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Cited by 116Ion channel regulation and functionCardiac electrophysiology and arrhythmiasIon Transport and Channel Regulation

A kinetic map of the homomeric voltage-gated potassium channel (Kv) family

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Ranjan, Rajnish, Logette, Emmanuelle, Marani, Michela, Herzog, Mirjia, Tâche, Valérie, Scantamburlo, Enrico, Buchillier, Valérie, Markram, Henry·2019·Frontiers in Cellular Neuroscience
DOI 10.3389/fncel.2019.00358PMC PMC6710402
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Abstract

The voltage-gated potassium (Kv) channels, encoded by 40 genes, repolarize all electrically excitable cells, including plant, cardiac and neuronal cells. Although these genes were fully sequenced decades ago, a comprehensive kinetic characterization of all Kv channels is still missing, especially near physiological temperature. Here, we present a standardized kinetic map of the 40 homomeric Kv channels systematically characterized at 15°C, 25°C and 35°C. Importantly, the Kv kinetics at 35°C differ significantly from commonly reported kinetics, usually performed at room temperature. We observed voltage-dependent Q10 for all active Kv channels and inherent heterogeneity in kinetics for some of them. Kinetic properties are consistent across different host cell lines and conserved across mouse, rat and human. All electrophysiology data from all Kv channels are made available through public website (Channelpedia). This dataset provides a solid foundation for exploring kinetics of heteromeric channels, roles of auxiliary subunits, kinetic modulation, and for building accurate Kv models.

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  • Many biological processes vary considerably over 4-5 °C, well within the range of what is normally considered room temperature.

    “because many biological processes vary considerably over 4-5 • C [40,55-59], well within the range of what is normally considered room temperature.”

    From A feature and not a bug: Replication failures can lead to new biology (2026) · cites this paper as [55]

    The Results section (page not provided) reports substantial changes in Kv-channel kinetics across measurements at 15, 25, and 35°C, supporting temperature sensitivity. It does not establish that many biological processes vary considerably over a 4–5°C difference within the room-temperature range. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • Some channel kinetics measured at low temperature were qualitatively different from measurements made close to physiological temperatures.

    “Some channel kinetics measured at low temperature were qualitatively different from measurements made close to physiological temperatures [55], and Q10 varied with the voltage and temperature at which currents were measured [55].”

    From A feature and not a bug: Replication failures can lead to new biology (2026) · cites this paper as [55]

  • Q10 varied with the voltage and temperature at which currents were measured.

    “Some channel kinetics measured at low temperature were qualitatively different from measurements made close to physiological temperatures [55], and Q10 varied with the voltage and temperature at which currents were measured [55].”

    From A feature and not a bug: Replication failures can lead to new biology (2026) · cites this paper as [55]

  • Measurements at 35 °C may vary considerably from those that were made at lower temperatures.

    “Measurements at 35 • C may vary considerably from those that were made at lower temperatures.”

    From A feature and not a bug: Replication failures can lead to new biology (2026) · cites this paper as [55]

  • Ranjan et al. created a kinetic map of 40 homomeric K+ channels' function from 15 °C to 35 °C.

    “In a remarkable study Ranjan et al. [55] created a kinetic map of 40 homomeric K + channels' function from 15 • C to 35 • C.”

    From A feature and not a bug: Replication failures can lead to new biology (2026) · cites this paper as [55]

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Research works printed but not linked: 86

  1. Adams D. J. Oxford G. S. (1983). Interaction of internal anions with potassium channels of the squid giant axon. J. Gen. Physiol. 82, 429– 448. 10.1085/jgp.82.4.429 6315855 PMC2228656 · DOI
  2. Alberts B. Wilson J. H. Hunt T. (eds.). (2008). Molecular Biology of the Cell, 5th Edn. New York, NY: Garland Science.
  3. Aromolaran A. S. Subramanyam P. Chang D. D. Kobertz W. R. Colecraft H. M. (2014). LQT1 mutations in KCNQ1 C-terminus assembly domain suppress IKs using different mechanisms. Cardiovasc. Res. 104, 501– 511. 10.1093/cvr/cvu231 25344363 PMC4296111 · DOI
  4. Bähring R. Vardanyan V. Pongs O. (2004). Differential modulation of Kv1 channel-mediated currents by co-expression of Kvbeta3 subunit in a mammalian cell-line. Mol. Membr. Biol. 21, 19– 25. 10.1080/09687680310001597749 14668135 · DOI
  5. Barhanin J. Lesage F. Guillemare E. Fink M. Lazdunski M. Romey G. (1996). K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current. Nature 384, 78– 80. 10.1038/384078a0 8900282 · DOI
  6. Beam K. G. Donaldson P. L. (1983). A quantitative study of potassium channel kinetics in rat skeletal muscle from 1 to 37 degrees C. J. Gen. Physiol. 81, 485– 512. 10.1085/jgp.81.4.485 6304231 PMC2215581 · DOI · Paper page
  7. Begum R. Bakiri Y. Volynski K. E. Kullmann D. M. (2016). Action potential broadening in a presynaptic channelopathy. Nat. Commun. 7: 12102. 10.1038/ncomms12102 27381274 PMC4935806 · DOI
  8. Bett G. C. L. Morales M. J. Beahm D. L. Duffey M. E. Rasmusson R. L. (2006). Ancillary subunits and stimulation frequency determine the potency of chromanol 293B block of the KCNQ1 potassium channel. J. Physiol. 576, 755– 767. 10.1113/jphysiol.2006.116012 16887873 PMC1890396 · DOI
  9. Bezanilla F. (2000). The voltage sensor in voltage-dependent ion channels. Physiol. Rev. 80, 555– 592. 10.1152/physrev.2000.80.2.555 10747201 · DOI
  10. Bezanilla F. Armstrong C. M. (1977). Inactivation of the sodium channel. I. Sodium current experiments. J. Gen. Physiol. 70, 549– 566. 10.1085/jgp.70.5.549 591911 PMC2228478 · DOI
  11. Bocksteins E. Mayeur E. Van Tilborg A. Regnier G. Timmermans J.-P. Snyders D. J. (2014). The subfamily-specific interaction between Kv2.1 and Kv6.4 subunits is determined by interactions between the N- and C-termini. PLoS ONE 9: e98960. 10.1371/journal.pone.0098960 24901643 PMC4047056 · DOI
  12. Brooks N. L. Corey M. J. Schwalbe R. A. (2006). Characterization of N-glycosylation consensus sequences in the Kv3.1 channel. FEBS J. 273, 3287– 3300. 10.1111/j.1742-4658.2006.05339.x 16792699 · DOI
  13. Clay J. R. (1988). Lack of effect of internal fluoride ions on potassium channels in squid axons. Biophys. J. 53, 647– 648. 10.1016/S0006-3495(88)83144-8 2454679 PMC1330238 · DOI
  14. Coetzee W. A. Amarillo Y. Chiu J. Chow A. Lau D. McCormack T.. (1999). Molecular diversity of K+ channels. Ann. N. Y. Acad. Sci. 868, 233– 285. 10.1111/j.1749-6632.1999.tb11293.x 10414301 · DOI · Paper page
  15. D'Adamo M. C. Gallenmüller C. Servettini I. Hartl E. Tucker S. J. Arning L.. (2014). Novel phenotype associated with a mutation in the KCNA1(Kv1.1) gene. Front. Physiol. 5: 525. 10.3389/fphys.2014.00525 25642194 PMC4295438 · DOI
  16. Desai R. Kronengold J. Mei J. Forman S. A. Kaczmarek L. K. (2008). Protein kinase C modulates inactivation of Kv3.3 channels. J. Biol. Chem. 283, 22283– 22294. 10.1074/jbc.M801663200 18539595 PMC2494927 · DOI
  17. Dodson P. D. Barker M. C. Forsythe I. D. (2002). Two heteromeric Kv1 potassium channels differentially regulate action potential firing. J. Neurosci. Off. J. Soc. Neurosci. 22, 6953– 6961. 10.1523/JNEUROSCI.22-16-06953.2002 12177193 PMC6757903 · DOI
  18. Duménieu M. Oulé M. Kreutz M. R. Lopez-Rojas J. (2017). The segregated expression of voltage-gated potassium and sodium channels in neuronal membranes: functional implications and regulatory mechanisms. Front. Cell. Neurosci. 11: 115. 10.3389/fncel.2017.00115 28484374 PMC5403416 · DOI
  19. Engeland B. Neu A. Ludwig J. Roeper J. Pongs O. (1998). Cloning and functional expression of rat ether-à-go-go-like K+ channel genes. J. Physiol. 513 (Pt 3), 647– 654. 10.1111/j.1469-7793.1998.647ba.x 9824707 PMC2231332 · DOI
  20. Fejtl M. Czubayko U. Hümmer A. Krauter T. Lepple-Wienhues A. (2007). Flip-the-tip: automated patch clamping based on glass electrodes. Methods Mol. Biol. 403, 71– 85. 10.1007/978-1-59745-529-9_5 18827988 · DOI
  21. Fernandez F. R. Morales E. Rashid A. J. Dunn R. J. Turner R. W. (2003). Inactivation of Kv3.3 potassium channels in heterologous expression systems. J. Biol. Chem. 278, 40890– 40898. 10.1074/jbc.M304235200 12923191 · DOI
  22. Ficker E. Dennis A. T. Wang L. Brown A. M. (2003). Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG. Circ. Res. 92, e87– 100. 10.1161/01.RES.0000079028.31393.15 12775586 · DOI
  23. Finol-Urdaneta R. K. Remedi M. S. Raasch W. Becker S. Clark R. B. Strüver N.. (2012). Block of Kv1.7 potassium currents increases glucose-stimulated insulin secretion. EMBO Mol. Med. 4, 424– 434. 10.1002/emmm.201200218 22438204 PMC3403299 · DOI
  24. Finol-Urdaneta R. K. Strüver N. Terlau H. (2006). Molecular and functional differences between heart mKv1.7 channel isoforms. J. Gen. Physiol. 128, 133– 145. 10.1085/jgp.200609498 16801386 PMC2151556 · DOI
  25. Gabel L. A. Nisenbaum E. S. (1998). Biophysical characterization and functional consequences of a slowly inactivating potassium current in neostriatal neurons. J. Neurophysiol. 79, 1989– 2002. 10.1152/jn.1998.79.4.1989 9535963 · DOI
  26. Gamper N. Stockand J. D. Shapiro M. S. (2005). The use of Chinese hamster ovary (CHO) cells in the study of ion channels. J. Pharmacol. Toxicol. Methods 51, 177– 185. 10.1016/j.vascn.2004.08.008 15862463 · DOI
  27. Gilling M. Rasmussen H. B. Calloe K. Sequeira A. F. Baretto M. Oliveira G.. (2013). Dysfunction of the heteromeric KV7.3/KV7.5 potassium channel is associated with autism spectrum disorders. Front. Genet. 4: 54. 10.3389/fgene.2013.00054 23596459 PMC3627139 · DOI
  28. Glazebrook P. A. Ramirez A. N. Schild J. H. Shieh C.-C. Doan T. Wible B. A.. (2002). Potassium channels Kv1.1, Kv1.2 and Kv1.6 influence excitability of rat visceral sensory neurons. J. Physiol. 541, 467– 482. 10.1113/jphysiol.2001.018333 12042352 PMC2290329 · DOI
  29. Graves T. D. Hanna M. G. (2005). Neurological channelopathies. Postgrad. Med. J. 81, 20– 32. 10.1136/pgmj.2004.022012 15640425 PMC1743173 · DOI
  30. Hadley J. K. Passmore G. M. Tatulian L. Al-Qatari M. Ye F. Wickenden A. D.. (2003). Stoichiometry of expressed KCNQ2/KCNQ3 potassium channels and subunit composition of native ganglionic M channels deduced from block by tetraethylammonium. J. Neurosci. Off. J. Soc. Neurosci. 23, 5012– 5019. 10.1523/JNEUROSCI.23-12-05012.2003 12832524 PMC6741196 · DOI
  31. Hatton W. J. Mason H. S. Carl A. Doherty P. Latten M. J. Kenyon J. L.. (2001). Functional and molecular expression of a voltage-dependent K+ channel (Kv1.1) in interstitial cells of Cajal. J. Physiol. 533, 315– 327. 10.1111/j.1469-7793.2001.0315a.x 11389194 PMC2278641 · DOI
  32. Heginbotham L. Lu Z. Abramson T. MacKinnon R. (1994). Mutations in the K+ channel signature sequence. Biophys. J. 66, 1061– 1067. 10.1016/S0006-3495(94)80887-2 8038378 PMC1275813 · DOI
  33. Heinemann S. H. Rettig J. Graack H. R. Pongs O. (1996). Functional characterization of Kv channel beta-subunits from rat brain. J. Physiol. 493, 625– 633. 10.1113/jphysiol.1996.sp021409 8799886 PMC1159012 · DOI
  34. Hodgkin A. L. Huxley A. F. (1952). A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117, 500– 544. 10.1113/jphysiol.1952.sp004764 12991237 PMC1392413 · DOI · Paper page
  35. Hoshi T. Heinemann S. (2001). Regulation of cell function by methionine oxidation and reduction. J. Physiol. 531, 1– 11. 10.1111/j.1469-7793.2001.0001j.x 11179387 PMC2278441 · DOI · Paper page
  36. Jensen C. S. Rasmussen H. B. Misonou H. (2011). Neuronal trafficking of voltage-gated potassium channels. Mol. Cell. Neurosci. 48, 288– 297. 10.1016/j.mcn.2011.05.007 21627990 · DOI
  37. John V. H. Main M. J. Powell A. J. Gladwell Z. M. Hick C. Sidhu H. S.. (2004). Heterologous expression and functional analysis of rat Nav1.8 (SNS) voltage-gated sodium channels in the dorsal root ganglion neuroblastoma cell line ND7-23. Neuropharmacology 46, 425– 438. 10.1016/j.neuropharm.2003.09.018 14975698 · DOI
  38. Jow F. Zhang Z.-H. Kopsco D. C. Carroll K. C. Wang K. (2004). Functional coupling of intracellular calcium and inactivation of voltage-gated Kv1.1/Kvbeta1.1 A-type K+ channels. Proc. Natl. Acad. Sci. U.S.A. 101, 15535– 15540. 10.1073/pnas.0402081101 15486093 PMC524431 · DOI
  39. Ju M. Stevens L. Leadbitter E. 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. 10.1074/jbc.M212973200 12560340 · DOI
  40. Kaczmarek L. K. (2006). Non-conducting functions of voltage-gated ion channels. Nat. Rev. Neurosci. 7, 761– 771. 10.1038/nrn1988 16988652 · DOI
  41. Khorkova O. Golowasch J. (2007). Neuromodulators, not activity, control coordinated expression of ionic currents. J. Neurosci. Off. J. Soc. Neurosci. 27, 8709– 8718. 10.1523/JNEUROSCI.1274-07.2007 PMC3558984 17687048 · DOI
  42. Kostyuk P. G. Krishtal O. A. Pidoplichko V. I. (1975). Effect of internal fluoride and phosphate on membrane currents during intracellular dialysis of nerve cells. Nature 257, 691– 693. 10.1038/257691a0 1186845 · DOI
  43. Kramer J. W. Post M. A. Brown A. M. Kirsch G. E. (1998). Modulation of potassium channel gating by coexpression of Kv2.1 with regulatory Kv5.1 or Kv6.1 alpha-subunits. Am. J. Physiol. 274, C1501– 1510. 10.1152/ajpcell.1998.274.6.C1501 9696692 · DOI
  44. Kullmann D. M. Waxman S. G. (2010). Neurological channelopathies: new insights into disease mechanisms and ion channel function. J. Physiol. 588, 1823– 1827. 10.1113/jphysiol.2010.190652 20375141 PMC2901970 · DOI
  45. Labro A. J. Priest M. F. Lacroix J. J. Snyders D. J. Bezanilla F. (2015). Kv3.1 uses a timely resurgent K+ current to secure action potential repolarization. Nat. Commun. 6: 10173. 10.1038/ncomms10173 26673941 PMC4703866 · DOI
  46. Lai H. C. Jan L. Y. (2006). The distribution and targeting of neuronal voltage-gated ion channels. Nat. Rev. Neurosci. 7, 548– 562. 10.1038/nrn1938 16791144 · DOI
  47. Lalik P. H. Krafte D. S. Volberg W. A. Ciccarelli R. B. (1993). Characterization of endogenous sodium channel gene expressed in Chinese hamster ovary cells. Am. J. Physiol. 264, C803– 809. 10.1152/ajpcell.1993.264.4.C803 7682773 · DOI
  48. Lee S. C. Deutsch C. (1990). Temperature dependence of K+-channel properties in human T lymphocytes. Biophys. J. 57, 49– 62. 10.1016/S0006-3495(90)82506-6 2297562 PMC1280642 · DOI
  49. Levitan I. B. (2006). Signaling protein complexes associated with neuronal ion channels. Nat. Neurosci. 9, 305– 310. 10.1038/nn1647 16498425 · DOI
  50. Li G.-R. Dong M.-Q. (2010). Pharmacology of cardiac potassium channels. Adv. Pharmacol. 59, 93– 134. 10.1016/S1054-3589(10)59004-5 20933200 · DOI
  51. Li T. Lu G. Chiang E. Y. Chernov-Rogan T. Grogan J. L. Chen J. (2017). High-throughput electrophysiological assays for voltage gated ion channels using SyncroPatch 768PE. PLoS ONE. 12: e0180154. 10.1371/journal.pone.0180154 28683073 PMC5500279 · DOI
  52. Li Y. Um S. Y. McDonald T. V. (2006). Voltage-gated potassium channels: regulation by accessory subunits. Neurosci. Rev. J. Bringing Neurobiol. Neurol. Psychiatry 12, 199– 210. 10.1177/1073858406287717 16684966 · DOI
  53. Lipscombe D. (2005). Neuronal proteins custom designed by alternative splicing. Curr. Opin. Neurobiol. 15, 358– 363. 10.1016/j.conb.2005.04.002 15961039 · DOI
  54. López-López J. R. De Luis D. A. Gonzalez C. (1993). Properties of a transient K+ current in chemoreceptor cells of rabbit carotid body. J. Physiol. 460, 15– 32. 10.1113/jphysiol.1993.sp019456 8387583 PMC1175198 · DOI
  55. Loussouarn G. Charpentier F. Mohammad-Panah R. Kunzelmann K. Baró I. Escande D. (1997). KvLQT1 potassium channel but not IsK is the molecular target for trans-6-cyano-4-(N-ethylsulfonyl-N-methylamino)-3-hydroxy-2,2-dimethyl- chromane. Mol. Pharmacol. 52, 1131– 1136. 10.1124/mol.52.6.1131 9396783 · DOI
  56. Majumder K. De Biasi M. Wang Z. Wible B. A. (1995). Molecular cloning and functional expression of a novel potassium channel beta-subunit from human atrium. FEBS Lett. 361, 13– 16. 10.1016/0014-5793(95)00120-X 7890032 · DOI
  57. Nakajo K. Kubo Y. (2008). Second coiled-coil domain of KCNQ channel controls current expression and subfamily specific heteromultimerization by salt bridge networks. J. Physiol. 586, 2827– 2840. 10.1113/jphysiol.2007.148601 18440995 PMC2517212 · DOI
  58. NCBI Resource Coordinators (2013). Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 41, D8– D20. 10.1093/nar/gks1189 23193264 PMC3531099 · DOI
  59. Nicoll R. A. (1988). The coupling of neurotransmitter receptors to ion channels in the brain. Science 241, 545– 551. 10.1126/science.2456612 2456612 · DOI
  60. Noma K. Kimura K. Minatohara K. Nakashima H. Nagao Y. Mizoguchi A.. (2009). Triple N-glycosylation in the long S5-P loop regulates the activation and trafficking of the Kv12.2 potassium channel. J. Biol. Chem. 284, 33139– 33150. 10.1074/jbc.M109.021519 19808681 PMC2785156 · DOI
  61. O'Gorman S. Fox D. T. Wahl G. M. (1991). Recombinase-mediated gene activation and site-specific integration in mammalian cells. Science 251, 1351– 1355. 10.1126/science.1900642 1900642 · DOI
  62. Oliver K. L. Franceschetti S. Milligan C. J. Muona M. Mandelstam S. A. Canafoglia L.. (2017). Myoclonus epilepsy and ataxia due to KCNC1 mutation: Analysis of 20 cases and K+ channel properties. Ann. Neurol. 81, 677– 689. 10.1002/ana.24929 28380698 · DOI
  63. Petersen K. R. Nerbonne J. M. (1999). Expression environment determines K+ current properties: Kv1 and Kv4 alpha-subunit-induced K+ currents in mammalian cell lines and cardiac myocytes. Pflugers Arch. 437, 381– 392. 10.1007/s004240050792 9914394 · DOI
  64. Pongs O. Schwarz J. R. (2010). Ancillary subunits associated with voltage-dependent K+ channels. Physiol. Rev. 90, 755– 796. 10.1152/physrev.00020.2009 20393197 · DOI
  65. Post J. M. Hume J. R. Archer S. L. Weir E. K. (1992). Direct role for potassium channel inhibition in hypoxic pulmonary vasoconstriction. Am. J. Physiol. 262, C882– 890. 10.1152/ajpcell.1992.262.4.C882 1566816 · DOI
  66. Rajakulendran S. Schorge S. Kullmann D. M. Hanna M. G. (2007). Episodic ataxia type 1: a neuronal potassium channelopathy. Neurother. J. Am. Soc. Exp. Neurother. 4, 258– 266. 10.1016/j.nurt.2007.01.010 17395136 · DOI
  67. Rasband M. N. (2010). Clustered K+ channel complexes in axons. Neurosci. Lett. 486, 101– 106. 10.1016/j.neulet.2010.08.081 20816921 PMC2990350 · DOI
  68. Rezazadeh S. Kurata H. T. Claydon T. W. Kehl S. J. Fedida D. (2007). An activation gating switch in Kv1.2 is localized to a threonine residue in the S2-S3 linker. Biophys. J. 93, 4173– 4186. 10.1529/biophysj.107.116160 17766348 PMC2098734 · DOI
  69. Ritter D. M. Ho C. O'Leary M. E. Covarrubias M. (2012). Modulation of Kv3.4 channel N-type inactivation by protein kinase C shapes the action potential in dorsal root ganglion neurons. J. Physiol. 590, 145– 161. 10.1113/jphysiol.2011.218560 22063632 PMC3300053 · DOI
  70. Rodriguez-Menchaca A. A. Adney S. K. Tang Q.-Y. Meng X.-Y. Rosenhouse-Dantsker A. Cui M.. (2012). PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4-S5 linker. Proc. Natl. Acad. Sci. U.S. A. 109, E2399– 2408. 10.1073/pnas.1207901109 22891352 PMC3437867 · DOI
  71. Salinas M. Duprat F. Heurteaux C. Hugnot J. P. Lazdunski M. (1997). New modulatory alpha subunits for mammalian Shab K+ channels. J. Biol. Chem. 272, 24371– 24379. 10.1074/jbc.272.39.24371 9305895 · DOI
  72. Sanguinetti M. C. Curran M. E. Zou A. Shen J. Spector P. S. Atkinson D. L.. (1996). Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel. Nature 384, 80– 83. 10.1038/384080a0 8900283 · DOI
  73. Shah N. H. Aizenman E. (2014). Voltage-gated potassium channels at the crossroads of neuronal function, ischemic tolerance, and neurodegeneration. Transl. Stroke Res. 5, 38– 58. 10.1007/s12975-013-0297-7 PMC3946373 24323720 · DOI
  74. Southan C. Sharman J. L. Benson H. E. Faccenda E. Pawson A. J. Alexander S. P. H.. (2016). The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. Nucleic Acids Res. 44, D1054– 1068. 10.1093/nar/gkv1037 26464438 PMC4702778 · DOI
  75. Stephens G. J. Page K. M. Burley J. R. Berrow N. S. Dolphin A. C. (1997). Functional expression of rat brain cloned alpha1E calcium channels in COS-7 cells. Pflüg. Arch. Eur. J. Physiol. 433, 523– 532. 10.1007/s004240050308 9000432 · DOI
  76. Storm J. F. (1988). Temporal integration by a slowly inactivating K+ current in hippocampal neurons. Nature 336, 379– 381. 10.1038/336379a0 3194020 · DOI
  77. Sturm P. Wimmers S. Schwarz J. R. Bauer C. K. (2005). Extracellular potassium effects are conserved within the rat erg K+ channel family. J. Physiol. 564, 329– 345. 10.1113/jphysiol.2004.078840 15705650 PMC1464433 · DOI
  78. Teeters J. L. Godfrey K. Young R. Dang C. Friedsam C. Wark B.. (2015). Neurodata without borders: creating a common data format for neurophysiology. Neuron 88, 629– 634. 10.1016/j.neuron.2015.10.025 26590340 · DOI
  79. Trimmer J. S. (2015). Subcellular localization of K+ channels in mammalian brain neurons: remarkable precision in the midst of extraordinary complexity. Neuron 85, 238– 256. 10.1016/j.neuron.2014.12.042 25611506 PMC4303806 · DOI
  80. Vacher H. Mohapatra D. P. Trimmer J. S. (2008). Localization and targeting of voltage-dependent ion channels in mammalian central neurons. Physiol. Rev. 88, 1407– 1447. 10.1152/physrev.00002.2008 18923186 PMC2587220 · DOI
  81. van der Wijst J. Glaudemans B. Venselaar H. Nair A. V. Forst A.-L. Hoenderop J. G. J.. (2010). Functional analysis of the Kv1.1 N255D mutation associated with autosomal dominant hypomagnesemia. J. Biol. Chem. 285, 171– 178. 10.1074/jbc.M109.041517 19903818 PMC2804162 · DOI
  82. Wang H. S. Pan Z. Shi W. Brown B. S. Wymore R. S. Cohen I. S.. (1998). KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel. Science 282, 1890– 1893. 10.1126/science.282.5395.1890 9836639 · DOI
  83. Wimmers S. Bauer C. K. Schwarz J. R. (2002). Biophysical properties of heteromultimeric erg K+ channels. Pflugers Arch. 445, 423– 430. 10.1007/s00424-002-0936-4 12466946 · DOI
  84. Yao F. Svensjö T. Winkler T. Lu M. Eriksson C. Eriksson E. (1998). Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells. Hum. Gene Ther. 9, 1939– 1950. 10.1089/hum.1998.9.13-1939 9741432 · DOI
  85. Zeng H. Balasubramanian B. Penniman J. R. Kinose F. Salata J. J. Lagrutta A. (2013). Halide ion effects on human Ether-à-go-go related gene potassium channel properties. Assay Drug Dev. Technol. 11, 544– 550. 10.1089/adt.2013.531 24147984 · DOI
  86. Zhang J. Carver C. M. Choveau F. S. Shapiro M. S. (2016). Clustering and functional coupling of diverse ion channels and signaling proteins revealed by super-resolution STORM microscopy in neurons. Neuron 92, 461– 478. 10.1016/j.neuron.2016.09.014 27693258 PMC5553284 · DOI

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Sorted by citations

Authors
Ranjan, R., Logette, E., Marani, M., Herzog, M., Tâche, V., Scantamburlo, E., Buchillier, V., & Markram, H.
Affiliations
École Polytechnique Fédérale de Lausanne (CH)
Corresponding author
  • Ranjan, Rajnish
  • Markram, Henry
ORCID
Venue
Frontiers in Cellular Neuroscience
Publisher
Frontiers Media SA
Published
2019-08-20
Volume
13
Pages
358-358
ISSN
1662-5102 (ISSN-L)
DOI
10.3389/fncel.2019.00358
PMC
PMC6710402
OpenAlex
W2963659755
Cited by
116
References
2
Citations by year
2026: 13 · 2025: 14 · 2024: 25 · 2023: 17 · 2022: 15 · 2021: 18 · 2020: 12 · 2019: 1
FWCI
3.77
Type
journal article
Language
en
Open access
Licence
Locations
  • Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
Funders
École Polytechnique Fédérale de Lausanne
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords
voltage-gated potassium channels, channel kinetics, temperature dependence, Q10, kinetic heterogeneity, homomeric channels, kinetic model, auxiliary subunits, heteromeric channels

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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