • Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel
    • Schünke, S., Stoldt, M., Lecher, J., Kaupp, U. B., and Willbold, D. (2011). Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. Proc. Natl. Acad. Sci. U.S.A. 108, 6121-6126.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6121-6126
    • Schünke, S.1    Stoldt, M.2    Lecher, J.3    Kaupp, U.B.4    Willbold, D.5
  • 192
    • 28044453940 scopus 로고    scopus 로고
    • Expression of a calmodulinbinding KCNQ2 potassium channel fragment modulates neuronal M-current and membrane excitability
    • Shahidullah, M., Santarelli, L. C., Wen, H., and Levitan, I. B. (2005). Expression of a calmodulinbinding KCNQ2 potassium channel fragment modulates neuronal M-current and membrane excitability. Proc. Natl. Acad. Sci. U.S.A. 102, 16454-16459.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16454-16459
    • Shahidullah, M.1    Santarelli, L.C.2    Wen, H.3    Levitan, I.B.4
  • 193
    • 33646810883 scopus 로고    scopus 로고
    • Calmodulin is essential for cardiac IKS channel gating and assembly: impaired function in long-QT mutations
    • Shamgar, L., Ma, L., Schmitt, N., Haitin, Y., Peretz, A., Wiener, R., Hirsch, J., Pongs, O., and Atali, B. (2006). Calmodulin is essential for cardiac IKS channel gating and assembly: impaired function in long-QT mutations. Circ. Res. 98, 1055-1063.
    • (2006) Circ. Res. , vol.98 , pp. 1055-1063
    • Shamgar, L.1    Ma, L.2    Schmitt, N.3    Haitin, Y.4    Peretz, A.5    Wiener, R.6    Hirsch, J.7    Pongs, O.8    Atali, B.9
  • 194
    • 0030025308 scopus 로고    scopus 로고
    • The inward rectification mechanism of the HERG cardiac potassium channel
    • Smith, P. L., Baukrowitz, T., and Yellen, G. (1996). The inward rectification mechanism of the HERG cardiac potassium channel. Nature 379, 833-836.
    • (1996) Nature , vol.379 , pp. 833-836
    • Smith, P.L.1    Baukrowitz, T.2    Yellen, G.3
  • 195
    • 0036097030 scopus 로고    scopus 로고
    • Fast and slow voltage sensor movements in HERG potassium channels
    • Smith, P. L., and Yellen, G. (2002). Fast and slow voltage sensor movements in HERG potassium channels. J. Gen. Physiol. 119, 275-293.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 275-293
    • Smith, P.L.1    Yellen, G.2
  • 197
    • 0035078574 scopus 로고    scopus 로고
    • Threedimensional structure of a voltagegated potassium channel at 2 5 nm resolution
    • Sokolova, O., Kolmakova-Partensky, L., and Grigorieff, N. (2001). Threedimensional structure of a voltagegated potassium channel at 2.5 nm resolution. Structure 9, 215-220.
    • (2001) Structure , vol.9 , pp. 215-220
    • Sokolova, O.1    Kolmakova-Partensky, L.2    Grigorieff, N.3
  • 199
    • 62949118937 scopus 로고    scopus 로고
    • Roles of surface residues of intracellular domains of heag potassium channels
    • Stevens, L., Ju, M., and Wray, D. (2009). Roles of surface residues of intracellular domains of heag potassium channels. Eur. Biophys. J. 38, 523-532.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 523-532
    • Stevens, L.1    Ju, M.2    Wray, D.3
  • 200
    • 4344686915 scopus 로고    scopus 로고
    • Molecular basis of slow activation of the human ether-á-go-go related gene potassium channel
    • Subbiah, R. N., Clarke, C. E., Smith, D. J., Zhao, J., Campbell, T. J., and Vandenberg, J. I. (2004). Molecular basis of slow activation of the human ether-á-go-go related gene potassium channel. J. Physiol. 558, 417-431.
    • (2004) J. Physiol. , vol.558 , pp. 417-431
    • Subbiah, R.N.1    Clarke, C.E.2    Smith, D.J.3    Zhao, J.4    Campbell, T.J.5    Vandenberg, J.I.6
  • 202
    • 20444428008 scopus 로고    scopus 로고
    • Regulation of ion channels by phosphatidylinositol 4
    • Suh, B., and Hille, B. (2005). Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Neurobiol. 15, 1-9.
    • (2005) 5-bisphosphate. Curr. Opin. Neurobiol. , vol.15 , pp. 1-9
    • Suh, B.1    Hille, B.2
  • 203
    • 29144477159 scopus 로고    scopus 로고
    • Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels
    • Surti, T. S., Huang, L., Jan, Y. N., Jan, L. Y., and Cooper, E. C. (2005). Identification by mass spectrometry and functional characterization of two phosphorylation sites of KCNQ2/KCNQ3 channels. Proc. Natl. Acad. Sci. U.S.A. 102, 17828-17833.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17828-17833
    • Surti, T.S.1    Huang, L.2    Jan, Y.N.3    Jan, L.Y.4    Cooper, E.C.5
  • 204
    • 9944226711 scopus 로고    scopus 로고
    • Towards a structural view of gating in potassium channels
    • Swartz, K. J. (2004). Towards a structural view of gating in potassium channels. Nat. Rev. Neurosci. 5, 905-916.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 905-916
    • Swartz, K.J.1
  • 205
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K. J. (2008). Sensing voltage across lipid membranes. Nature 456, 891-897.
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 206
    • 34548499865 scopus 로고    scopus 로고
    • Structural dynamics in the gating ring of cyclic nucleotidegated ion channels
    • Taraska, J. W., and Zagotta, W. N. (2007). Structural dynamics in the gating ring of cyclic nucleotidegated ion channels. Nat. Struct. Mol. Biol. 14, 854-860.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 854-860
    • Taraska, J.W.1    Zagotta, W.N.2
  • 207
    • 0030859332 scopus 로고    scopus 로고
    • Amino terminal-dependent gating of the potassium channel rat eag is compensated by a mutation in the S4 segment
    • Terlau, H., Heinemann, S. H., Stühmer, W., Pongs, O., and Ludwig, J. (1997). Amino terminal-dependent gating of the potassium channel rat eag is compensated by a mutation in the S4 segment. J. Physiol. 502, 537-543.
    • (1997) J. Physiol. , vol.502 , pp. 537-543
    • Terlau, H.1    Heinemann, S.H.2    Stühmer, W.3    Pongs, O.4    Ludwig, J.5
  • 209
    • 0033600758 scopus 로고    scopus 로고
    • Deletion of protein kinase A phosphorylation sites in the HERG potassium channel inhibits activation shift by protein kinase A
    • Thomas, D., Zhang, W., Karle, C. A., Kathöfer, S., Schöls, W., Kübler, W., and Kiehn, J. (1999). Deletion of protein kinase A phosphorylation sites in the HERG potassium channel inhibits activation shift by protein kinase A. J. Biol. Chem. 274, 27457-27462.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27457-27462
    • Thomas, D.1    Zhang, W.2    Karle, C.A.3    Kathöfer, S.4    Schöls, W.5    Kübler, W.6    Kiehn, J.7
  • 212
    • 0029007356 scopus 로고
    • HERG, a human inward rectifier in the voltage-gated potassium channel family
    • Trudeau, M. C., Warmke, J. W., Ganetzky, B., and Robertson, G. A. (1995). HERG, a human inward rectifier in the voltage-gated potassium channel family. Science 269, 92-95.
    • (1995) Science , vol.269 , pp. 92-95
    • Trudeau, M.C.1    Warmke, J.W.2    Ganetzky, B.3    Robertson, G.A.4
  • 213
    • 0033521647 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase α participates in the m1 muscarinic acetylcholine receptordependent regulation of Kv1 2 channel activity
    • Tsai, W., Morielli, A. D., Cachero, T. G., and Peralta, E. G. (1999). Receptor protein tyrosine phosphatase α participates in the m1 muscarinic acetylcholine receptordependent regulation of Kv1.2 channel activity. EMBO J. 18, 109-118.
    • (1999) EMBO J , vol.18 , pp. 109-118
    • Tsai, W.1    Morielli, A.D.2    Cachero, T.G.3    Peralta, E.G.4
  • 215
    • 80054717695 scopus 로고    scopus 로고
    • Diverse roles for auxiliary subunits in phosphorylation-dependent regulation of mammalian brain voltage-gated potassium channels
    • Vacher, H., and Trimmer, J. S. (2011). Diverse roles for auxiliary subunits in phosphorylation-dependent regulation of mammalian brain voltage-gated potassium channels. Pflügers Arch. 462, 631-643.
    • (2011) Pflügers Arch , vol.462 , pp. 631-643
    • Vacher, H.1    Trimmer, J.S.2
  • 217
    • 3142704245 scopus 로고    scopus 로고
    • Arranging the elements of the potassium channel: the T1 domain occludes the cytoplasmic face of the channel
    • Varhsney, A., Chanda, B., and Mathew, M. K. (2004). Arranging the elements of the potassium channel: the T1 domain occludes the cytoplasmic face of the channel. Eur. Biophys. J. 33, 370-376.
    • (2004) Eur. Biophys. J. , vol.33 , pp. 370-376
    • Varhsney, A.1    Chanda, B.2    Mathew, M.K.3
  • 219
    • 0346041553 scopus 로고    scopus 로고
    • S4 movement in a mammalian HCN channel
    • Vemana, S., Pandey, S., and Larsson, H. P. (2004). S4 movement in a mammalian HCN channel. J. Gen. Physiol. 123, 21-32.
    • (2004) J. Gen. Physiol. , vol.123 , pp. 21-32
    • Vemana, S.1    Pandey, S.2    Larsson, H.P.3
  • 221
    • 0033530381 scopus 로고    scopus 로고
    • Long QT syndromes and torsade de pointes
    • Viskin, S. (1999). Long QT syndromes and torsade de pointes. Lancet 354, 1625-1633.
    • (1999) Lancet , vol.354 , pp. 1625-1633
    • Viskin, S.1
  • 222
    • 78650973241 scopus 로고    scopus 로고
    • Mapping the sequence of conformational changes underlying selectivity filter gating in the Kv11 1 potassium channel
    • Wang, D. T., Hill, A. P., Mann, S. A., Tan, P. S., and Vandenberg, J. I. (2011). Mapping the sequence of conformational changes underlying selectivity filter gating in the Kv11.1 potassium channel. Nat. Struct. Mol. Biol. 18, 35-41.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 35-41
    • Wang, D.T.1    Hill, A.P.2    Mann, S.A.3    Tan, P.S.4    Vandenberg, J.I.5
  • 224
    • 22244469050 scopus 로고    scopus 로고
    • Functionally active T1-T1 interfaces revealed by the accessibility of intracellular thiolate groups in Kv4 channels
    • Wang, G., Shahidullah, M., Rocha, C. A., Strang, C., Pfaffinger, P. J., and Covarrubias, M. (2005). Functionally active T1-T1 interfaces revealed by the accessibility of intracellular thiolate groups in Kv4 channels. J. Gen. Physiol. 126, 55-69.
    • (2005) J. Gen. Physiol. , vol.126 , pp. 55-69
    • Wang, G.1    Shahidullah, M.2    Rocha, C.A.3    Strang, C.4    Pfaffinger, P.J.5    Covarrubias, M.6
  • 226
    • 0031742141 scopus 로고    scopus 로고
    • Regulation of deactivation by an amino terminal domain in human ether-a-gogo-related gene potassium channels
    • Wang, J., Trudeau, M. C., Zappia, A. M., and Robertson,G.A. (1998). Regulation of deactivation by an amino terminal domain in human ether-a-gogo-related gene potassium channels. J. Gen. Physiol. 112, 637-647.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 637-647
    • Wang, J.1    Trudeau, M.C.2    Zappia, A.M.3    Robertson, G.A.4
  • 227
    • 70249124205 scopus 로고    scopus 로고
    • Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
    • Wang, L., and Sigworth, F. J. (2009). Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 461, 242-245.
    • (2009) Nature , vol.461 , pp. 242-245
    • Wang, L.1    Sigworth, F.J.2
  • 228
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to eag in Drosophila and mammals
    • Warmke, J. W., and Ganetzky, B. (1994). A family of potassium channel genes related to eag in Drosophila and mammals. Proc. Natl. Acad. Sci. U.S.A. 91, 3438-3442.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3438-3442
    • Warmke, J.W.1    Ganetzky, B.2
  • 230
    • 0037107123 scopus 로고    scopus 로고
    • Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels
    • Wen, H., and Levitan, I. B. (2002). Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels. J. Neurosci. 22, 7991-8001.
    • (2002) J. Neurosci. , vol.22 , pp. 7991-8001
    • Wen, H.1    Levitan, I.B.2
  • 231
    • 0037025337 scopus 로고    scopus 로고
    • Calcium/calmodulindependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel
    • Whang, Z., Wilson, G. F., and Griffith, L. C. (2002). Calcium/calmodulindependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel. J. Biol. Chem. 277, 24022-24029.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24022-24029
    • Whang, Z.1    Wilson, G.F.2    Griffith, L.C.3
  • 233
    • 0038182556 scopus 로고    scopus 로고
    • Solution structure and function of the " tandem inactivation domain" of the neuronal A-type potassium channel Kv1
    • Wissmann, R., Bildl, W., Oliver, D., Beyermann, M., Kalbitzer, H. R., Bentrop, D., and Fakler, B. (2003). Solution structure and function of the " tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4. J. Biol. Chem. 278, 16142-16150.
    • (2003) 4. J. Biol. Chem. , vol.278 , pp. 16142-16150
    • Wissmann, R.1    Bildl, W.2    Oliver, D.3    Beyermann, M.4    Kalbitzer, H.R.5    Bentrop, D.6    Fakler, B.7
  • 234
    • 60549108756 scopus 로고    scopus 로고
    • Intracellular regions of potassium channels: Kv2 1 and heag
    • Wray, D. (2009). Intracellular regions of potassium channels: Kv2.1 and heag. Eur. Biophys. J. 38, 285-292.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 285-292
    • Wray, D.1
  • 235
    • 73449119314 scopus 로고    scopus 로고
    • Voltage-gated potassium channels as therapeutic targets
    • Wulff, H., Castle, N. A., and Pardo, L. A. (2009). Voltage-gated potassium channels as therapeutic targets. Nat. Rev. Drug Disc. 8, 982-1001.
    • (2009) Nat. Rev. Drug Disc. , vol.8 , pp. 982-1001
    • Wulff, H.1    Castle, N.A.2    Pardo, L.A.3
  • 238
    • 78649403213 scopus 로고    scopus 로고
    • Kinesin I transports tetramerized Kv3 channels through the axon initial segment via direct binding
    • Xu, M., Gu, Y., Barry, J., and Gu, C. (2010). Kinesin I transports tetramerized Kv3 channels through the axon initial segment via direct binding. J. Neurosci. 30, 15987-16001.
    • (2010) J. Neurosci. , vol.30 , pp. 15987-16001
    • Xu, M.1    Gu, Y.2    Barry, J.3    Gu, C.4
  • 240
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • Yellen, G. (1998). The moving parts of voltage-gated ion channels. Q. Rev. Biophys. 31, 239-295.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 239-295
    • Yellen, G.1
  • 241
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen, G. (2002). The voltage-gated potassium channels and their relatives. Nature 419, 35-42.
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 242
    • 29844433234 scopus 로고    scopus 로고
    • Overview of molecular relationships in the voltage-gated ion channel superfamily
    • Yu, F. H., Yarov-Yarovoy, V., Gutman, G. A., and Catterall, W. A. (2005). Overview of molecular relationships in the voltage-gated ion channel superfamily. Pharmacol. Rev. 57, 387-395.
    • (2005) Pharmacol. Rev. , vol.57 , pp. 387-395
    • Yu, F.H.1    Yarov-Yarovoy, V.2    Gutman, G.A.3    Catterall, W.A.4
  • 243
    • 0037047394 scopus 로고    scopus 로고
    • The identification and characterization of noncontinuous calmodulinbinding site in noninactivating voltage-dependent KCNQ potassium channels
    • Yus-Nájera, E., Santana-Castro, I., and Villarroel, A. (2002). The identification and characterization of noncontinuous calmodulinbinding site in noninactivating voltage-dependent KCNQ potassium channels. J. Biol. Chem. 277, 28545-28553.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28545-28553
    • Yus-Nájera, E.1    Santana-Castro, I.2    Villarroel, A.3
  • 245
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta, W. N., Olivier, N. B., Black, K. D., Young, E. C., Olson, R., and Gouaux, E. (2003). Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425, 200-205.
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 246
    • 0037468826 scopus 로고    scopus 로고
    • PIP2 activates KCNQ channels, and its hydrolysis underlies receptormediated inhibition of M currents
    • Zhang, H., Craciun, L. C., Mirshahi, T., Rohács, T., Lopes, C. M. B., Jin, T., and Logothetis, D. E. (2003). PIP2 activates KCNQ channels, and its hydrolysis underlies receptormediated inhibition of M currents. Neuron 37, 963-975.
    • (2003) Neuron , vol.37 , pp. 963-975
    • Zhang, H.1    Craciun, L.C.2    Mirshahi, T.3    Rohács, T.4    Lopes, C.M.B.5    Jin, T.6    Logothetis, D.E.7
  • 247
    • 33645122652 scopus 로고    scopus 로고
    • Interactions between charged residues in the transmembrane segments of the voltage-sensing domain in the hERG channel
    • Zhang, M., Liu, J., Jiang, M., Wu, D.-M., Sonawane, K., Guy, H. R., and Tseng, G.-N. (2005). Interactions between charged residues in the transmembrane segments of the voltage-sensing domain in the hERG channel. J. Membr. Biol. 207, 169-181.
    • (2005) J. Membr. Biol. , vol.207 , pp. 169-181
    • Zhang, M.1    Liu, J.2    Jiang, M.3    Wu, D.-M.4    Sonawane, K.5    Guy, H.R.6    Tseng, G.-N.7
  • 248
    • 10344246598 scopus 로고    scopus 로고
    • Gating charges in the activation and inactivation processes of the HERG channel
    • Zhang, M., Liu, J., and Tseng, G.-N. (2004). Gating charges in the activation and inactivation processes of the HERG channel. J. Gen. Physiol. 124, 703-718.
    • (2004) J. Gen. Physiol. , vol.124 , pp. 703-718
    • Zhang, M.1    Liu, J.2    Tseng, G.-N.3
  • 249
  • 250
    • 77953412214 scopus 로고    scopus 로고
    • Analysis of the interactions between the C-terminal cytoplasmic domains of KCNQ1 and KCNE1 channel subunits
    • Zheng, R., Thompson, K., Obeng-Gymah, E., Alessi, D., Chen, J., Cheng, H., and McDonald, T. V. (2010). Analysis of the interactions between the C-terminal cytoplasmic domains of KCNQ1 and KCNE1 channel subunits. Biochem. J. 428, 75-84.
    • (2010) Biochem. J. , vol.428 , pp. 75-84
    • Zheng, R.1    Thompson, K.2    Obeng-Gymah, E.3    Alessi, D.4    Chen, J.5    Cheng, H.6    McDonald, T.V.7
  • 251
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou, M., Morais-Cabral, J. H., Mann, S., and MacKinnon, R. (2001). Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature 411, 657-661.
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 252
    • 77953722106 scopus 로고    scopus 로고
    • A twist on potassium channel gating
    • Zhou, W., and Jan, L. (2010). A twist on potassium channel gating. Cell 141, 920-922.
    • (2010) Cell , vol.141 , pp. 920-922
    • Zhou, W.1    Jan, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.