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Science 7 July 1995:
Vol. 269. no. 5220, pp. 92 - 95
DOI: 10.1126/science.7604285

Articles

Science, Vol 269, Issue 5220, 92-95
Copyright © 1995 by American Association for the Advancement of Science


articles

HERG, a human inward rectifier in the voltage-gated potassium channel family

MC Trudeau, JW Warmke, B Ganetzky, and GA Robertson

Department of Physiology, University of Wisconsin Medical School, Madison 53706, USA.

In contrast to other members of the Eag family of voltage-gated, outwardly rectifying potassium channels, the human eag-related gene (HERG) has now been shown to encode an inwardly rectifying potassium channel. The properties of HERG channels are consistent with the gating properties of Eag-related and other outwardly rectifying, S4-containing potassium channels, but with the addition of an inactivation mechanism that attenuates potassium efflux during depolarization. Because mutations in HERG cause a form of long-QT syndrome, these properties of HERG channel function may be critical to the maintenance of normal cardiac rhythmicity.


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E. Gopal, Y.-J. Fei, M. Sugawara, S. Miyauchi, L. Zhuang, P. Martin, S. B. Smith, P. D. Prasad, and V. Ganapathy (2004)
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Cardiac IKr Channels Minimally Comprise hERG 1a and 1b Subunits.
E. M. C. Jones, E. C. Roti Roti, J. Wang, S. A. Delfosse, and G. A. Robertson (2004)
J. Biol. Chem. 279, 44690-44694
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Voltage-Gated Potassium Channels in Cell Proliferation.
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Physiology 19, 285-292
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Rb+ Flux through hERG Channels Affects the Potency of Channel Blocking Drugs: Correlation with Data Obtained Using a High-Throughput Rb+ Efflux Assay.
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Muscarinic modulation of erg potassium current.
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Pharmacological rescue of trafficking defective HERG channels formed by coassembly of wild-type and long QT mutant N470D subunits.
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Potassium andlong QT syndrome: A new look at an old therapy.
E. Bisinov, J. H. Mitchell, and C. T. January (2003)
J. Am. Coll. Cardiol. 42, 1783-1784
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Acceleration of human myoblast fusion by depolarization: graded Ca2+ signals involved.
J.-H. Liu, S. Konig, M. Michel, S. Arnaudeau, J. Fischer-Lougheed, C. R. Bader, and L. Bernheim (2003)
Development 130, 3437-3446
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APETx1, a New Toxin from the Sea Anemone Anthopleura elegantissima, Blocks Voltage-Gated Human Ether-a-go-go-Related Gene Potassium Channels.
S. Diochot, E. Loret, T. Bruhn, L. Beress, and M. Lazdunski (2003)
Mol. Pharmacol. 64, 59-69
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Inhibition of HERG K+ current and prolongation of the guinea-pig ventricular action potential by 4-aminopyridine.
J M Ridley, J T Milnes, Y H Zhang, H J Witchel, and J C Hancox (2003)
J. Physiol. 549, 667-672
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Saxitoxin Is a Gating Modifier of hERG K+ Channels.
J. Wang, J. J. Salata, and P. B. Bennett (2003)
J. Gen. Physiol. 121, 583-598
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Voltage-Dependent Profile of Human Ether-a-go-go-Related Gene Channel Block Is Influenced by a Single Residue in the S6 Transmembrane Domain.
J. A. Sanchez-Chapula, T. Ferrer, R. A. Navarro-Polanco, and M. C. Sanguinetti (2003)
Mol. Pharmacol. 63, 1051-1058
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Modulation of human ether-a-go-go-related K+ (HERG) channel inactivation by Cs+ and K+.
S. Zhang, S. J Kehl, and D. Fedida (2003)
J. Physiol. 548, 691-702
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Caenorhabditis elegans UNC-103 ERG-Like Potassium Channel Regulates Contractile Behaviors of Sex Muscles in Males before and during Mating.
L. R. Garcia and P. W. Sternberg (2003)
J. Neurosci. 23, 2696-2705
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Dissociation of E-4031 from the HERG channel caused by mutations of an amino acid results in greater block at high stimulation frequency.
K. Ishii, M. Nagai, M. Takahashi, and M. Endoh (2003)
Cardiovasc Res 57, 651-659
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Cloning and Functional Characterization of the Smooth Muscle Ether-a-go-go-related Gene K+ Channel. POTENTIAL ROLE OF A CONSERVED AMINO ACID SUBSTITUTION IN THE S4 REGION.
F. Shoeb, A. P. Malykhina, and H. I. Akbarali (2003)
J. Biol. Chem. 278, 2503-2514
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Functional and pharmacological properties of canine ERG potassium channels.
J. Wang, K. Della Penna, H. Wang, J. Karczewski, T. M. Connolly, K. S. Koblan, P. B. Bennett, and J. J. Salata (2003)
Am J Physiol Heart Circ Physiol 284, H256-H267
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Modulation of the ERG K+ Current by the Tyrosine Phosphatase, SHP-1.
F. S. Cayabyab, F. W. L. Tsui, and L. C. Schlichter (2002)
J. Biol. Chem. 277, 48130-48138
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