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Nature Genet. 12, 17\u201323 (1996).","journal-title":"Nature Genet."},{"key":"BF35036198_CR4","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1126\/science.279.5349.403","volume":"279","author":"C Biervert","year":"1998","unstructured":"Biervert, C.  et al. A potassium channel mutation in neonatal human epilepsy.  Science 279, 403\u2013406 ( 1998).Full-length KCNQ2 is cloned and shown to be mutated in affected members of a large family with BFNC. The mutation that truncates the C terminus leads to non-functional channels that have no dominant-negative effect on wild-type subunits.","journal-title":"Science"},{"key":"BF35036198_CR5","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1038\/ng0198-25","volume":"18","author":"NA Singh","year":"1998","unstructured":"Singh, N. A.  et al. A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns. Nature Genet. 18, 25\u201329 (1998).Positional cloning is used to identify KCNQ2. Several mutations, including a genomic deletion, are found in families with BFNC.","journal-title":"Nature Genet."},{"key":"BF35036198_CR6","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1038\/ng0198-53","volume":"18","author":"C Charlier","year":"1998","unstructured":"Charlier, C.  et al. A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family. Nature Genet. 18, 53\u201355 (1998).","journal-title":"Nature Genet."},{"key":"BF35036198_CR7","doi-asserted-by":"publisher","first-page":"186","DOI":"10.1038\/ng0297-186","volume":"15","author":"N Neyroud","year":"1997","unstructured":"Neyroud, N.  et al. A novel mutation in the potassium channel gene KVLQT1 causes the Jervell and Lange-Nielsen cardioauditory syndrome. 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KvLQT1 and IsK (minK) proteins associate to form the I Ks cardiac potassium current. Nature  384, 78\u201380 (1996). In parallel to the work by Sanguinetti  et al . this paper finally identifies KCNQ1 as the partner for KCNE1 (minK, IsK).","journal-title":"Nature"},{"key":"BF35036198_CR10","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1038\/384080a0","volume":"384","author":"MC Sanguinetti","year":"1996","unstructured":"Sanguinetti, M. C.  et al. Coassembly of KVLQT1 and minK (IsK) proteins to form cardiac IKs potassium channel. Nature  384, 80\u201383 (1996). In parallel to the work by Barhanin  et al . this paper shows that KCNQ1 and KCNE1 underlie the  I Ks  current. It also shows that oocytes express a KCNQ1 homologue, which explains why  Xenopus  oocytes were the only expression system in which KCNE1 could be expressed previously.","journal-title":"Nature"},{"key":"BF35036198_CR11","doi-asserted-by":"publisher","first-page":"1251","DOI":"10.1016\/S0896-6273(00)80255-X","volume":"17","author":"DE Vetter","year":"1996","unstructured":"Vetter, D. E.  et al. Inner ear defects induced by null mutation of the isk gene. Neuron 17, 1251\u20131264 (1996).The first disruption of the   Kcne1 (isk ) gene in mice. This thorough study shows a collapse of the scala media shortly after birth. Transepithelial measurements show that the current across the stria vascularis is nearly abolished.","journal-title":"Neuron"},{"key":"BF35036198_CR12","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1038\/35003200","volume":"403","author":"BC Schroeder","year":"2000","unstructured":"Schroeder, B. C.  et al. A constitutively open potassium channel formed by KCNQ1 and KCNE3. Nature 403, 196\u2013 199 (2000).KCNE3 is shown to greatly affect KCNQ1 gating. It acts differently from KCNE1 by constitutively opening the channel.  In situ  hybridization and comparison with native currents indicate that the KCNQ1\/ KCNE3 channel may be important for intestinal chloride secretion.","journal-title":"Nature"},{"key":"BF35036198_CR13","doi-asserted-by":"publisher","first-page":"1890","DOI":"10.1126\/science.282.5395.1890","volume":"282","author":"HS Wang","year":"1998","unstructured":"Wang, H. S.  et al. KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel. Science 282, 1890\u2013 1893 (1998).The kinetic and pharmacological properties of KCNQ2\/KCNQ3 heteromeric channels are shown to correlate with those of M-currents. This work finally indicates a solution to the molecular identity of this important regulator of neuronal excitability.","journal-title":"Science"},{"key":"BF35036198_CR14","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1038\/283673a0","volume":"283","author":"DA Brown","year":"1980","unstructured":"Brown, D. A. & Adams, P. R. Muscarinic suppression of a novel voltage-sensitive K+ current in a vertebrate neurone.  Nature 283, 673\u2013676 ( 1980).","journal-title":"Nature"},{"key":"BF35036198_CR15","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1038\/25367","volume":"396","author":"BC Schroeder","year":"1998","unstructured":"Schroeder, B. C., Kubisch, C., Stein, V. & Jentsch, T. J. Moderate loss of function of cyclic-AMP-modulated KCNQ2\/KCNQ3 K+ channels causes epilepsy. Nature 396, 687\u2013 690 (1998).Like reference 13, this work shows that KCNQ2 and KCNQ3 form heteromers. Analysis of KCNQ2 and KCNQ3 mutants within this heteromer indicates that the loss of currents in heterozygous patients with BFNC is surprisingly small (25%). In addition, KCNQ2\/KCNQ3 currents are shown to be activated by cAMP.","journal-title":"Nature"},{"key":"BF35036198_CR16","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1046\/j.1471-4159.2000.0750028.x","volume":"75","author":"H Watanabe","year":"2000","unstructured":"Watanabe, H.  et al. Disruption of the epilepsy KCNQ2 gene results in neural hyperexcitability . J. Neurochem. 75, 28\u2013 33 (2000).","journal-title":"J. Neurochem."},{"key":"BF35036198_CR17","doi-asserted-by":"publisher","first-page":"24089","DOI":"10.1074\/jbc.M003245200","volume":"275","author":"BC Schroeder","year":"2000","unstructured":"Schroeder, B. C., Hechenberger, M., Weinreich, F., Kubisch, C. & Jentsch, T. J. KCNQ5, a novel potassium channel broadly expressed in brain, mediates M-type currents. J. Biol. 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