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Volumn 136, Issue 2, 2010, Pages 203-224

Modification of hERG1 channel gating by Cd2+

Author keywords

[No Author keywords available]

Indexed keywords

CADMIUM; COBALT; KCNH1 PROTEIN, HUMAN; LANTHANUM; PIPERIDINE DERIVATIVE; POTASSIUM CHANNEL HERG; QUINOLINE DERIVATIVE; RPR260243; ZINC; 4 [3 (6 METHOXY 4 QUINOLINYL) 3 OXOPROPYL] 1 [3 (2,3,5 TRIFLUOROPHENYL) 2 PROPYNYL] 3 PIPERIDINECARBOXYLIC ACID;

EID: 77955044096     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201010450     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4 segment; to gating charge in the Shaker K+ channel
    • doi:10.1016/S0896-6273(00)80143-9
    • Aggarwal, S.K., and R. MacKinnon. 1996. Contribution of the S4 segment; to gating charge in the Shaker K+ channel. Neuron. 16:1169-1177. doi:10.1016/S0896-6273(00)80143-9
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 2
    • 25644437209 scopus 로고    scopus 로고
    • Focused electric field across the voltage sensor of potassium channels
    • doi:10.1016/j.neuron.2005.08.020
    • Altern, C.A., and R. Horn. 2005. Focused electric field across the voltage sensor of potassium channels. Neuron. 48:25-29. doi:10.1016/j.neuron. 2005.08.020
    • (2005) Neuron. , vol.48 , pp. 25-29
    • Altern, C.A.1    Horn, R.2
  • 3
    • 0033014675 scopus 로고    scopus 로고
    • Proton and zinc effects on HERG currents
    • doi:10.1.016/S0006-3495(99)76889-X
    • Anumonwo, J.M.J. Horta, M. Delmar, S.M. Tafret, and J. Jalife. 1999. Proton and zinc effects on HERG currents. Biophys. J. 77:282-298. doi:10.1.016/S0006-3495(99)76889-X
    • (1999) Biophys. J. , vol.77 , pp. 282-298
    • Horta, A.J.M.J.1    Delmar, M.2    Tafret, S.M.3    Jalife, J.4
  • 4
    • 0017743723 scopus 로고
    • Inactivation of the sodium channel. II. Gating current experiments
    • doi:10.1085/jgp.70.5.567
    • Armstrong, C.M., and F. Bezanilla. 1977. Inactivation of the sodium channel. II. Gating current experiments. J. Gen. Physiol. 70:567-590. doi:10.1085/jgp.70.5.567
    • (1977) J. Gen. Physiol. , vol.70 , pp. 567-590
    • Armstrong, C.M.1    Bezanilla, F.2
  • 5
    • 0032763120 scopus 로고    scopus 로고
    • 2+and other divalent cations
    • doi:10.1085/jgp.114.6.819
    • 2+ and other divalent cations. J. Gen. Physiol. 114:819-838. doi:10.1085/jgp.114.6.819
    • (1999) J. Gen. Physiol. , vol.114 , pp. 819-838
    • Cherny, V.V.1    DeCoursey, T.E.2
  • 6
    • 0028914969 scopus 로고
    • A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome
    • doi:10.10.16/0092-8674(95)90358-5
    • Curran, M.E., I. Splawski, K.W. Timothy, G.M. Vincent, E.D. Green, and M.T. Keating. 1995. A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell. 80:795-803. doi:10.10.16/0092-8674(95)90358-5
    • (1995) Cell. , vol.80 , pp. 795-803
    • Curran, M.E.1    Splawski, I.2    Timothy, K.W.3    Vincent, G.M.4    Green, E.D.5    Keating, M.T.6
  • 7
    • 54449100445 scopus 로고    scopus 로고
    • Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation
    • doi:10.1073/pnas.0806486105
    • DeCaen, P.G., V. Yarov-Yarovoy, Y. Zhao, T. Scheuer, and W.A. Catterall. 2008. Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation. Proc. Natl. Acad. Sci. USA. 105:15142-15147. doi:10.1073/pnas.0806486105
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15142-15147
    • DeCaen, P.G.1    Yarov-Yarovoy, V.2    Zhao, Y.3    Scheuer, T.4    Catterall, W.A.5
  • 8
    • 76049115811 scopus 로고    scopus 로고
    • Sequential formation of ion pairs during activation of a sodium channel voltage sensor
    • doi:10.1073/pnas.0912307.106
    • DeCaen, P.G., V. Yarov-Yarovoy, E.M. Sharp, T. Scheuer, and W.A. Catterall. 2009. Sequential formation of ion pairs during activation of a sodium channel voltage sensor. Proc. Natl. Acad. Sci. USA. 106:22498-22503. doi:10.1073/pnas.0912307.106
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 22498-22503
    • DeCaen, P.G.1    Yarov-Yarovoy, V.2    Sharp, E.M.3    Scheuer, T.4    Catterall, W.A.5
  • 9
    • 25844437886 scopus 로고    scopus 로고
    • 2+-induced modification of human ether-à-go-go-related gene (hERG) channel activation
    • doi:10.1113/jphysiol.2005.089094
    • 2+-induced modification of human ether-à-go-go-related gene (hERG) channel activation. J. Physiol. 567:737-755. doi:10.1113/jphysiol.2005.089094
    • (2005) J. Physiol. , vol.567 , pp. 737-755
    • Fernandez, D.1    Chanta, A.2    Kinard, K.I.3    Sanguinetti, M.C.4
  • 14
    • 0032750066 scopus 로고    scopus 로고
    • 2+) destabilization of the inactivated state
    • doi:10.1016/S0006-3495(99)77088-8
    • 2+) destabilization of the inactivated state. Biophys. J. 77:2534-2541. doi:10.1016/S0006-3495(99)77088-8
    • (1999) Biophys. J. , vol.77 , pp. 2534-2541
    • Johnson Jr., J.R.1    Baiser, J.R.2    Bennett, P.B.3
  • 16
    • 0035875963 scopus 로고    scopus 로고
    • A novel extracellular calcium sensing mechanism in voltage-gated potassium ion channels
    • Johnson, J.P. Jr., J.R. Baiser, and P.B. Bennett. 2001. A novel extracellular calcium sensing mechanism in voltage-gated potassium ion channels. J. Neurosa. 21:4143-4153.
    • (2001) J. Neurosa. , vol.21 , pp. 4143-4153
    • Johnson Jr., J.P.1    Baiser, J.R.2    Bennett, P.B.3
  • 18
    • 0035936798 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cardiac arrhythmias
    • doi:10.1016/S0092-8674(01)00243-4
    • Keating, M.T., and M.C. Sanguinetti. 2001. Molecular and cellular mechanisms of cardiac arrhythmias. Cell. 104:569-580. doi:10.1016/S0092-8674(01) 00243-4
    • (2001) Cell. , vol.104 , pp. 569-580
    • Keating, M.T.1    Sanguinetti, M.C.2
  • 19
    • 44349170359 scopus 로고    scopus 로고
    • Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating
    • Lin, M.C., and D.M. Papazian. 2007. Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating. Channels (Austin). 1:429-437.
    • (2007) Channels (Austin) , vol.1 , pp. 429-437
    • Lin, M.C.1    Papazian, D.M.2
  • 20
    • 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
    • doi:10.1085/jgp.200308788
    • Liu, J., M. Zhang, M. Jiang, and G.N. Tseng. 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. doi:10.1085/jgp.200308788
    • (2003) J. Gen. Physiol. , vol.121 , pp. 599-614
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.N.4
  • 21
    • 0035893487 scopus 로고    scopus 로고
    • Effects of premature stimulation on HERG K(+) channels
    • doi:10.1113/jphysiol.2001.0.12690
    • Lu, Y., M.R Mahaut-Smith, A. Varghese, C.L. Huang, P.R. Kemp, and J.I. Vandenberg. 2001. Effects of premature stimulation on HERG K(+) channels. J. Physiol. 537:843-851. doi:10.1113/jphysiol.2001.0.12690
    • (2001) J. Physiol. , vol.537 , pp. 843-851
    • Lu, Y.1    Mahaut-Smith, M.R.2    Varghese, A.3    Huang, C.L.4    Kemp, P.R.5    Vandenberg, J.I.6
  • 22
    • 0035816728 scopus 로고    scopus 로고
    • Molecular interactions between two long-QT syndrome gene products, HERG and KCNE2, rationalized by in vitro and in silico analysis
    • doi:10.1161/hh1301.093633
    • Mazhari, R., J.L. Greenstein, R.L. Winslow, E. Marbán, and H.B. Nuss. 2001. Molecular interactions between two long-QT syndrome gene products, HERG and KCNE2, rationalized by in vitro and in silico analysis. Circ. Res. 89:33-38. doi:10.1161/hh1301.093633
    • (2001) Circ. Res. , vol.89 , pp. 33-38
    • Mazhari, R.1    Greenstein, J.L.2    Winslow, R.L.3    Marbán, E.4    Nuss, H.B.5
  • 23
    • 11244328061 scopus 로고    scopus 로고
    • v1.2 L-type calcium channels: Dissociation of effects on ionic current; and gating current
    • doi:10.1529/biophysj.104.051714
    • v1.2 L-type calcium channels: dissociation of effects on ionic current; and gating current. Biophys. J. 88:211-223. doi:10.1529/biophysj.104. 051714
    • (2005) Biophys. J. , vol.88 , pp. 211-223
    • McDonough, S.I.1    Mori, Y.2    Bean, B.R.3
  • 25
    • 35348824829 scopus 로고    scopus 로고
    • Structural basis of action for a human ether-a-go-go-related gene 1 potassium channel activator
    • doi:10.1073/pnas.0703934104
    • Perry, M., F.B. Sachse, and M.C. Sanguinetti. 2007. Structural basis of action for a human ether-a-go-go-related gene 1 potassium channel activator. Proc. Natl. Acad, Sci. USA. 104:13827-13832. doi:10.1073/pnas.0703934104
    • (2007) Proc. Natl. Acad, Sci. USA , vol.104 , pp. 13827-13832
    • Perry, M.1    Sachse, F.B.2    Sanguinetti, M.C.3
  • 26
    • 0041836223 scopus 로고    scopus 로고
    • Gating currents associated with intramembrane charge displacement in HERG potassium channels
    • doi:10.1073/pnas.1832721100
    • Piper, D.R., A. Varghese, M.C. Sanguinetti, and M. Tristani-Firouzi. 2003. Gating currents associated with intramembrane charge displacement in HERG potassium channels. Proc. Natl. Acad. Sci. USA. 100:10534-10539. doi:10.1073/pnas.1832721100
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10534-10539
    • Piper, D.R.1    Varghese, A.2    Sanguinetti, M.C.3    Tristani-Firouzi, M.4
  • 27
    • 38349135764 scopus 로고    scopus 로고
    • Cooperative interactions between R531 and acidic residues in the voltage sensing module of hERG1 channels
    • doi:.10.1159/000113745
    • Piper, D.R., J. Rupp, F.B. Sachse, M.C. Sanguinetti, and M. TristaniFirouzi. 2008. Cooperative interactions between R531 and acidic residues in the voltage sensing module of hERG1 channels. Cell. Physiol. Biochem. 21:37-46. doi:.10.1159/000113745
    • (2008) Cell. Physiol. Biochem. , vol.21 , pp. 37-46
    • Piper, D.R.1    Rupp, J.2    Sachse, F.B.3    Sanguinetti, M.C.4    TristaniFirouzi, M.5
  • 28
    • 46149091062 scopus 로고    scopus 로고
    • + channels
    • doi:10.1016/j.neuron.2008.05.006
    • + channels. Neuron. 59:98-109. doi:10.1016/j.neuron.2008.05.006
    • (2008) Neuron. , vol.59 , pp. 98-109
    • Posson, D.J.1    Selvin, P.R.2
  • 30
    • 0038452402 scopus 로고    scopus 로고
    • 2+) in metalloproteins
    • doi:10.1016/S0162-0134(98)10042-9
    • 2+) in metalloproteins. J. Inorg. Biochem. 71:115-127. doi:10.1016/S0162-0134(98)10042- 9
    • (1998) J. Inorg. Biochem. , vol.71 , pp. 115-127
    • Rulísek, L.1    Vondrásek, J.2
  • 31
    • 0034116864 scopus 로고    scopus 로고
    • Altered gating of HERG potassium channels by cobalt and lanthanum
    • Sanchez-Chapula, J.A., and M.C. Sanguinetti. 2000. Altered gating of HERG potassium channels by cobalt and lanthanum. Pflugers Arch. 440:264-274.
    • (2000) Pflugers Arch. , vol.440 , pp. 264-274
    • Sanchez-Chapula, J.A.1    Sanguinetti, M.C.2
  • 32
    • 77955021669 scopus 로고    scopus 로고
    • HERG1 channelopathies
    • doi:10.1007/s00424-009-0758-8
    • Sanguinetti, M.C 2010. HERG1 channelopathies. Pflugers Arch. 460:265-276. doi:10.1007/s00424-009-0758-8
    • (2010) Pflugers Arch. , vol.460 , pp. 265-276
    • Sanguinetti, M.C.1
  • 33
    • 33645317063 scopus 로고    scopus 로고
    • HERG potassium channels and cardiac arrhythmia
    • doi:10.1038/nature04710
    • Sanguinetti, M.C., and M. Tristani-Firouzi. 2006. hERG potassium channels and cardiac arrhythmia. Nature. 440:463-469. doi:10.1038/nature04710
    • (2006) Nature. , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 35
    • 0031952461 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels
    • doi: 10.1085/jgp. 111.2.313
    • Schoppa, N.E., and FJ. Sigworth. 1998. Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels. J. Gen. Physiol 111:313-342. doi: 10.1085/jgp. 111.2.313
    • (1998) J. Gen. Physiol , vol.111 , pp. 313-342
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 36
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • doi:10.1126/science.1553560
    • Schoppa, N.E., K. McGormack, M.A. Tanouye, and F.J. Sigworth. 1992. The size of gating charge in wild-type and mutant Shaker potassium channels. Science. 255:1712-1715. doi:10.1126/science.1553560
    • (1992) Science. , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McGormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 38
    • 0027971204 scopus 로고
    • Voltage gating of ion channels
    • doi:10.1017/sb033583500002894
    • Sigworth, F.J. 1994. Voltage gating of ion channels. Q. Rev. Biophys. 27:1-40. doi:10.1017/sb033583500002894
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 1-40
    • Sigworth, F.J.1
  • 40
    • 0032321375 scopus 로고    scopus 로고
    • Cut-open oocyte voltage-clamp technique
    • P.N. Conn, editor. Academic Press, San Diego
    • Stefani, E., and. F. Bezanilla. 1998. Cut-open oocyte voltage-clamp technique. In Methods in Enzymology. P.N. Conn, editor. Academic Press, San Diego. 300-318.
    • (1998) Methods in Enzymology. , pp. 300-318
    • Stefani, E.1    Bezanilla, F.2
  • 41
    • 0026726052 scopus 로고
    • Electrophysiological recording from Xenopus oocytes
    • doi:10.1016/0076-6879(92)07021-F
    • Stühmer, W. 1992. Electrophysiological recording from Xenopus oocytes. Methods Enzymol. 207:319-339. doi:10.1016/0076-6879(92)07021-F
    • (1992) Methods Enzymol. , vol.207 , pp. 319-339
    • Stühmer, W.1
  • 42
    • 0025736634 scopus 로고
    • Gating currents of inactivating and non-inactivating potassium channels expressed in Xenopus oocytes
    • doi:10.1007/BF00550881
    • Stühmer, W., F. Conti, M. Stocker, O. Pongs, and S.H. Heinemann. 1991. Gating currents of inactivating and non-inactivating potassium channels expressed in Xenopus oocytes. Pflugers Arch. 418:423-429. doi:10.1007/BF00550881
    • (1991) Pflugers Arch. , vol.418 , pp. 423-429
    • Stühmer, W.1    Conti, F.2    Stocker, M.3    Pongs, O.4    Heinemann, S.H.5
  • 44
    • 0029007356 scopus 로고
    • HERG, a human inward rectifier in the voltage-gated potassium channel family
    • doi:10.1126/science.7604285
    • Trudeau, M.C., J.W. Warmke, B. Ganetzky, and G.A. Robertson. 1995. HERG, a human inward rectifier in the voltage-gated potassium channel family. Science. 269:92-95. doi:10.1126/science.7604285
    • (1995) Science. , vol.269 , pp. 92-95
    • Trudeau, M.C.1    Warmke, J.W.2    Ganetzky, B.3    Robertson, G.A.4
  • 45
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to eag in Dmsophila and mammals
    • doi:10.1073/pnas.91.8.3438
    • Wartlike, J.W., and B. Ganetzky. 1994. A family of potassium channel genes related to eag in Dmsophila and mammals. Proc. Natl. Acad. Sci. USA. 91:3438-3442. doi:10.1073/pnas.91.8.3438
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3438-3442
    • Wartlike, J.W.1    Ganetzky, B.2
  • 46
    • 0028085276 scopus 로고
    • Shaker potassium, channel gating. II: Transitions in the activation pathway
    • doi:10.1085/jgp.103.2.279
    • Zagotta, W.N., T. Hoshi, J. Dittman, and R.W. Aldrich. 1994. Shaker potassium, channel gating. II: transitions in the activation pathway. J. Gen. Physiol. 103:279-319. doi:10.1085/jgp.103.2.279
    • (1994) J. Gen. Physiol. , vol.103 , pp. 279-319
    • Zagotta, W.N.1    Hoshi, T.2    Dittman, J.3    Aldrich, R.W.4


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