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Volumn 5, Issue OCT, 2014, Pages

CLC channel function and dysfunction in health and disease

Author keywords

Anion channel; Bartter syndrome; CLC channel; Leukencephalopathy; Myotonia congenita; Patch clamp

Indexed keywords

CHLORIDE CHANNEL; CHLORIDE CHANNEL 1; CHLORIDE CHANNEL 2; CHLORIDE CHANNEL KA; CHLORIDE CHANNEL KB; PROTEIN BARTTIN; UNCLASSIFIED DRUG;

EID: 84908417266     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00378     Document Type: Article
Times cited : (87)

References (138)
  • 1
    • 0035426049 scopus 로고    scopus 로고
    • Drastic reduction of the slow gate of human muscle chloride channel (ClC-1) by mutation C277S
    • Accardi, A., Ferrera, L., and Pusch, M. (2001). Drastic reduction of the slow gate of human muscle chloride channel (ClC-1) by mutation C277S. J. Physiol. 534, 745-752. doi: 10.1111/j.1469-7793.2001.00745.x
    • (2001) J. Physiol , vol.534 , pp. 745-752
    • Accardi, A.1    Ferrera, L.2    Pusch, M.3
  • 2
    • 33748798473 scopus 로고    scopus 로고
    • Synergism between halide binding and proton transport in a CLC-type exchanger
    • Accardi, A., Lobet, S., Williams, C., Miller, C., and Dutzler, R. (2006). Synergism between halide binding and proton transport in a CLC-type exchanger. J. Mol. Biol. 362, 691-699. doi: 10.1016/j.jmb.2006.07.081
    • (2006) J. Mol. Biol , vol.362 , pp. 691-699
    • Accardi, A.1    Lobet, S.2    Williams, C.3    Miller, C.4    Dutzler, R.5
  • 3
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels
    • Accardi, A., and Miller, C. (2004). Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels. Nature 427, 803-807. doi: 10.1038/nature02314
    • (2004) Nature , vol.427 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 4
    • 0033811517 scopus 로고    scopus 로고
    • Fast and slow gating relaxations in the muscle chloride channel ClC-1
    • Accardi, A., and Pusch, M. (2000). Fast and slow gating relaxations in the muscle chloride channel ClC-1. J. Gen. Physiol. 116, 433-444. doi: 10.1085/jgp.116.3.433
    • (2000) J. Gen. Physiol , vol.116 , pp. 433-444
    • Accardi, A.1    Pusch, M.2
  • 6
    • 0016166945 scopus 로고
    • On the repetitive discharge in myotonic muscle fibres
    • Adrian, R. H., and Bryant, S. H. (1974). On the repetitive discharge in myotonic muscle fibres. J. Physiol. 240, 505-515.
    • (1974) J. Physiol , vol.240 , pp. 505-515
    • Adrian, R.H.1    Bryant, S.H.2
  • 7
    • 34447345385 scopus 로고    scopus 로고
    • Common genetic variants and haplotypes in renal CLCNKA gene are associated to salt-sensitive hypertension
    • Barlassina, C., Fiume, C. D., Lanzani, C., Manunta, P., Guffanti, G., Ruello, A., et al. (2007). Common genetic variants and haplotypes in renal CLCNKA gene are associated to salt-sensitive hypertension. Hum. Mol. Genet. 16, 1630-1638. doi: 10.1093/hmg/ddm112
    • (2007) Hum. Mol. Genet , vol.16 , pp. 1630-1638
    • Barlassina, C.1    Fiume, C.D.2    Lanzani, C.3    Manunta, P.4    Guffanti, G.5    Ruello, A.6
  • 8
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • Bateman, A. (1997). The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 22, 12-13. doi: 10.1016/S0968-0004(96)30046-7
    • (1997) Trends Biochem. Sci , vol.22 , pp. 12-13
    • Bateman, A.1
  • 9
    • 0029763195 scopus 로고    scopus 로고
    • Molecular basis for decreased muscle chloride conductance in the myotonic goat
    • Beck, C. L., Fahlke, Ch., and George, A. L. (1996). Molecular basis for decreased muscle chloride conductance in the myotonic goat. Proc. Natl. Acad. Sci. U.S.A. 93, 11248-11252. doi: 10.1073/pnas.93.20.11248
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11248-11252
    • Beck, C.L.1    Fahlke, C.2    George, A.L.3
  • 10
    • 84885168677 scopus 로고    scopus 로고
    • Molecular determinants of common gating of a ClC chloride channel
    • Bennetts, B., and Parker, M. W. (2013). Molecular determinants of common gating of a ClC chloride channel. Nat. Commun. 4:2507. doi: 10.1038/ncomms3507
    • (2013) Nat. Commun , vol.4 , pp. 2507
    • Bennetts, B.1    Parker, M.W.2
  • 11
    • 33845596698 scopus 로고    scopus 로고
    • Patients with biallelic mutations in the chloride channel gene CLCNKB: long-term management and outcome
    • Bettinelli, A., Borsa, N., Bellantuono, R., Syrèn, M.-L., Calabrese, R., Edefonti, A., et al. (2007). Patients with biallelic mutations in the chloride channel gene CLCNKB: long-term management and outcome. Am. J. Kidney Dis. 49, 91-98. doi: 10.1053/j.ajkd.2006.10.001
    • (2007) Am. J. Kidney Dis , vol.49 , pp. 91-98
    • Bettinelli, A.1    Borsa, N.2    Bellantuono, R.3    Syrèn, M.-L.4    Calabrese, R.5    Edefonti, A.6
  • 12
    • 0035189356 scopus 로고    scopus 로고
    • Mutation of BSND causes Bartter syndrome with sensorineural deafness and kidney failure
    • Birkenhäger, R., Otto, E., Schürmann, M. J., Vollmer, M., Ruf, E. M., Maier-Lutz, I., et al. (2001). Mutation of BSND causes Bartter syndrome with sensorineural deafness and kidney failure. Nat. Genet. 29, 310-314. doi: 10.1038/ng752
    • (2001) Nat. Genet , vol.29 , pp. 310-314
    • Birkenhäger, R.1    Otto, E.2    Schürmann, M.J.3    Vollmer, M.4    Ruf, E.M.5    Maier-Lutz, I.6
  • 13
    • 34250339675 scopus 로고    scopus 로고
    • Leukoencephalopathy upon disruption of the chloride channel ClC-2
    • Blanz, J., Schweizer, M., Auberson, M., Maier, H., Muenscher, A., Hübner, C. A., et al. (2007). Leukoencephalopathy upon disruption of the chloride channel ClC-2. J. Neurosci. 27, 6581-6589. doi: 10.1523/JNEUROSCI.0338-07.2007
    • (2007) J. Neurosci , vol.27 , pp. 6581-6589
    • Blanz, J.1    Schweizer, M.2    Auberson, M.3    Maier, H.4    Muenscher, A.5    Hübner, C.A.6
  • 14
    • 0035868910 scopus 로고    scopus 로고
    • Male germ cells and photoreceptors, both dependent on close cell-cell interactions, degenerate upon ClC-2 Cl- channel disruption
    • Bösl, M. R., Stein, V., Hübner, C., Zdebik, A. A., Jordt, S.-E., Mukhopadhyay, A. K., et al. (2001). Male germ cells and photoreceptors, both dependent on close cell-cell interactions, degenerate upon ClC-2 Cl- channel disruption. EMBO J. 20, 1289-1299. doi: 10.1093/emboj/20.6.1289
    • (2001) EMBO J , vol.20 , pp. 1289-1299
    • Bösl, M.R.1    Stein, V.2    Hübner, C.3    Zdebik, A.A.4    Jordt, S.-E.5    Mukhopadhyay, A.K.6
  • 15
    • 0023238072 scopus 로고
    • Muscle chloride channels
    • Bretag, A. H. (1987). Muscle chloride channels. Physiol. Rev. 67, 618-724.
    • (1987) Physiol. Rev , vol.67 , pp. 618-724
    • Bretag, A.H.1
  • 16
    • 0007424242 scopus 로고
    • The electrophysiology of myotonia, with a review of congenital myotonia of goats
    • Bryant, S. H. (1973). "The electrophysiology of myotonia, with a review of congenital myotonia of goats," in New Developments in Electromyography and Clinical Neurophysiology, ed J. E. Desmedt (Basel: S. Karger), 420-450.
    • (1973) New Developments in Electromyography and Clinical Neurophysiology , pp. 420-450
    • Bryant, S.H.1
  • 17
    • 0015170319 scopus 로고
    • Chloride conductance in normal and myotonic muscle fibres and the action of monocarboxylic aromatic acids
    • Bryant, S. H., and Morales-Aguilera, A. (1971). Chloride conductance in normal and myotonic muscle fibres and the action of monocarboxylic aromatic acids. J. Physiol. 219, 367-383.
    • (1971) J. Physiol , vol.219 , pp. 367-383
    • Bryant, S.H.1    Morales-Aguilera, A.2
  • 18
    • 33845354986 scopus 로고    scopus 로고
    • Large movement in the C terminus of CLC-0 chloride channel during slow gating
    • Bykova, E. A., Zhang, X.-D., Chen, T.-Y., and Zheng, J. (2006). Large movement in the C terminus of CLC-0 chloride channel during slow gating. Nat. Struct. Mol. Biol. 13, 1115-1119. doi: 10.1038/nsmb1176
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 1115-1119
    • Bykova, E.A.1    Zhang, X.-D.2    Chen, T.-Y.3    Zheng, J.4
  • 19
    • 79952309013 scopus 로고    scopus 로고
    • Loss-of-function DNA sequence variant in the CLCNKA chloride channel implicates the cardio-renal axis in interindividual heart failure risk variation
    • Cappola, T. P., Matkovich, S. J., Wang, W., van Booven, D., Li, M., Wang, X., et al. (2011). Loss-of-function DNA sequence variant in the CLCNKA chloride channel implicates the cardio-renal axis in interindividual heart failure risk variation. Proc. Natl. Acad. Sci. U.S.A. 108, 2456-2461. doi: 10.1073/pnas.1017494108
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 2456-2461
    • Cappola, T.P.1    Matkovich, S.J.2    Wang, W.3    van Booven, D.4    Li, M.5    Wang, X.6
  • 21
    • 1842583683 scopus 로고    scopus 로고
    • Basolateral ClC-2 chloride channels in surface colon epithelium: regulation by a direct effect of intracellular chloride
    • Catalán, M., Niemeyer, M. I., Cid, L. P., and Sepúlveda, F. V. (2004). Basolateral ClC-2 chloride channels in surface colon epithelium: regulation by a direct effect of intracellular chloride. Gastroenterology 126, 1104-1114. doi: 10.1053/j.gastro.2004.01.010
    • (2004) Gastroenterology , vol.126 , pp. 1104-1114
    • Catalán, M.1    Niemeyer, M.I.2    Cid, L.P.3    Sepúlveda, F.V.4
  • 22
    • 84876251947 scopus 로고    scopus 로고
    • Novel brain expression of ClC-1 chloride channels and enrichment of CLCN1 variants in epilepsy
    • Chen, T. T., Klassen, T. L., Goldman, A. M., Marini, C., Guerrini, R., and Noebels, J. L. (2013). Novel brain expression of ClC-1 chloride channels and enrichment of CLCN1 variants in epilepsy. Neurology 80, 1078-1085. doi: 10.1212/WNL.0b013e31828868e7
    • (2013) Neurology , vol.80 , pp. 1078-1085
    • Chen, T.T.1    Klassen, T.L.2    Goldman, A.M.3    Marini, C.4    Guerrini, R.5    Noebels, J.L.6
  • 23
    • 77950370158 scopus 로고    scopus 로고
    • Disruption of ClC-2 expression is associated with progressive neurodegeneration in aging mice
    • Cortez, M. A., Li, C., Whitehead, S. N., Dhani, S. U., D'Antonio, C., Huan, L. J., et al. (2010). Disruption of ClC-2 expression is associated with progressive neurodegeneration in aging mice. Neuroscience 167, 154-162. doi: 10.1016/j.neuroscience.2010.01.042
    • (2010) Neuroscience , vol.167 , pp. 154-162
    • Cortez, M.A.1    Li, C.2    Whitehead, S.N.3    Dhani, S.U.4    D'Antonio, C.5    Huan, L.J.6
  • 24
    • 6044278151 scopus 로고    scopus 로고
    • SPI-0211 activates T84 cell chloride transport and recombinant human ClC-2 chloride currents
    • Cuppoletti, J., Malinowska, D. H., Tewari, K. P., Li, Q.-J., Sherry, A. M., Patchen, M. L., et al. (2004). SPI-0211 activates T84 cell chloride transport and recombinant human ClC-2 chloride currents. Am. J. Physiol. Cell Physiol. 287, C1173-C1183. doi: 10.1152/ajpcell.00528.2003
    • (2004) Am. J. Physiol. Cell Physiol , vol.287 , pp. C1173-C1183
    • Cuppoletti, J.1    Malinowska, D.H.2    Tewari, K.P.3    Li, Q.-J.4    Sherry, A.M.5    Patchen, M.L.6
  • 25
    • 7044262786 scopus 로고    scopus 로고
    • Mutations and polymorphisms of the CLCN2 gene in idiopathic epilepsy
    • D'Agostino, D., Bertelli, M., Gallo, S., Cecchin, S., Albiero, E., Garofalo, P. G., et al. (2004). Mutations and polymorphisms of the CLCN2 gene in idiopathic epilepsy. Neurology 63, 1500-1502. doi: 10.1212/01.WNL.0000142093.94998.1A
    • (2004) Neurology , vol.63 , pp. 1500-1502
    • D'Agostino, D.1    Bertelli, M.2    Gallo, S.3    Cecchin, S.4    Albiero, E.5    Garofalo, P.G.6
  • 26
    • 33947305641 scopus 로고    scopus 로고
    • Transporters as Channels
    • DeFelice, L. J., and Goswami, T. (2007). Transporters as Channels. Annu. Rev. Physiol. 69, 87-112. doi: 10.1146/annurev.physiol.69.031905.164816
    • (2007) Annu. Rev. Physiol , vol.69 , pp. 87-112
    • DeFelice, L.J.1    Goswami, T.2
  • 27
    • 84879026505 scopus 로고    scopus 로고
    • Brain white matter oedema due to ClC-2 chloride channel deficiency: an observational analytical study
    • Depienne, C., Bugiani, M., Dupuits, C., Galanaud, D., Touitou, V., Postma, N., et al. (2013). Brain white matter oedema due to ClC-2 chloride channel deficiency: an observational analytical study. Lancet Neurol. 12, 659-668. doi: 10.1016/S1474-4422(13)70053-X
    • (2013) Lancet Neurol , vol.12 , pp. 659-668
    • Depienne, C.1    Bugiani, M.2    Dupuits, C.3    Galanaud, D.4    Touitou, V.5    Postma, N.6
  • 28
    • 28244475369 scopus 로고    scopus 로고
    • Quantitative analysis of the voltage-dependent gating of mouse parotid ClC-2 chloride channel
    • De Santiago, J. A., Nehrke, K., and Arreola, J. (2005). Quantitative analysis of the voltage-dependent gating of mouse parotid ClC-2 chloride channel. J. Gen. Physiol. 126, 591-603. doi: 10.1085/jgp.200509310
    • (2005) J. Gen. Physiol , vol.126 , pp. 591-603
    • De Santiago, J.A.1    Nehrke, K.2    Arreola, J.3
  • 29
    • 36849079521 scopus 로고    scopus 로고
    • ATP depletion inhibits the endocytosis of ClC-2
    • Dhani, S. U., Kim Chiaw, P., Huan, L.-J., and Bear, C. E. (2008). ATP depletion inhibits the endocytosis of ClC-2. J. Cell. Physiol. 214, 273-280. doi: 10.1002/jcp.21192
    • (2008) J. Cell. Physiol , vol.214 , pp. 273-280
    • Dhani, S.U.1    Kim Chiaw, P.2    Huan, L.-J.3    Bear, C.E.4
  • 30
    • 78650887200 scopus 로고    scopus 로고
    • Chloride currents from the transverse tubular system in adult mammalian skeletal muscle fibers
    • DiFranco, M., Herrera, A., and Vergara, J. L. (2011). Chloride currents from the transverse tubular system in adult mammalian skeletal muscle fibers. J. Gen. Physiol. 137, 21-41. doi: 10.1085/jgp.201010496
    • (2011) J. Gen. Physiol , vol.137 , pp. 21-41
    • DiFranco, M.1    Herrera, A.2    Vergara, J.L.3
  • 31
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity
    • Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., and MacKinnon, R. (2002). X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 415, 287-294. doi: 10.1038/415287a
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 32
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., Campbell, E. B., and MacKinnon, R. (2003). Gating the selectivity filter in ClC chloride channels. Science 300, 108-112. doi: 10.1126/science.1082708
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 33
    • 0035969520 scopus 로고    scopus 로고
    • Barttin is a Cl- channel beta-subunit crucial for renal Cl- reabsorption and inner ear K+ secretion
    • Estévez, R., Boettger, T., Stein, V., Birkenhäger, R., Otto, E., Hildebrandt, F., et al. (2001). Barttin is a Cl- channel beta-subunit crucial for renal Cl- reabsorption and inner ear K+ secretion. Nature 414, 558-561. doi: 10.1038/35107099
    • (2001) Nature , vol.414 , pp. 558-561
    • Estévez, R.1    Boettger, T.2    Stein, V.3    Birkenhäger, R.4    Otto, E.5    Hildebrandt, F.6
  • 34
    • 3042648417 scopus 로고    scopus 로고
    • Functional and structural conservation of CBS domains from CLC chloride channels
    • Estévez, R., Pusch, M., Ferrer-Costa, C., Orozco, M., and Jentsch, T. J. (2004). Functional and structural conservation of CBS domains from CLC chloride channels. J. Physiol. 557, 363-378. doi: 10.1113/jphysiol.2003.058453
    • (2004) J. Physiol , vol.557 , pp. 363-378
    • Estévez, R.1    Pusch, M.2    Ferrer-Costa, C.3    Orozco, M.4    Jentsch, T.J.5
  • 35
    • 79961135175 scopus 로고    scopus 로고
    • Physiology and pathophysiology of ClC-K/barttin channels
    • Fahlke, Ch., and Fischer, M. (2010). Physiology and pathophysiology of ClC-K/barttin channels. Front. Physiol. 1:155. doi: 10.3389/fphys.2010.00155
    • (2010) Front. Physiol , vol.1 , pp. 155
    • Fahlke, C.1    Fischer, M.2
  • 36
    • 0028950604 scopus 로고
    • Chloride currents across the membrane of mammalian skeletal muscle fibres
    • Fahlke, Ch., and Rüdel, R. (1995). Chloride currents across the membrane of mammalian skeletal muscle fibres. J. Physiol. 484, 355-368.
    • (1995) J. Physiol , vol.484 , pp. 355-368
    • Fahlke, C.1    Rüdel, R.2
  • 37
    • 0029162517 scopus 로고
    • An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels
    • Fahlke, Ch., Rüdel, R., Mitrovic, N., Zhou, M., and George, A. L. Jr. (1995). An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels. Neuron 15, 463-472. doi: 10.1016/0896-6273(95)90050-0
    • (1995) Neuron , vol.15 , pp. 463-472
    • Fahlke, C.1    Rüdel, R.2    Mitrovic, N.3    Zhou, M.4    George Jr., A.L.5
  • 38
    • 0031468569 scopus 로고    scopus 로고
    • Pore-forming segments in voltage-gated chloride channels
    • Fahlke, Ch., Yu, H. T., Beck, C. L., Rhodes, T. H., and George, A. L. (1997). Pore-forming segments in voltage-gated chloride channels. Nature 390, 529-532. doi: 10.1038/37391
    • (1997) Nature , vol.390 , pp. 529-532
    • Fahlke, C.1    Yu, H.T.2    Beck, C.L.3    Rhodes, T.H.4    George, A.L.5
  • 39
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng, L., Campbell, E. B., Hsiung, Y., and MacKinnon, R. (2010). Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330, 635-641. doi: 10.1126/science.1195230
    • (2010) Science , vol.330 , pp. 635-641
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 40
    • 77955625453 scopus 로고    scopus 로고
    • Barttin activates ClC-K channel function by modulating gating
    • Fischer, M., Janssen, A. G. H., and Fahlke, Ch. (2010). Barttin activates ClC-K channel function by modulating gating. J. Am. Soc. Nephrol. 21, 1281-1289. doi: 10.1681/ASN.2009121274
    • (2010) J. Am. Soc. Nephrol , vol.21 , pp. 1281-1289
    • Fischer, M.1    Janssen, A.G.H.2    Fahlke, C.3
  • 41
    • 77956187511 scopus 로고    scopus 로고
    • Regulation of fast-spiking basket cell synapses by the chloride channel ClC-2
    • Földy, C., Lee, S.-H., Morgan, R. J., and Soltesz, I. (2010). Regulation of fast-spiking basket cell synapses by the chloride channel ClC-2. Nat. Neurosci. 13, 1047-1049. doi: 10.1038/nn.2609
    • (2010) Nat. Neurosci , vol.13 , pp. 1047-1049
    • Földy, C.1    Lee, S.-H.2    Morgan, R.J.3    Soltesz, I.4
  • 42
    • 33646051988 scopus 로고    scopus 로고
    • Influence of gain of function epithelial chloride channel ClC-Kb mutation on hearing thresholds
    • Frey, A., Lampert, A., Waldegger, S., Jeck, N., Waldegger, P., Artunc, F., et al. (2006). Influence of gain of function epithelial chloride channel ClC-Kb mutation on hearing thresholds. Hear. Res. 214, 68-75. doi: 10.1016/j.heares.2006.02.001
    • (2006) Hear. Res , vol.214 , pp. 68-75
    • Frey, A.1    Lampert, A.2    Waldegger, S.3    Jeck, N.4    Waldegger, P.5    Artunc, F.6
  • 43
    • 8744242213 scopus 로고    scopus 로고
    • Novel mutations of the chloride channel Kb gene in two japanese patients clinically diagnosed as bartter syndrome with hypocalciuria
    • Fukuyama, S., Hiramatsu, M., Akagi, M., Higa, M., and Ohta, T. (2004). Novel mutations of the chloride channel Kb gene in two japanese patients clinically diagnosed as bartter syndrome with hypocalciuria. J. Clin. Endocrinol. Metab. 89, 5847-5850. doi: 10.1210/jc.2004-0775
    • (2004) J. Clin. Endocrinol. Metab , vol.89 , pp. 5847-5850
    • Fukuyama, S.1    Hiramatsu, M.2    Akagi, M.3    Higa, M.4    Ohta, T.5
  • 44
    • 56649100778 scopus 로고    scopus 로고
    • Gating of human ClC-2 chloride channels and regulation by carboxy-terminal domains
    • Garcia-Olivares, J., Alekov, A., Boroumand, M. R., Begemann, B., Hidalgo, P., and Fahlke, Ch. (2008). Gating of human ClC-2 chloride channels and regulation by carboxy-terminal domains. J. Physiol. 586, 5325-5336. doi: 10.1113/jphysiol.2008.158097
    • (2008) J. Physiol , vol.586 , pp. 5325-5336
    • Garcia-Olivares, J.1    Alekov, A.2    Boroumand, M.R.3    Begemann, B.4    Hidalgo, P.5    Fahlke, C.6
  • 45
    • 0027481915 scopus 로고
    • Molecular basis of Thomsen's disease (autosomal dominant myotonia congenita)
    • George, A. L., Crackower, M. A., Abdalla, J. A., Hudson, A. J., and Ebers, G. C. (1993). Molecular basis of Thomsen's disease (autosomal dominant myotonia congenita). Nat. Genet. 3, 305-310. doi: 10.1038/ng0493-305
    • (1993) Nat. Genet , vol.3 , pp. 305-310
    • George, A.L.1    Crackower, M.A.2    Abdalla, J.A.3    Hudson, A.J.4    Ebers, G.C.5
  • 46
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux, E., and MacKinnon, R. (2005). Principles of selective ion transport in channels and pumps. Science 310, 1461-1465. doi: 10.1126/science.1113666
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2
  • 47
    • 77956253091 scopus 로고    scopus 로고
    • A regulatory calcium-binding site at the subunit interface of CLC-K kidney chloride channels
    • Gradogna, A., Babini, E., Picollo, A., and Pusch, M. (2010). A regulatory calcium-binding site at the subunit interface of CLC-K kidney chloride channels. J. Gen. Physiol. 136, 311-323. doi: 10.1085/jgp.201010455
    • (2010) J. Gen. Physiol , vol.136 , pp. 311-323
    • Gradogna, A.1    Babini, E.2    Picollo, A.3    Pusch, M.4
  • 48
    • 0027051182 scopus 로고
    • Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume
    • Gründer, S., Thiemann, A., Pusch, M., and Jentsch, T. J. (1992). Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume. Nature 360, 759-762. doi: 10.1038/360759a0
    • (1992) Nature , vol.360 , pp. 759-762
    • Gründer, S.1    Thiemann, A.2    Pusch, M.3    Jentsch, T.J.4
  • 49
    • 84879773470 scopus 로고    scopus 로고
    • ClC-3 Is an intracellular chloride/proton exchanger with large voltage-dependent nonlinear capacitance
    • Guzman, R. E., Grieschat, M., Fahlke, Ch., and Alekov, A. K. (2013). ClC-3 Is an intracellular chloride/proton exchanger with large voltage-dependent nonlinear capacitance. ACS Chem. Neurosci. 4, 994-1003. doi: 10.1021/cn400032z
    • (2013) ACS Chem. Neurosci , vol.4 , pp. 994-1003
    • Guzman, R.E.1    Grieschat, M.2    Fahlke, C.3    Alekov, A.K.4
  • 50
    • 0042166134 scopus 로고    scopus 로고
    • Molecular mechanisms of Bartter syndrome caused by mutations in the BSND gene
    • Hayama, A., Rai, T., Sasaki, S., and Uchida, S. (2003). Molecular mechanisms of Bartter syndrome caused by mutations in the BSND gene. Histochem. Cell Biol. 119, 485-493. doi: 10.1007/s00418-003-0535-2
    • (2003) Histochem. Cell Biol , vol.119 , pp. 485-493
    • Hayama, A.1    Rai, T.2    Sasaki, S.3    Uchida, S.4
  • 51
    • 1842424664 scopus 로고    scopus 로고
    • The role of the Carboxyl Terminus in ClC chloride channel function
    • Hebeisen, S., Biela, A., Giese, B., Müller-Newen, G., Hidalgo, P., and Fahlke, Ch. (2004). The role of the Carboxyl Terminus in ClC chloride channel function. J. Biol. Chem. 279, 13140-13147. doi: 10.1074/jbc. M312649200
    • (2004) J. Biol. Chem , vol.279 , pp. 13140-13147
    • Hebeisen, S.1    Biela, A.2    Giese, B.3    Müller-Newen, G.4    Hidalgo, P.5    Fahlke, C.6
  • 52
    • 24144461620 scopus 로고    scopus 로고
    • Carboxy-terminal truncations modify the outer pore vestibule of muscle chloride channels
    • Hebeisen, S., and Fahlke, Ch. (2005). Carboxy-terminal truncations modify the outer pore vestibule of muscle chloride channels. Biophys. J. 89, 1710-1720. doi: 10.1529/biophysj.104.056093
    • (2005) Biophys. J. , vol.89
    • Hebeisen, S.1    Fahlke, C.2
  • 53
    • 34047250328 scopus 로고    scopus 로고
    • Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress
    • Hinzpeter, A., Fritsch, J., Borot, F., Trudel, S., Vieu, D.-L., Brouillard, F., et al. (2007). Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress. J. Biol. Chem. 282, 2423-2432. doi: 10.1074/jbc. M608251200
    • (2007) J. Biol. Chem , vol.282
    • Hinzpeter, A.1    Fritsch, J.2    Borot, F.3    Trudel, S.4    Vieu, D.-L.5    Brouillard, F.6
  • 54
    • 70449308592 scopus 로고
    • The influence of potassium and chloride ions on the membrane potential of single muscle fibres
    • Hodgkin, A. L., and Horowicz, P. (1959). The influence of potassium and chloride ions on the membrane potential of single muscle fibres. J. Physiol. 148, 127-160.
    • (1959) J. Physiol. , vol.148 , pp. 127-160
    • Hodgkin, A.L.1    Horowicz, P.2
  • 55
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin, A. L., and Huxley, A. F. (1952). A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117, 500-544.
    • (1952) J. Physiol , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 56
    • 84901924901 scopus 로고    scopus 로고
    • Disrupting MLC1 and GlialCAM and ClC-2 interactions in leukodystrophy entails glial chloride channel dysfunction
    • Hoegg-Beiler, M. B., Sirisi, S., Orozco, I. J., Ferrer, I., Hohensee, S., Auberson, M., et al. (2014). Disrupting MLC1 and GlialCAM and ClC-2 interactions in leukodystrophy entails glial chloride channel dysfunction. Nat. Commun. 5:3475. doi: 10.1038/ncomms4475
    • (2014) Nat. Commun. , vol.5 , pp. 3475
    • Hoegg-Beiler, M.B.1    Sirisi, S.2    Orozco, I.J.3    Ferrer, I.4    Hohensee, S.5    Auberson, M.6
  • 57
    • 59849125866 scopus 로고    scopus 로고
    • Cereblon is expressed in the retina and binds to voltage-gated chloride channels
    • Hohberger, B., and Enz, R. (2009). Cereblon is expressed in the retina and binds to voltage-gated chloride channels. FEBS Lett. 583, 633-637. doi: 10.1016/j.febslet.2009.01.018
    • (2009) FEBS Lett , vol.583 , pp. 633-637
    • Hohberger, B.1    Enz, R.2
  • 58
    • 84903413891 scopus 로고    scopus 로고
    • Targeting kidney CLC-K channels: pharmacological profile in a human cell line versus Xenopus oocytes. Biochim
    • Imbrici, P., Liantonio, A., Gradogna, A., Pusch, M., and Camerino, D. C. (2014). Targeting kidney CLC-K channels: pharmacological profile in a human cell line versus Xenopus oocytes. Biochim. Biophys. Acta 1838, 2484-2491. doi: 10.1016/j.bbamem.2014.05.017
    • (2014) Biophys. Acta , vol.1838 , pp. 2484-2491
    • Imbrici, P.1    Liantonio, A.2    Gradogna, A.3    Pusch, M.4    Camerino, D.C.5
  • 60
    • 49649112453 scopus 로고    scopus 로고
    • Ion permeation through a Cl--selective channel designed from a CLC Cl-/H+ exchanger
    • Jayaram, H., Accardi, A., Wu, F., Williams, C., and Miller, C. (2008). Ion permeation through a Cl--selective channel designed from a CLC Cl-/H+ exchanger. Proc. Natl. Acad. Sci. U.S.A. 105, 11194-11199. doi: 10.1073/pnas.0804503105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 11194-11199
    • Jayaram, H.1    Accardi, A.2    Wu, F.3    Williams, C.4    Miller, C.5
  • 61
    • 79952074056 scopus 로고    scopus 로고
    • Structure of a slow CLC Cl-/H+ antiporter from a cyanobacterium
    • Jayaram, H., Robertson, J. L., Wu, F., Williams, C., and Miller, C. (2011). Structure of a slow CLC Cl-/H+ antiporter from a cyanobacterium. Biochemistry 50, 788-794. doi: 10.1021/bi1019258
    • (2011) Biochemistry , vol.50 , pp. 788-794
    • Jayaram, H.1    Robertson, J.L.2    Wu, F.3    Williams, C.4    Miller, C.5
  • 62
    • 0347362500 scopus 로고    scopus 로고
    • A common sequence variation of the CLCNKB gene strongly activates ClC-Kb chloride channel activity
    • Jeck, N., Waldegger, P., Doroszewicz, J., Seyberth, H., and Waldegger, S. (2004). A common sequence variation of the CLCNKB gene strongly activates ClC-Kb chloride channel activity. Kidney Int. 65, 190-197. doi: 10.1111/j.1523-1755.2004.00363.x
    • (2004) Kidney Int , vol.65
    • Jeck, N.1    Waldegger, P.2    Doroszewicz, J.3    Seyberth, H.4    Waldegger, S.5
  • 63
    • 84879009837 scopus 로고    scopus 로고
    • From mice to man: chloride transport in leukoencephalopathy
    • Jentsch, T. J. (2013). From mice to man: chloride transport in leukoencephalopathy. Lancet Neurol. 12, 626-628. doi: 10.1016/S1474-4422(13)70068-1
    • (2013) Lancet Neurol , vol.12 , pp. 626-628
    • Jentsch, T.J.1
  • 64
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes
    • Jentsch, T. J., Steinmeyer, K., and Schwarz, G. (1990). Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 348, 510-514. doi: 10.1038/348510a0
    • (1990) Nature , vol.348 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 65
    • 84908401839 scopus 로고    scopus 로고
    • GlialCAM, a CLC-2 Cl- Channel subunit, activates the slow gate of CLC chloride channels
    • Jeworutzki, E., Lagostena, L., Elorza-Vidal, X., López-Hernández, T., Estévez, R., and Pusch, M. (2014). GlialCAM, a CLC-2 Cl- Channel subunit, activates the slow gate of CLC chloride channels. Biophys. J. 107, 1105-1116. doi: 10.1016/j.bpj.2014.07.040
    • (2014) Biophys. J. , vol.107 , pp. 1105-1116
    • Jeworutzki, E.1    Lagostena, L.2    Elorza-Vidal, X.3    López-Hernández, T.4    Estévez, R.5    Pusch, M.6
  • 66
    • 84858019171 scopus 로고    scopus 로고
    • GlialCAM, a protein defective in a leukodystrophy, serves as a ClC-2 Cl- channel auxiliary subunit
    • Jeworutzki, E., López-Hernández, T., Capdevila-Nortes, X., Sirisi, S., Bengtsson, L., Montolio, M., et al. (2012). GlialCAM, a protein defective in a leukodystrophy, serves as a ClC-2 Cl- channel auxiliary subunit. Neuron 73, 951-961. doi: 10.1016/j.neuron.2011.12.039
    • (2012) Neuron , vol.73 , pp. 951-961
    • Jeworutzki, E.1    López-Hernández, T.2    Capdevila-Nortes, X.3    Sirisi, S.4    Bengtsson, L.5    Montolio, M.6
  • 67
    • 0019479992 scopus 로고
    • Labyrinthine barriers and cochlear homeostasis
    • Juhn, S. K., and Rybak, L. P. (1981). Labyrinthine barriers and cochlear homeostasis. Acta Otolaryngol. 91, 529-534. doi: 10.3109/00016488109138538
    • (1981) Acta Otolaryngol , vol.91 , pp. 529-534
    • Juhn, S.K.1    Rybak, L.P.2
  • 68
    • 0028360729 scopus 로고
    • Two highly homologous members of the CLC chloride channel family in both rat and human kidney
    • Kieferle, S., Fong, P., Bens, M., Vandewalle, A., and Jentsch, T. J. (1994). Two highly homologous members of the CLC chloride channel family in both rat and human kidney. Proc. Natl. Acad. Sci. U.S.A. 91, 6943-6947. doi: 10.1073/pnas.91.15.6943
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6943-6947
    • Kieferle, S.1    Fong, P.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 69
    • 79959667218 scopus 로고    scopus 로고
    • Exome sequencing of ion channel genes reveals complex profiles confounding personal risk assessment in epilepsy
    • Klassen, T., Davis, C., Goldman, A., Burgess, D., Chen, T., Wheeler, D., et al. (2011). Exome sequencing of ion channel genes reveals complex profiles confounding personal risk assessment in epilepsy. Cell 145, 1036-1048. doi: 10.1016/j.cell.2011.05.025
    • (2011) Cell , vol.145 , pp. 1036-1048
    • Klassen, T.1    Davis, C.2    Goldman, A.3    Burgess, D.4    Chen, T.5    Wheeler, D.6
  • 71
    • 0026705098 scopus 로고
    • The skeletal muscle chloride channel in dominant and recessive human myotonia
    • Koch, M. C., Steinmeyer, K., Lorenz, C., Ricker, K., Wolf, F., Otto, M., et al. (1992). The skeletal muscle chloride channel in dominant and recessive human myotonia. Science 257, 797-800. doi: 10.1126/science.1379744
    • (1992) Science , vol.257 , pp. 797-800
    • Koch, M.C.1    Steinmeyer, K.2    Lorenz, C.3    Ricker, K.4    Wolf, F.5    Otto, M.6
  • 72
    • 84873733768 scopus 로고    scopus 로고
    • Myotonia congenita mutation enhances the degradation of human CLC-1 chloride channels
    • Lee, T.-T., Zhang, X.-D., Chuang, C.-C., Chen, J.-J., Chen, Y.-A., Chen, S.-C., et al. (2013). Myotonia congenita mutation enhances the degradation of human CLC-1 chloride channels. PLoS ONE 8:e55930. doi: 10.1371/journal.pone.0055930
    • (2013) PLoS ONE , vol.8 , pp. e55930
    • Lee, T.-T.1    Zhang, X.-D.2    Chuang, C.-C.3    Chen, J.-J.4    Chen, Y.-A.5    Chen, S.-C.6
  • 73
    • 0035072651 scopus 로고    scopus 로고
    • Mutations of MLC1 (KIAA0027), encoding a putative membrane protein, cause megalencephalic leukoencephalopathy with subcortical cysts
    • Leegwater, P. A. J., Yuan, B. Q., van der Steen, J., Mulders, J., Könst, A. A. M., Boor, P. K. I., et al. (2001). Mutations of MLC1 (KIAA0027), encoding a putative membrane protein, cause megalencephalic leukoencephalopathy with subcortical cysts. Am. J. Hum. Genet. 68, 831-838. doi: 10.1086/319519
    • (2001) Am. J. Hum. Genet , vol.68 , pp. 831-838
    • Leegwater, P.A.J.1    Yuan, B.Q.2    van der Steen, J.3    Mulders, J.4    Könst, A.A.M.5    Boor, P.K.I.6
  • 74
    • 79957896458 scopus 로고    scopus 로고
    • ClC-7 is a slowly voltage-gated 2Cl-/1H+-exchanger and requires Ostm1 for transport activity
    • Leisle, L., Ludwig, C. F., Wagner, F. A., Jentsch, T. J., and Stauber, T. (2011). ClC-7 is a slowly voltage-gated 2Cl-/1H+-exchanger and requires Ostm1 for transport activity. EMBO J. 30, 2140-2152. doi: 10.1038/emboj.2011.137
    • (2011) EMBO J , vol.30 , pp. 2140-2152
    • Leisle, L.1    Ludwig, C.F.2    Wagner, F.A.3    Jentsch, T.J.4    Stauber, T.5
  • 75
    • 83555164699 scopus 로고    scopus 로고
    • In vivo administration of CLC-K kidney chloride channels inhibitors increases water diuresis in rats: a new drug target for hypertension?
    • Liantonio, A., Gramegna, G., Camerino, G. M., Dinardo, M. M., Scaramuzzi, A., Potenza, M. A., et al. (2012). In vivo administration of CLC-K kidney chloride channels inhibitors increases water diuresis in rats: a new drug target for hypertension? J. Hypertens. 30, 153-167. doi: 10.1097/HJH.0b013e32834d9eb9
    • (2012) J. Hypertens. , vol.30 , pp. 153-167
    • Liantonio, A.1    Gramegna, G.2    Camerino, G.M.3    Dinardo, M.M.4    Scaramuzzi, A.5    Potenza, M.A.6
  • 76
    • 30044450910 scopus 로고    scopus 로고
    • Activation and inhibition of kidney CLC-K chloride channels by fenamates
    • Liantonio, A., Picollo, A., Babini, E., Carbonara, G., Fracchiolla, G., Loiodice, F., et al. (2006). Activation and inhibition of kidney CLC-K chloride channels by fenamates. Mol. Pharmacol. 69, 165-173. doi: 10.1124/mol.105.017384
    • (2006) Mol. Pharmacol , vol.69 , pp. 165-173
    • Liantonio, A.1    Picollo, A.2    Babini, E.3    Carbonara, G.4    Fracchiolla, G.5    Loiodice, F.6
  • 77
    • 84871701543 scopus 로고    scopus 로고
    • Intracellular proton access in a Cl-/H+ antiporter
    • Lim, H.-H., Shane, T., and Miller, C. (2012). Intracellular proton access in a Cl-/H+ antiporter. PLoS Biol. 10:e1001441. doi: 10.1371/journal.pbio.1001441
    • (2012) PLoS Biol , vol.10 , pp. e1001441
    • Lim, H.-H.1    Shane, T.2    Miller, C.3
  • 78
    • 0033000370 scopus 로고    scopus 로고
    • Elimination of the slow gating of Clc-0 chloride channel by a point mutation
    • Lin, Y.-W., Lin, C.-W., and Chen, T.-Y. (1999). Elimination of the slow gating of Clc-0 chloride channel by a point mutation. J. Gen. Physiol. 114, 1-12. doi: 10.1085/jgp.114.1.1
    • (1999) J. Gen. Physiol. , vol.114 , pp. 1-12
    • Lin, Y.-W.1    Lin, C.-W.2    Chen, T.-Y.3
  • 79
    • 30444442312 scopus 로고    scopus 로고
    • Ion-binding properties of the ClC chloride selectivity filter
    • Lobet, S., and Dutzler, R. (2006). Ion-binding properties of the ClC chloride selectivity filter. EMBO J. 25, 24-33. doi: 10.1038/sj.emboj.7600909
    • (2006) EMBO J , vol.25 , pp. 24-33
    • Lobet, S.1    Dutzler, R.2
  • 80
    • 0029843417 scopus 로고    scopus 로고
    • Heteromultimeric CLC chloride channels with novel properties
    • Lorenz, C., Pusch, M., and Jentsch, T. J. (1996). Heteromultimeric CLC chloride channels with novel properties. Proc. Natl. Acad. Sci. U.S.A. 93, 13362-13366. doi: 10.1073/pnas.93.23.13362
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13362-13366
    • Lorenz, C.1    Pusch, M.2    Jentsch, T.J.3
  • 81
    • 78650063521 scopus 로고    scopus 로고
    • Sarcolemmal-restricted localization of functional ClC-1 channels in mouse skeletal muscle
    • Lueck, J. D., Rossi, A. E., Thornton, C. A., Campbell, K. P., and Dirksen, R. T. (2010). Sarcolemmal-restricted localization of functional ClC-1 channels in mouse skeletal muscle. J. Gen. Physiol. 136, 597-613. doi: 10.1085/jgp.201010526
    • (2010) J. Gen. Physiol. , vol.136 , pp. 597-613
    • Lueck, J.D.1    Rossi, A.E.2    Thornton, C.A.3    Campbell, K.P.4    Dirksen, R.T.5
  • 82
    • 79955981353 scopus 로고    scopus 로고
    • Movement of hClC-1 C-termini during common gating and limits on their cytoplasmic location
    • Ma, L., Rychkov, G. Y., Bykova, E. A., Zheng, J., and Bretag, A. H. (2011). Movement of hClC-1 C-termini during common gating and limits on their cytoplasmic location. Biochem. J. 436, 415-428. doi: 10.1042/BJ20102153
    • (2011) Biochem. J. , vol.436 , pp. 415-428
    • Ma, L.1    Rychkov, G.Y.2    Bykova, E.A.3    Zheng, J.4    Bretag, A.H.5
  • 83
    • 0032477820 scopus 로고    scopus 로고
    • Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains
    • Maduke, M., Williams, C., and Miller, C. (1998). Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains. Biochemistry 37, 1315-1321. doi: 10.1021/bi972418o
    • (1998) Biochemistry , vol.37 , pp. 1315-1321
    • Maduke, M.1    Williams, C.2    Miller, C.3
  • 84
    • 50249151393 scopus 로고    scopus 로고
    • A cytoplasmic domain mutation in ClC-Kb affects long-distance communication across the membrane
    • Martinez, G. Q., and Maduke, M. (2008). A cytoplasmic domain mutation in ClC-Kb affects long-distance communication across the membrane. PLoS ONE 3:e2746. doi: 10.1371/journal.pone.0002746
    • (2008) PLoS ONE , vol.3 , pp. e2746
    • Martinez, G.Q.1    Maduke, M.2
  • 85
    • 0032947011 scopus 로고    scopus 로고
    • Overt nephrogenic diabetes insipidus in mice lacking the CLC-K1 chloride channel
    • Matsumura, Y., Uchida, S., Kondo, Y., Miyazaki, H., Ko, S. B., Hayama, A., et al. (1999). Overt nephrogenic diabetes insipidus in mice lacking the CLC-K1 chloride channel. Nat. Genet. 21, 95-98. doi: 10.1038/5036
    • (1999) Nat. Genet. , vol.21 , pp. 95-98
    • Matsumura, Y.1    Uchida, S.2    Kondo, Y.3    Miyazaki, H.4    Ko, S.B.5    Hayama, A.6
  • 86
    • 33846076778 scopus 로고    scopus 로고
    • Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5
    • Meyer, S., Savaresi, S., Forster, I. C., and Dutzler, R. (2007). Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5. Nat. Struct. Mol. Biol. 14, 60-67. doi: 10.1038/nsmb1188
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 60-67
    • Meyer, S.1    Savaresi, S.2    Forster, I.C.3    Dutzler, R.4
  • 87
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax. Philos
    • Miller, C. (1982). Open-state substructure of single chloride channels from Torpedo electroplax. Philos. Trans. R. Soc. Lond. B Biol. Sci. 299, 401-411. doi: 10.1098/rstb.1982.0140
    • (1982) Trans. R. Soc. Lond. B Biol. Sci. , vol.299 , pp. 401-411
    • Miller, C.1
  • 88
    • 0041358801 scopus 로고    scopus 로고
    • ClC channels reading eukaryotic function through prokaryotic spectacles
    • Miller, C. (2003). ClC channels reading eukaryotic function through prokaryotic spectacles. J. Gen. Physiol. 122, 129-131. doi: 10.1085/jgp.200308898
    • (2003) J. Gen. Physiol. , vol.122 , pp. 129-131
    • Miller, C.1
  • 89
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • Miller, C., and White, M. M. (1984). Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl. Acad. Sci. U.S.A. 81, 2772-2775. doi: 10.1073/pnas.81.9.2772
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 90
    • 0032945795 scopus 로고    scopus 로고
    • Comparison of amphibian and human ClC-5: similarity of functional properties and inhibition by external Ph
    • Mo, L., Hellmich, H. L., Fong, P., Wood, T., Embesi, J., and Wills, N. K. (1999). Comparison of amphibian and human ClC-5: similarity of functional properties and inhibition by external pH. J. Membr. Biol. 168, 253-264. doi: 10.1007/s002329900514
    • (1999) J. Membr. Biol. , vol.168 , pp. 253-264
    • Mo, L.1    Hellmich, H.L.2    Fong, P.3    Wood, T.4    Embesi, J.5    Wills, N.K.6
  • 91
    • 77954357979 scopus 로고    scopus 로고
    • The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression
    • Neagoe, I., Stauber, T., Fidzinski, P., Bergsdorf, E.-Y., and Jentsch, T. J. (2010). The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression. J. Biol. Chem. 285, 21689-21697. doi: 10.1074/jbc. M110.125971
    • (2010) J. Biol. Chem. , vol.285 , pp. 21689-21697
    • Neagoe, I.1    Stauber, T.2    Fidzinski, P.3    Bergsdorf, E.-Y.4    Jentsch, T.J.5
  • 92
    • 0037189525 scopus 로고    scopus 로고
    • Loss of hyperpolarization-activated Cl- current in salivary acinar cells from Clcn2 knockout mice
    • Nehrke, K., Arreola, J., Nguyen, H.-V., Pilato, J., Richardson, L., Okunade, G., et al. (2002). Loss of hyperpolarization-activated Cl- current in salivary acinar cells from Clcn2 knockout mice. J. Biol. Chem. 277, 23604-23611. doi: 10.1074/jbc. M202900200
    • (2002) J. Biol. Chem. , vol.277 , pp. 23604-23611
    • Nehrke, K.1    Arreola, J.2    Nguyen, H.-V.3    Pilato, J.4    Richardson, L.5    Okunade, G.6
  • 93
    • 73349099352 scopus 로고    scopus 로고
    • No evidence for a role of CLCN2 variants in idiopathic generalized epilepsy
    • Niemeyer, M. I., Cid, L. P., Sepúlveda, F. V., Blanz, J., Auberson, M., and Jentsch, T. J. (2010). No evidence for a role of CLCN2 variants in idiopathic generalized epilepsy. Nat. Genet. 42, 3. doi: 10.1038/ng0110-3
    • (2010) Nat. Genet. , vol.42 , Issue.3
    • Niemeyer, M.I.1    Cid, L.P.2    Sepúlveda, F.V.3    Blanz, J.4    Auberson, M.5    Jentsch, T.J.6
  • 94
    • 0345767047 scopus 로고    scopus 로고
    • A conserved pore-lining glutamate as a voltage- and chloride-dependent gate in the ClC-2 chloride channel
    • Niemeyer, M. I., Cid, L. P., Zúñiga, L., Catalán, M., and Sepúlveda, F. V. (2003). A conserved pore-lining glutamate as a voltage- and chloride-dependent gate in the ClC-2 chloride channel. J. Physiol. 553, 873-879. doi: 10.1113/jphysiol.2003.055988
    • (2003) J. Physiol. , vol.553 , pp. 873-879
    • Niemeyer, M.I.1    Cid, L.P.2    Zúñiga, L.3    Catalán, M.4    Sepúlveda, F.V.5
  • 95
    • 7944234789 scopus 로고    scopus 로고
    • Functional evaluation of human ClC-2 chloride channel mutations associated with idiopathic generalized epilepsies. Physiol
    • Niemeyer, M. I., Yusef, Y. R., Cornejo, I., Flores, C. A., Sepúlveda, F. V., and Cid, L. P. (2004). Functional evaluation of human ClC-2 chloride channel mutations associated with idiopathic generalized epilepsies. Physiol. Genomics 19, 74-83. doi: 10.1152/physiolgenomics.00070.2004
    • (2004) Genomics , vol.19 , pp. 74-83
    • Niemeyer, M.I.1    Yusef, Y.R.2    Cornejo, I.3    Flores, C.A.4    Sepúlveda, F.V.5    Cid, L.P.6
  • 97
    • 8644269702 scopus 로고    scopus 로고
    • Heterogeneous distribution of chloride channels along the distal convoluted tubule probed by single-cell RT-PCR and patch clamp
    • Nissant, A., Lourdel, S., Baillet, S., Paulais, M., Marvao, P., Teulon, J., et al. (2004). Heterogeneous distribution of chloride channels along the distal convoluted tubule probed by single-cell RT-PCR and patch clamp. Am. J. Physiol. Ren. Physiol. 287, F1233-F1243. doi: 10.1152/ajprenal.00155.2004
    • (2004) Am. J. Physiol. Ren. Physiol. , vol.287 , pp. F1233-F1243
    • Nissant, A.1    Lourdel, S.2    Baillet, S.3    Paulais, M.4    Marvao, P.5    Teulon, J.6
  • 98
    • 0034637457 scopus 로고    scopus 로고
    • Single-channel analysis of a ClC-2-like chloride conductance in cultured rat cortical astrocytes
    • Nobile, M., Pusch, M., Rapisarda, C., and Ferroni, S. (2000). Single-channel analysis of a ClC-2-like chloride conductance in cultured rat cortical astrocytes. FEBS Lett. 479, 10-14. doi: 10.1016/S0014-5793(00)01876-7
    • (2000) FEBS Lett , vol.479 , pp. 10-14
    • Nobile, M.1    Pusch, M.2    Rapisarda, C.3    Ferroni, S.4
  • 100
    • 0036264983 scopus 로고    scopus 로고
    • Aldosterone and high-NaCl diet modulate ClC-2 chloride channel gene expression in rat kidney
    • Ornellas, D. S., Nascimento, D. S., Christoph, D. H., Guggino, W. B., and Morales, M. M. (2002). Aldosterone and high-NaCl diet modulate ClC-2 chloride channel gene expression in rat kidney. Pflügers Arch. 444, 193-201. doi: 10.1007/s00424-002-0788-y
    • (2002) Pflügers Arch , vol.444 , pp. 193-201
    • Ornellas, D.S.1    Nascimento, D.S.2    Christoph, D.H.3    Guggino, W.B.4    Morales, M.M.5
  • 101
    • 4344666270 scopus 로고    scopus 로고
    • Molecular determinants of differential pore blocking of kidney CLC-K chloride channels
    • Picollo, A., Liantonio, A., Didonna, M. P., Elia, L., Camerino, D. C., and Pusch, M. (2004). Molecular determinants of differential pore blocking of kidney CLC-K chloride channels. EMBO Rep. 5, 584-589. doi: 10.1038/sj.embor.7400169
    • (2004) EMBO Rep , vol.5 , pp. 584-589
    • Picollo, A.1    Liantonio, A.2    Didonna, M.P.3    Elia, L.4    Camerino, D.C.5    Pusch, M.6
  • 102
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo, A., and Pusch, M. (2005). Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436, 420-423. doi: 10.1038/nature03720
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 103
    • 84860739823 scopus 로고    scopus 로고
    • Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H+/Cl- exchanger
    • Picollo, A., Xu, Y., Johner, N., Bernèche, S., and Accardi, A. (2012). Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H+/Cl- exchanger. Nat. Struct. Mol. Biol. 19, 525-531. doi: 10.1038/nsmb.2277
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 525-531
    • Picollo, A.1    Xu, Y.2    Johner, N.3    Bernèche, S.4    Accardi, A.5
  • 104
    • 0028040145 scopus 로고
    • Low single channel conductance of the major skeletal muscle chloride channel, ClC-1
    • Pusch, M., Steinmeyer, K., and Jentsch, T. J. (1994). Low single channel conductance of the major skeletal muscle chloride channel, ClC-1. Biophys. J. 66, 149-152. doi: 10.1016/S0006-3495(94)80753-2
    • (1994) Biophys. J , vol.66 , pp. 149-152
    • Pusch, M.1    Steinmeyer, K.2    Jentsch, T.J.3
  • 105
    • 0029559938 scopus 로고
    • Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel
    • Pusch, M., Steinmeyer, K., Koch, M. C., and Jentsch, T. J. (1995). Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel. Neuron 15, 1455-1463. doi: 10.1016/0896-6273(95)90023-3
    • (1995) Neuron , vol.15 , pp. 1455-1463
    • Pusch, M.1    Steinmeyer, K.2    Koch, M.C.3    Jentsch, T.J.4
  • 106
    • 80155123631 scopus 로고    scopus 로고
    • ClC-2 channels regulate neuronal excitability, not intracellular chloride levels
    • Ratté, S., and Prescott, S. A. (2011). ClC-2 channels regulate neuronal excitability, not intracellular chloride levels. J. Neurosci. 31, 15838-15843. doi: 10.1523/JNEUROSCI.2748-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 15838-15843
    • Ratté, S.1    Prescott, S.A.2
  • 107
    • 0032813687 scopus 로고    scopus 로고
    • A missense mutation in canine ClC-1 causes recessive myotonia congenita in the dog
    • Rhodes, T. H., Vite, C. H., Giger, U., Patterson, D. F., Fahlke, Ch., and George, A. L. Jr. (1999). A missense mutation in canine ClC-1 causes recessive myotonia congenita in the dog. FEBS Lett. 456, 54-58. doi: 10.1016/S0014-5793(99)00926-6
    • (1999) FEBS Lett , vol.456 , pp. 54-58
    • Rhodes, T.H.1    Vite, C.H.2    Giger, U.3    Patterson, D.F.4    Fahlke, C.5    George Jr., A.L.6
  • 108
    • 68249121051 scopus 로고    scopus 로고
    • Molecular basis of DFNB73: mutations of BSND can cause nonsyndromic deafness or bartter syndrome
    • Riazuddin, S., Anwar, S., Fischer, M., Ahmed, Z. M., Khan, S. Y., Janssen, A. G. H., et al. (2009). Molecular basis of DFNB73: mutations of BSND can cause nonsyndromic deafness or bartter syndrome. Am. J. Hum. Genet. 85, 273-280. doi: 10.1016/j.ajhg.2009.07.003
    • (2009) Am. J. Hum. Genet , vol.85 , pp. 273-280
    • Riazuddin, S.1    Anwar, S.2    Fischer, M.3    Ahmed, Z.M.4    Khan, S.Y.5    Janssen, A.G.H.6
  • 109
    • 84870478532 scopus 로고    scopus 로고
    • Dominantly inherited myotonia congenita resulting from a mutation that increases open probability of the muscle chloride channel CLC-1
    • Richman, D. P., Yu, Y., Lee, T.-T., Tseng, P.-Y., Yu, W.-P., Maselli, R. A., et al. (2012). Dominantly inherited myotonia congenita resulting from a mutation that increases open probability of the muscle chloride channel CLC-1. Neuromolecular Med. 14, 328-337. doi: 10.1007/s12017-012-8190-1
    • (2012) Neuromolecular Med , vol.14 , pp. 328-337
    • Richman, D.P.1    Yu, Y.2    Lee, T.-T.3    Tseng, P.-Y.4    Yu, W.-P.5    Maselli, R.A.6
  • 110
    • 78650171241 scopus 로고    scopus 로고
    • Design, function and structure of a monomeric ClC transporter
    • Robertson, J. L., Kolmakova-Partensky, L., and Miller, C. (2010). Design, function and structure of a monomeric ClC transporter. Nature 468, 844-847. doi: 10.1038/nature09556
    • (2010) Nature , vol.468 , pp. 844-847
    • Robertson, J.L.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 111
    • 0031750188 scopus 로고    scopus 로고
    • Permeation and Block of the Skeletal Muscle Chloride Channel, ClC-1, by Foreign Anions
    • Rychkov, G. Y., Pusch, M., Roberts, M. L., Jentsch, T. J., and Bretag, A. H. (1998). Permeation and Block of the Skeletal Muscle Chloride Channel, ClC-1, by Foreign Anions. J. Gen. Physiol. 111, 653-665. doi: 10.1085/jgp.111.5.653
    • (1998) J. Gen. Physiol. , vol.111 , pp. 653-665
    • Rychkov, G.Y.1    Pusch, M.2    Roberts, M.L.3    Jentsch, T.J.4    Bretag, A.H.5
  • 112
    • 61649116159 scopus 로고    scopus 로고
    • Two novel CLCN2 mutations accelerating chloride channel deactivation are associated with idiopathic generalized epilepsy
    • Saint-Martin, C., Gauvain, G., Teodorescu, G., Gourfinkel-An, I., Fedirko, E., Weber, Y. G., et al. (2009). Two novel CLCN2 mutations accelerating chloride channel deactivation are associated with idiopathic generalized epilepsy. Hum. Mutat. 30, 397-405. doi: 10.1002/humu.20876
    • (2009) Hum. Mutat. , vol.30 , pp. 397-405
    • Saint-Martin, C.1    Gauvain, G.2    Teodorescu, G.3    Gourfinkel-An, I.4    Fedirko, E.5    Weber, Y.G.6
  • 113
    • 0032921415 scopus 로고    scopus 로고
    • The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia
    • Saviane, C., Conti, F., and Pusch, M. (1999). The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia. J. Gen. Physiol. 113, 457-468. doi: 10.1085/jgp.113.3.457
    • (1999) J. Gen. Physiol. , vol.113 , pp. 457-468
    • Saviane, C.1    Conti, F.2    Pusch, M.3
  • 114
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel, O., Zdebik, A. A., Lourdel, S., and Jentsch, T. J. (2005). Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436, 424-427. doi: 10.1038/nature03860
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 115
    • 1642366722 scopus 로고    scopus 로고
    • Salt wasting and deafness resulting from mutations in two chloride channels
    • Schlingmann, K. P., Konrad, M., Jeck, N., Waldegger, P., Reinalter, S. C., Holder, M., et al. (2004). Salt wasting and deafness resulting from mutations in two chloride channels. N Engl. J. Med. 350, 1314-1319. doi: 10.1056/NEJMoa032843
    • (2004) N Engl. J. Med. , vol.350 , pp. 1314-1319
    • Schlingmann, K.P.1    Konrad, M.2    Jeck, N.3    Waldegger, P.4    Reinalter, S.C.5    Holder, M.6
  • 117
    • 0032584074 scopus 로고    scopus 로고
    • Analysis of ClC-2 channels as an alternative pathway for chloride conduction in cystic fibrosis airway cells
    • Schwiebert, E. M., Cid-Soto, L. P., Stafford, D., Carter, M., Blaisdell, C. J., Zeitlin, P. L., et al. (1998). Analysis of ClC-2 channels as an alternative pathway for chloride conduction in cystic fibrosis airway cells. Proc. Natl. Acad. Sci. U.S.A. 95, 3879-3884. doi: 10.1073/pnas.95.7.3879
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3879-3884
    • Schwiebert, E.M.1    Cid-Soto, L.P.2    Stafford, D.3    Carter, M.4    Blaisdell, C.J.5    Zeitlin, P.L.6
  • 118
    • 0019229699 scopus 로고
    • The variance of sodium current fluctuations at the node of Ranvier
    • Sigworth, F. J. (1980). The variance of sodium current fluctuations at the node of Ranvier. J. Physiol. 307, 97-129.
    • (1980) J. Physiol. , vol.307 , pp. 97-129
    • Sigworth, F.J.1
  • 119
    • 0034722038 scopus 로고    scopus 로고
    • Distribution of chloride channel-2-immunoreactive neuronal and astrocytic processes in the hippocampus
    • Sìk, A., Smith, R. L., and Freund, T. F. (2000). Distribution of chloride channel-2-immunoreactive neuronal and astrocytic processes in the hippocampus. Neuroscience 101, 51-65. doi: 10.1016/S0306-4522(00)00360-2
    • (2000) Neuroscience , vol.101 , pp. 51-65
    • Sìk, A.1    Smith, R.L.2    Freund, T.F.3
  • 120
    • 63849297175 scopus 로고    scopus 로고
    • CLCNKB-T481S and essential hypertension in a Ghanaian population
    • Sile, S., Velez, D. R., Gillani, N. B., Narsia, T., Moore, J. H., George, A. L., et al. (2009). CLCNKB-T481S and essential hypertension in a Ghanaian population. J. Hypertens. 27, 298-304. doi: 10.1097/HJH.0b013e3283140c9e
    • (2009) J. Hypertens. , vol.27 , pp. 298-304
    • Sile, S.1    Velez, D.R.2    Gillani, N.B.3    Narsia, T.4    Moore, J.H.5    George, A.L.6
  • 121
    • 16944366243 scopus 로고    scopus 로고
    • Mutations in the chloride channel gene, CLCNKB, cause Bartter's syndrome type III
    • Simon, D. B., Bindra, R. S., Mansfield, T. A., Nelson-Williams, C., Mendonca, E., Stone, R., et al. (1997). Mutations in the chloride channel gene, CLCNKB, cause Bartter's syndrome type III. Nat. Genet. 17, 171-178. doi: 10.1038/ng1097-171
    • (1997) Nat. Genet , vol.17 , pp. 171-178
    • Simon, D.B.1    Bindra, R.S.2    Mansfield, T.A.3    Nelson-Williams, C.4    Mendonca, E.5    Stone, R.6
  • 122
    • 0028133253 scopus 로고
    • The role of an inwardly rectifying chloride conductance in postsynaptic inhibition
    • Staley, K. (1994). The role of an inwardly rectifying chloride conductance in postsynaptic inhibition. J. Neurophysiol. 72, 273-284.
    • (1994) J. Neurophysiol , vol.72 , pp. 273-284
    • Staley, K.1
  • 123
    • 0030222772 scopus 로고    scopus 로고
    • Alteration of GABAA receptor function following gene transfer of the CLC-2 chloride channel
    • Staley, K., Smith, R., Schaack, J., Wilcox, C., and Jentsch, T. J. (1996). Alteration of GABAA receptor function following gene transfer of the CLC-2 chloride channel. Neuron 17, 543-551. doi: 10.1016/S0896-6273(00)80186-5
    • (1996) Neuron , vol.17 , pp. 543-551
    • Staley, K.1    Smith, R.2    Schaack, J.3    Wilcox, C.4    Jentsch, T.J.5
  • 124
    • 0026039594 scopus 로고
    • Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel
    • Steinmeyer, K., Ortland, C., and Jentsch, T. J. (1991). Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel. Nature 354, 301-304. doi: 10.1038/354301a0
    • (1991) Nature , vol.354 , pp. 301-304
    • Steinmeyer, K.1    Ortland, C.2    Jentsch, T.J.3
  • 125
    • 84912011877 scopus 로고    scopus 로고
    • ClC-1 and ClC-2 form hetero-dimeric channels with novel protopore functions
    • Stölting, G., Fischer, M., and Fahlke, Ch. (2014). ClC-1 and ClC-2 form hetero-dimeric channels with novel protopore functions. Pflugers Arch. 1-14. doi: 10.1007/s00424-014-1490-6
    • (2014) Pflugers Arch , pp. 1-14
    • Stölting, G.1    Fischer, M.2    Fahlke, C.3
  • 127
    • 34548569398 scopus 로고    scopus 로고
    • Barttin binds to the outer lateral surface of the ClC-K2 chloride channel
    • Tajima, M., Hayama, A., Rai, T., Sasaki, S., and Uchida, S. (2007). Barttin binds to the outer lateral surface of the ClC-K2 chloride channel. Biochem. Biophys. Res. Commun. 362, 858-864. doi: 10.1016/j.bbrc.2007.08.097
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 858-864
    • Tajima, M.1    Hayama, A.2    Rai, T.3    Sasaki, S.4    Uchida, S.5
  • 128
    • 0026522116 scopus 로고
    • A chloride channel widely expressed in epithelial and non-epithelial cells
    • Thiemann, A., Gründer, S., Pusch, M., and Jentsch, T. J. (1992). A chloride channel widely expressed in epithelial and non-epithelial cells. Nature 356, 57-60. doi: 10.1038/356057a0
    • (1992) Nature , vol.356 , pp. 57-60
    • Thiemann, A.1    Gründer, S.2    Pusch, M.3    Jentsch, T.J.4
  • 129
    • 0030851745 scopus 로고    scopus 로고
    • Localization and induction by dehydration of ClC-K chloride channels in the rat kidney
    • Vandewalle, A., Cluzeaud, F., Bens, M., Kieferle, S., Steinmeyer, K., and Jentsch, T. J. (1997). Localization and induction by dehydration of ClC-K chloride channels in the rat kidney. Am. J. Physiol. 272, F678-F688.
    • (1997) Am. J. Physiol. , vol.272 , pp. F678-F688
    • Vandewalle, A.1    Cluzeaud, F.2    Bens, M.3    Kieferle, S.4    Steinmeyer, K.5    Jentsch, T.J.6
  • 130
    • 0036452353 scopus 로고    scopus 로고
    • Barttin increases surface expression and changes current properties of ClC-K channels
    • Waldegger, S., Jeck, N., Barth, P., Peters, M., Vitzthum, H., Wolf, K., et al. (2002). Barttin increases surface expression and changes current properties of ClC-K channels. Pflugers Arch. 444, 411-418. doi: 10.1007/s00424-002-0819-8
    • (2002) Pflugers Arch , vol.444 , pp. 411-418
    • Waldegger, S.1    Jeck, N.2    Barth, P.3    Peters, M.4    Vitzthum, H.5    Wolf, K.6
  • 131
    • 0036759083 scopus 로고    scopus 로고
    • The myotonia congenita mutation A331T confers a novel hyperpolarization-activated gate to the muscle chloride channel ClC-1
    • Warnstedt, M., Sun, C., Poser, B., Escriva, M. J., Tranebjaerg, L., Torbergsen, T., et al. (2002). The myotonia congenita mutation A331T confers a novel hyperpolarization-activated gate to the muscle chloride channel ClC-1. J. Neurosci. 22, 7462-7470.
    • (2002) J. Neurosci , vol.22 , pp. 7462-7470
    • Warnstedt, M.1    Sun, C.2    Poser, B.3    Escriva, M.J.4    Tranebjaerg, L.5    Torbergsen, T.6
  • 132
    • 84864302396 scopus 로고    scopus 로고
    • Disease-causing mutations C277R and C277Y modify gating of human ClC-1 chloride channels in myotonia congenita
    • Weinberger, S., Wojciechowski, D., Sternberg, D., Lehmann-Horn, F., Jurkat-Rott, K., Becher, T., et al. (2012). Disease-causing mutations C277R and C277Y modify gating of human ClC-1 chloride channels in myotonia congenita. J. Physiol. 590, 3449-3464. doi: 10.1113/jphysiol.2012.232785
    • (2012) J. Physiol , vol.590 , pp. 3449-3464
    • Weinberger, S.1    Wojciechowski, D.2    Sternberg, D.3    Lehmann-Horn, F.4    Jurkat-Rott, K.5    Becher, T.6
  • 133
    • 0035951822 scopus 로고    scopus 로고
    • Pores formed by single subunits in mixed dimers of different CLC chloride channels
    • Weinreich, F., and Jentsch, T. J. (2001). Pores formed by single subunits in mixed dimers of different CLC chloride channels. J. Biol. Chem. 276, 2347-2353. doi: 10.1074/jbc. M005733200
    • (2001) J. Biol. Chem , vol.276 , pp. 2347-2353
    • Weinreich, F.1    Jentsch, T.J.2
  • 134
    • 77649119477 scopus 로고    scopus 로고
    • A mathematical model of rat ascending Henle limb. III. Tubular function
    • Weinstein, A. M. (2010). A mathematical model of rat ascending Henle limb. III. Tubular function. Am. J. Physiol. Ren. Physiol. 298, F543-F556. doi: 10.1152/ajprenal.00232.2009
    • (2010) Am. J. Physiol. Ren. Physiol , vol.298 , pp. F543-F556
    • Weinstein, A.M.1
  • 135
    • 0030914684 scopus 로고    scopus 로고
    • Identification of functionally important regions of the muscular chloride channel ClC-1 by analysis of recessive and dominant myotonic mutations
    • Wollnik, B., Kubisch, C., Steinmeyer, K., and Pusch, M. (1997). Identification of functionally important regions of the muscular chloride channel ClC-1 by analysis of recessive and dominant myotonic mutations. Hum. Mol. Genet. 6, 805-811. doi: 10.1093/hmg/6.5.805
    • (1997) Hum. Mol. Genet , vol.6 , pp. 805-811
    • Wollnik, B.1    Kubisch, C.2    Steinmeyer, K.3    Pusch, M.4
  • 136
    • 0036846792 scopus 로고    scopus 로고
    • Novel CLCN1 mutations with unique clinical and electrophysiological consequences
    • Wu, F.-F., Ryan, A., Devaney, J., Warnstedt, M., Korade-Mirnics, Z., Poser, B., et al. (2002). Novel CLCN1 mutations with unique clinical and electrophysiological consequences. Brain 125, 2392-2407. doi: 10.1093/brain/awf246
    • (2002) Brain , vol.125 , pp. 2392-2407
    • Wu, F.-F.1    Ryan, A.2    Devaney, J.3    Warnstedt, M.4    Korade-Mirnics, Z.5    Poser, B.6
  • 137
    • 2542466643 scopus 로고    scopus 로고
    • Additional disruption of the ClC-2 Cl- channel does not exacerbate the cystic fibrosis phenotype of cystic fibrosis transmembrane conductance regulator mouse models
    • Zdebik, A. A., Cuffe, J. E., Bertog, M., Korbmacher, C., and Jentsch, T. J. (2004). Additional disruption of the ClC-2 Cl- channel does not exacerbate the cystic fibrosis phenotype of cystic fibrosis transmembrane conductance regulator mouse models. J. Biol. Chem. 279, 22276-22283. doi: 10.1074/jbc. M309899200
    • (2004) J. Biol. Chem , vol.279 , pp. 22276-22283
    • Zdebik, A.A.1    Cuffe, J.E.2    Bertog, M.3    Korbmacher, C.4    Jentsch, T.J.5
  • 138
    • 1642524953 scopus 로고    scopus 로고
    • The voltage-dependent ClC-2 chloride channel has a dual gating mechanism
    • Zúñiga, L., Niemeyer, M. I., Varela, D., Catalán, M., Cid, L. P., and Sepúlveda, F. V. (2004). The voltage-dependent ClC-2 chloride channel has a dual gating mechanism. J. Physiol. 555, 671-682. doi: 10.1113/jphysiol.2003.060046
    • (2004) J. Physiol , vol.555 , pp. 671-682
    • Zúñiga, L.1    Niemeyer, M.I.2    Varela, D.3    Catalán, M.4    Cid, L.P.5    Sepúlveda, F.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.