메뉴 건너뛰기




Volumn 63, Issue 1, 2006, Pages 12-24

Diversity of Cl- channels

Author keywords

Bestrophin; Ca2+ activation; CFTR; ClC; Knockout mouse; Pharmacology; Tweety; Volume regulation

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; ALKANOIC ACID; AMINOBENZOIC ACID DERIVATIVE; ANTHRACENE DERIVATIVE; CHLORIDE CHANNEL; FENAMIC ACID DERIVATIVE; FLUOXETINE; GLIBENCLAMIDE; MACROLIDE; MEFLOQUINE; MEMBRANE PROTEIN; SCORPION VENOM; STILBENEDISULFONIC ACID; SULFONYLUREA; SURAMIN; TAMOXIFEN; TOLBUTAMIDE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 30844450119     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5336-4     Document Type: Review
Times cited : (104)

References (133)
  • 1
    • 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
    • (1990) Nature , vol.348 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 2
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • Jentsch T. J., Stein V., Weinreich F. and Zdebik A. A. (2002) Molecular structure and physiological function of chloride channels. Physiol. Rev. 82: 503-568
    • (2002) Physiol. Rev. , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4
  • 3
    • 17744380220 scopus 로고    scopus 로고
    • Chloride channels go cell cycling
    • Nilius B. (2001) Chloride channels go cell cycling. J. Physiol. 532: 581
    • (2001) J. Physiol. , vol.532 , pp. 581
    • Nilius, B.1
  • 4
    • 0037318653 scopus 로고    scopus 로고
    • Amazing chloride channels: An overview
    • Nilius B. and Droogmans G. (2003) Amazing chloride channels: an overview. Acta Physiol. Scand. 177: 119-147
    • (2003) Acta Physiol. Scand. , vol.177 , pp. 119-147
    • Nilius, B.1    Droogmans, G.2
  • 5
    • 35448953443 scopus 로고    scopus 로고
    • Calcium activated chloride channels in vascular endothelial cells
    • Fuller K. (ed.), Academic Press, New York
    • Nilius B. and Droogmans G. (2002) Calcium activated chloride channels in vascular endothelial cells. In: Ca2+-activated Cl channels, pp. 327-344, Fuller K. (ed.), Academic Press, New York
    • (2002) Ca2+-activated Cl Channels , pp. 327-344
    • Nilius, B.1    Droogmans, G.2
  • 7
    • 0032514480 scopus 로고    scopus 로고
    • Pore stoichiometry of a voltage-gated chloride channel
    • Fahlke C., Rhodes T. H., Desai R. R. and George A. L. Jr. (1998) Pore stoichiometry of a voltage-gated chloride channel. Nature 394: 687-690
    • (1998) Nature , vol.394 , pp. 687-690
    • Fahlke, C.1    Rhodes, T.H.2    Desai, R.R.3    George Jr., A.L.4
  • 8
    • 0033781187 scopus 로고    scopus 로고
    • Cysteine modification of a putative pore residue in ClC-0: Implication for the pore stoichiometry of ClC chloride channels
    • Lin C. W. and Chen T. Y. (2000) Cysteine modification of a putative pore residue in ClC-0: implication for the pore stoichiometry of ClC chloride channels. J. Gen. Physiol. 116: 535-546
    • (2000) J. Gen. Physiol. , vol.116 , pp. 535-546
    • Lin, C.W.1    Chen, T.Y.2
  • 9
    • 15544388091 scopus 로고    scopus 로고
    • Structure and function of ClC channels
    • Chen T. Y. (2005) Structure and function of ClC channels. Annu. Rev. Physiol. 67: 809-839
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 809-839
    • Chen, T.Y.1
  • 10
    • 0028980536 scopus 로고
    • CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP
    • Schwiebert E. M., Egan M. E., Hwang T. H., Fulmer S. B., Alien S. S., Cutting G. R. et al. (1995) CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP. Cell 81: 1063-1073
    • (1995) Cell , vol.81 , pp. 1063-1073
    • Schwiebert, E.M.1    Egan, M.E.2    Hwang, T.H.3    Fulmer, S.B.4    Alien, S.S.5    Cutting, G.R.6
  • 11
    • 0037122768 scopus 로고    scopus 로고
    • Chloride channels are different
    • Jentsch T. J. (2002) Chloride channels are different. Nature 415: 276-277
    • (2002) Nature , vol.415 , pp. 276-277
    • Jentsch, T.J.1
  • 12
    • 0033610899 scopus 로고    scopus 로고
    • Molecular and functional characterization of a calcium-sensitive chloride channel from mouse lung
    • Gandhi R., Elble R. C., Gruber A. D., Schreur K. D., Ji H. L., Fuller C. M. et al. (1998) Molecular and functional characterization of a calcium-sensitive chloride channel from mouse lung. J. Biol. Chem. 273: 32096-32101
    • (1998) J. Biol. Chem. , vol.273 , pp. 32096-32101
    • Gandhi, R.1    Elble, R.C.2    Gruber, A.D.3    Schreur, K.D.4    Ji, H.L.5    Fuller, C.M.6
  • 14
    • 0037133670 scopus 로고    scopus 로고
    • The vitelliform macular dystrophy protein defines a new family of chloride channels
    • USA
    • Sun H., Tsunenari T., Yau K. W. and Nathans J. (2000) The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc. Natl. Acad. Sci. USA 99: 4008-4013
    • (2000) Proc. Natl. Acad. Sci. , vol.99 , pp. 4008-4013
    • Sun, H.1    Tsunenari, T.2    Yau, K.W.3    Nathans, J.4
  • 15
    • 2542495760 scopus 로고    scopus 로고
    • A novel Cl channel related to Drosophila flightless locus
    • Suzuki M. and Mizuno A. (2004) A novel Cl channel related to Drosophila flightless locus. J. Biol. Chem 279: 22461-22468
    • (2004) J. Biol. Chem , vol.279 , pp. 22461-22468
    • Suzuki, M.1    Mizuno, A.2
  • 17
    • 0032189020 scopus 로고    scopus 로고
    • Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel
    • Wadiche J. I. and Kavanaugh M. P. (1998) Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel. J. Neurosci. 18: 7650-7661
    • (1998) J. Neurosci. , vol.18 , pp. 7650-7661
    • Wadiche, J.I.1    Kavanaugh, M.P.2
  • 18
    • 0033547240 scopus 로고    scopus 로고
    • Rapid gating and anion permeability of an intracellular aquaporin
    • Yasui M., Hazama A., Kwon T. H., Nielsen S., Guggino W. B. and Agre P. (1999) Rapid gating and anion permeability of an intracellular aquaporin. Nature 402: 184-187
    • (1999) Nature , vol.402 , pp. 184-187
    • Yasui, M.1    Hazama, A.2    Kwon, T.H.3    Nielsen, S.4    Guggino, W.B.5    Agre, P.6
  • 19
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å 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 Å reveals the molecular basis of anion selectivity. Nature 415: 287-294
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 21
    • 0026701267 scopus 로고
    • Synthetic peptides and proteins as models for pore-forming structure of channel proteins
    • Grove A., Iwamoto T., Montal M. S., Tomich J. M. and Montal M. (1992) Synthetic peptides and proteins as models for pore-forming structure of channel proteins. Methods Enzymol. 207: 510-525
    • (1992) Methods Enzymol. , vol.207 , pp. 510-525
    • Grove, A.1    Iwamoto, T.2    Montal, M.S.3    Tomich, J.M.4    Montal, M.5
  • 22
    • 0027403316 scopus 로고
    • Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
    • Montal M. O., Iwamoto T., Tomich J. M. and Montal M. (1993) Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor. FEBS Lett. 320: 261-266
    • (1993) FEBS Lett. , vol.320 , pp. 261-266
    • Montal, M.O.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 23
    • 0027209828 scopus 로고
    • Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. I. Transmembrane segment M2 of the nicotinic cholinergic receptor channel is a key pore-lining structure
    • Montal O. M., Buhler L. K., Iwamoto T., Tomich J. M. and Montal M. (1993) Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. I. Transmembrane segment M2 of the nicotinic cholinergic receptor channel is a key pore-lining structure. J. Biol. Chem. 268: 14601-14607
    • (1993) J. Biol. Chem. , vol.268 , pp. 14601-14607
    • Montal, O.M.1    Buhler, L.K.2    Iwamoto, T.3    Tomich, J.M.4    Montal, M.5
  • 24
    • 30844451133 scopus 로고    scopus 로고
    • A
    • Conley E. and Brammer W. (eds.), Academic Press, London
    • A. In: Ion Channel Factsbook vol. 1, pp. 293-365, Conley E. and Brammer W. (eds.), Academic Press, London
    • (1996) Ion Channel Factsbook , vol.1 , pp. 293-365
    • Conley, E.1
  • 25
    • 0027509409 scopus 로고
    • GABA receptors, granule cells and genes
    • Farrant M. and Cull-Candy S. (1993) GABA receptors, granule cells and genes. Nature 361: 302-303
    • (1993) Nature , vol.361 , pp. 302-303
    • Farrant, M.1    Cull-Candy, S.2
  • 26
    • 30844474096 scopus 로고    scopus 로고
    • Cl glycine
    • Academic Press, London
    • Conley E. (1996) Cl glycine. In: Ion Channel Factsbook, vol. 1, pp. 367-399, Academic Press, London
    • (1996) Ion Channel Factsbook , vol.1 , pp. 367-399
    • Conley, E.1
  • 27
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion
    • Pusch M., Ludewig U., Rehfeldt A. and Jentsch T. J. (1995) Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion. Nature 373: 527-531
    • (1995) Nature , vol.373 , pp. 527-531
    • Pusch, M.1    Ludewig, U.2    Rehfeldt, A.3    Jentsch, T.J.4
  • 28
    • 0343812098 scopus 로고    scopus 로고
    • Chloride channels: An emerging molecular picture
    • Jentsch T. J. and Gunther W.(1997) Chloride channels: an emerging molecular picture. Bioessays 119:117-126
    • (1997) Bioessays , vol.119 , pp. 117-126
    • Jentsch, T.J.1    Gunther, W.2
  • 30
    • 0031596021 scopus 로고    scopus 로고
    • ClC-1 chloride channel mutations in myotonia congenita: Variable penetrance of mutations shifting the voltage dependence
    • Kubisch C., Schmidt-Rose T., Fontaine B., Bretag A. H. and Jentsch T. J. (1998) ClC-1 chloride channel mutations in myotonia congenita: variable penetrance of mutations shifting the voltage dependence. Hum. Mol. Genet. 7: 1753-1760
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1753-1760
    • Kubisch, C.1    Schmidt-Rose, T.2    Fontaine, B.3    Bretag, A.H.4    Jentsch, T.J.5
  • 31
    • 0026522116 scopus 로고
    • A chloride channel widely expressed in epithelial and non-epithelial cells
    • Thiemann A., Grunder S., Pusch M. and Jentsch T. J. (1992) A chloride channel widely expressed in epithelial and non-epithelial cells. Nature. 356: 57-60
    • (1992) Nature , vol.356 , pp. 57-60
    • Thiemann, A.1    Grunder, S.2    Pusch, M.3    Jentsch, T.J.4
  • 32
    • 0027051182 scopus 로고
    • Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume
    • Grunder 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
    • (1992) Nature , vol.360 , pp. 759-762
    • Grunder, S.1    Thiemann, A.2    Pusch, M.3    Jentsch, T.J.4
  • 33
    • 0028133253 scopus 로고
    • The role of an inwardly rectifying chloride conductance in postsynaptic inhibition
    • Stanley K. The role of an inwardly rectifying chloride conductance in postsynaptic inhibition. (1994) J. Neurophysiol. 72: 273-284
    • (1994) J. Neurophysiol. , vol.72 , pp. 273-284
    • Stanley, K.1
  • 34
    • 0027383197 scopus 로고
    • - concentration in the intralobular duct cells of mouse mandibular glands
    • - concentration in the intralobular duct cells of mouse mandibular glands. J. Membr. Biol. 135: 289-295
    • (1993) J. Membr. Biol. , vol.135 , pp. 289-295
    • Dinudom, A.1    Young, J.A.2    Cook, D.I.3
  • 35
    • 0029012848 scopus 로고
    • Differential expression of an inwardly rectifying chloride conductance in rat brain neurons: A potential mechanism for cell-specific modulation of postsynaptic inhibition
    • Smith R. L., Clayton G. H., Wilcox C. L., Escudero K. W. and Staley K. J. (1995) Differential expression of an inwardly rectifying chloride conductance in rat brain neurons: a potential mechanism for cell-specific modulation of postsynaptic inhibition. J. Neurosci. 15: 4057-4067
    • (1995) J. Neurosci. , vol.15 , pp. 4057-4067
    • Smith, R.L.1    Clayton, G.H.2    Wilcox, C.L.3    Escudero, K.W.4    Staley, K.J.5
  • 37
    • 0035868910 scopus 로고    scopus 로고
    • Male germ cells and photoreceptors, both depending 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., Mukhophadhyay A. K. et al. (2001) Male germ cells and photoreceptors, both depending on close cell-cell interactions, degenerate upon ClC-2 Cl-channel disruption. EMBO J. 20: 1289-1299
    • (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    Mukhophadhyay, A.K.6
  • 40
    • 10644262261 scopus 로고    scopus 로고
    • Activation of chloride currents in murine portal vein smooth muscle cells by membrane depolarization involves intracellular calcium release
    • Saleh S. N. and Greenwood I. A. (2005) Activation of chloride currents in murine portal vein smooth muscle cells by membrane depolarization involves intracellular calcium release. Am. J. Physiol. Cell. Physiol. 288: C122-131
    • (2005) Am. J. Physiol. Cell. Physiol. , vol.288
    • Saleh, S.N.1    Greenwood, I.A.2
  • 41
    • 0034687171 scopus 로고    scopus 로고
    • Vasoregulation by the b subunit of the calcium-activated potassium channel
    • Brenner R., Perez G. J., Bonev A. D., Eckman D. M., Kosek J. C., Wiler S. W. et al. (2000) Vasoregulation by the b subunit of the calcium-activated potassium channel. Nature 407: 870-876
    • (2000) Nature , vol.407 , pp. 870-876
    • Brenner, R.1    Perez, G.J.2    Bonev, A.D.3    Eckman, D.M.4    Kosek, J.C.5    Wiler, S.W.6
  • 42
    • 4744369280 scopus 로고    scopus 로고
    • Molecular and functional analyses of two new calcium-activated chloride channel family members from mouse eye and intestine
    • Evans S. R., Thoreson W. B. and Beck C. L. (2004) Molecular and functional analyses of two new calcium-activated chloride channel family members from mouse eye and intestine. J. Biol. Chem. 279: 41792-41800
    • (2004) J. Biol. Chem. , vol.279 , pp. 41792-41800
    • Evans, S.R.1    Thoreson, W.B.2    Beck, C.L.3
  • 43
    • 9444288754 scopus 로고    scopus 로고
    • The CLCA gene locus as a modulator of the gastrointestinal basic defect in cystic fibrosis
    • Ritzka M., Stanke F., Jansen S., Gruber A. D,. Pusch L., Woelfl S. et al. (2004) The CLCA gene locus as a modulator of the gastrointestinal basic defect in cystic fibrosis. Hum. Genet. 115: 483-491
    • (2004) Hum. Genet. , vol.115 , pp. 483-491
    • Ritzka, M.1    Stanke, F.2    Jansen, S.3    Gruber, A.D.4    Pusch, L.5    Woelfl, S.6
  • 44
    • 0037085537 scopus 로고    scopus 로고
    • Comparison of the properties of CLCA1 generated currents and I[Cl(Ca)] in murine portal vein smooth muscle cells
    • Britton F. C., Ohya S., Horowitz B. and Greenwood I. A. (2002) Comparison of the properties of CLCA1 generated currents and I[Cl(Ca)] in murine portal vein smooth muscle cells. J Physiol. 539: 107-117
    • (2002) J Physiol. , vol.539 , pp. 107-117
    • Britton, F.C.1    Ohya, S.2    Horowitz, B.3    Greenwood, I.A.4
  • 45
    • 0033231071 scopus 로고    scopus 로고
    • 2+ activated chloride channel CLCA2
    • 2+ activated chloride channel CLCA2. Cancer Res. 59: 5488-5491
    • (1999) Cancer Res. , vol.59 , pp. 5488-5491
    • Gruber, A.D.1    Pauli, B.U.2
  • 47
    • 0035816533 scopus 로고    scopus 로고
    • The breast cancer beta(4) integrin and endothelial human CLCA2 mediate lung metastasis
    • Ghany A., Cheng H. C., Elble R. C. and Pauli B. U. (2001) The breast cancer beta(4) integrin and endothelial human CLCA2 mediate lung metastasis. J. Biol. Chem. 276: 25438-25446
    • (2001) J. Biol. Chem. , vol.276 , pp. 25438-25446
    • Ghany, A.1    Cheng, H.C.2    Elble, R.C.3    Pauli, B.U.4
  • 48
    • 17344364275 scopus 로고    scopus 로고
    • Identification of the gene responsible for Best macular dystrophy
    • Petrukhin K., Koisti M. J., Bakall B., Li W., Xie G., Marknell T. et al. (1998) Identification of the gene responsible for Best macular dystrophy. Nat. Genet. 19: 241-224
    • (1998) Nat. Genet. , vol.19 , pp. 241-1224
    • Petrukhin, K.1    Koisti, M.J.2    Bakall, B.3    Li, W.4    Xie, G.5    Marknell, T.6
  • 49
    • 0031709885 scopus 로고    scopus 로고
    • Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease)
    • Marquardt A., Stohr H., Passmore L. A., Kramer F., Rivera A. and Weber B. H. (1998) Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease). Hum. Mol. Genet. 7: 1517-1525
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1517-1525
    • Marquardt, A.1    Stohr, H.2    Passmore, L.A.3    Kramer, F.4    Rivera, A.5    Weber, B.H.6
  • 50
    • 0003064472 scopus 로고    scopus 로고
    • Light-induced responses of the retinal pigment epithelium
    • Marmor M. F. and Wolfensberger T. J. (eds.), Oxford University Press, New York
    • Gallemore R. P., Hughes B. A. and Miller S. S. (1998) Light-induced responses of the retinal pigment epithelium. In: The Retinal Pigment Epithelium, Marmor M. F. and Wolfensberger T. J. (eds.), pp. 175-198, Oxford University Press, New York
    • (1998) The Retinal Pigment Epithelium , pp. 175-198
    • Gallemore, R.P.1    Hughes, B.A.2    Miller, S.S.3
  • 52
    • 12744261265 scopus 로고    scopus 로고
    • Volume-sensitivity of the bestrophin family of chloride channels
    • Fischmeister R. and Hartzell H. C. (2005) Volume-sensitivity of the bestrophin family of chloride channels. J. Physiol. 562: 477-491
    • (2005) J. Physiol. , vol.562 , pp. 477-491
    • Fischmeister, R.1    Hartzell, H.C.2
  • 53
    • 0001792851 scopus 로고    scopus 로고
    • VRAC: A multifunctional volume regulated anion channel in vascular endothelium
    • Kozlowski R. (ed.), Isis Medical Media Limited, Oxford
    • Nilius B., Voets T., Eggermont J. and Droogmans G. (1999) VRAC: a multifunctional volume regulated anion channel in vascular endothelium. In: Chloride Channels, Kozlowski R. (ed.), pp. 47-63. Isis Medical Media Limited, Oxford
    • (1999) Chloride Channels , pp. 47-63
    • Nilius, B.1    Voets, T.2    Eggermont, J.3    Droogmans, G.4
  • 54
    • 0030815584 scopus 로고    scopus 로고
    • Volume expansion-sensing outward-rectifier Cl channel: Fresh start to the molecular identity and volume sensor
    • Okada Y. (1997) Volume expansion-sensing outward-rectifier Cl channel: fresh start to the molecular identity and volume sensor. Am. J. Physiol. 273: C755-C789
    • (1997) Am. J. Physiol. , vol.273
    • Okada, Y.1
  • 55
    • 0031801378 scopus 로고    scopus 로고
    • The list of potential volume-sensitive chloride currents continues to swell (and shrink)
    • Clapham D. E. (1998) The list of potential volume-sensitive chloride currents continues to swell (and shrink). J. Physiol. Lond. 111: 623-624
    • (1998) J. Physiol. Lond. , vol.111 , pp. 623-624
    • Clapham, D.E.1
  • 57
    • 0032489679 scopus 로고    scopus 로고
    • The tyrosine kinase p56(lck) mediates activation of swelling-induced chloride channels in lymphocytes
    • Lepple-Wienhues A., Szabo I., Laun T., Kaba N. K., Gulbins E. and Lang F. (1998) The tyrosine kinase p56(lck) mediates activation of swelling-induced chloride channels in lymphocytes. J. Cell. Biol. 141: 281-286
    • (1998) J. Cell. Biol. , vol.141 , pp. 281-286
    • Lepple-Wienhues, A.1    Szabo, I.2    Laun, T.3    Kaba, N.K.4    Gulbins, E.5    Lang, F.6
  • 58
    • 0033118584 scopus 로고    scopus 로고
    • Role of RhoA and Rho kinase in the activation of volume-regulated anion channels in bovine endothelial cells
    • Nilius B., Voets T., Prenen J. Barth H., Aktories K., Kaibuchi K. et al.(1999) Role of RhoA and Rho kinase in the activation of volume-regulated anion channels in bovine endothelial cells. J. Physiol. 516: 67-74
    • (1999) J. Physiol. , vol.516 , pp. 67-74
    • Nilius, B.1    Voets, T.2    Prenen, J.3    Barth, H.4    Aktories, K.5    Kaibuchi, K.6
  • 59
    • 0026536805 scopus 로고
    • Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein
    • Valverde M. A., Diaz M., Sepulveda F. V., Gill D. R., Hyde S. C. and Higgins C. F. (1992) Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein. Nature 355: 830-833
    • (1992) Nature , vol.355 , pp. 830-833
    • Valverde, M.A.1    Diaz, M.2    Sepulveda, F.V.3    Gill, D.R.4    Hyde, S.C.5    Higgins, C.F.6
  • 61
    • 0026536805 scopus 로고
    • Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein
    • Valverde M. A., Diaz M., Sepulveda F. V., Gill D. R., Hyde S. C. and Higgins C. F. (1992) Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein. Nature 355: 830-833
    • (1992) Nature , vol.355 , pp. 830-833
    • Valverde, M.A.1    Diaz, M.2    Sepulveda, F.V.3    Gill, D.R.4    Hyde, S.C.5    Higgins, C.F.6
  • 62
    • 0029816342 scopus 로고    scopus 로고
    • The multidrug resistance P-glycoprotein modulates cell regulatory volume decrease
    • Valverde M. A., Bond T. D., Hardy S. P. Taylor J. C., Higgins C. F., Altamirano J. et al. (1996) The multidrug resistance P-glycoprotein modulates cell regulatory volume decrease. EMBO J. 15: 4460-4468
    • (1996) EMBO J. , vol.15 , pp. 4460-4468
    • Valverde, M.A.1    Bond, T.D.2    Hardy, S.P.3    Taylor, J.C.4    Higgins, C.F.5    Altamirano, J.6
  • 63
    • 0032080214 scopus 로고    scopus 로고
    • pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology
    • Krapivinsky G., Pu W., Wickman K., Krapivinsky L. and Clapham D. E. (1998) pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. J. Biol. Chem. 273: 10811-10814
    • (1998) J. Biol. Chem. , vol.273 , pp. 10811-10814
    • Krapivinsky, G.1    Pu, W.2    Wickman, K.3    Krapivinsky, L.4    Clapham, D.E.5
  • 64
    • 0034724675 scopus 로고    scopus 로고
    • ICln is essential for cellular and early embryonic viability
    • Pu W. T., Wickman K. and Clapham D. E. (2000) ICln is essential for cellular and early embryonic viability. J. Biol. Chem. 275: 12363-12366
    • (2000) J. Biol. Chem. , vol.275 , pp. 12363-12366
    • Pu, W.T.1    Wickman, K.2    Clapham, D.E.3
  • 66
    • 0034680866 scopus 로고    scopus 로고
    • Biophysical properties of ClC-3 differentiate it from swelling-activated chloride channels in Chinese hamster ovary-K1 cells
    • Li X., Shimada K., Showalter L. A. and Weinman S. A. (2000) Biophysical properties of ClC-3 differentiate it from swelling-activated chloride channels in Chinese hamster ovary-K1 cells. J. Biol. Chem. 275: 35994-35998
    • (2000) J. Biol. Chem. , vol.275 , pp. 35994-35998
    • Li, X.1    Shimada, K.2    Showalter, L.A.3    Weinman, S.A.4
  • 67
    • 0035907376 scopus 로고    scopus 로고
    • Human ClC-3 is not the swelling-activated chloride channel involved in cell volume regulation
    • Weylandt K. H., Valverde M. A., Nobles M., Raguz S., Amey J. S., Diaz M. et al. (2001) Human ClC-3 is not the swelling-activated chloride channel involved in cell volume regulation. J. Biol. Chem. 276: 17461-17467
    • (2001) J. Biol. Chem. , vol.276 , pp. 17461-17467
    • Weylandt, K.H.1    Valverde, M.A.2    Nobles, M.3    Raguz, S.4    Amey, J.S.5    Diaz, M.6
  • 68
    • 17744375755 scopus 로고    scopus 로고
    • Disruption of CIC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus
    • Stobrawa S. M., Breiderhoff T., Takamori S., Engel D., Schweizer M., Zdebik A. A. et al. (2001) Disruption of CIC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus. Neuron 29: 185-196
    • (2001) Neuron , vol.29 , pp. 185-196
    • Stobrawa, S.M.1    Breiderhoff, T.2    Takamori, S.3    Engel, D.4    Schweizer, M.5    Zdebik, A.A.6
  • 69
    • 16844370842 scopus 로고    scopus 로고
    • Hyposmotic activation of ICl, swell in rabbit nonpigmented ciliary epithelial cells involves increased ClC-3 trafficking to the plasma membrane
    • Vessey J. P., Shi C., Jollimore C. A., Stevens K. T., Coca-Prados M., Barnes S. et al. (2004) Hyposmotic activation of ICl, swell in rabbit nonpigmented ciliary epithelial cells involves increased ClC-3 trafficking to the plasma membrane. Biochem. Cell Biol. 82: 708-718
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 708-718
    • Vessey, J.P.1    Shi, C.2    Jollimore, C.A.3    Stevens, K.T.4    Coca-Prados, M.5    Barnes, S.6
  • 70
    • 14844290889 scopus 로고    scopus 로고
    • - concentration through volume-regulated ClC-3 chloride channels in A10 vascular smooth muscle cells
    • - concentration through volume-regulated ClC-3 chloride channels in A10 vascular smooth muscle cells. J. Biol. Chem. 280: 7301-7308
    • (2005) J. Biol. Chem. , vol.280 , pp. 7301-7308
    • Zhou, J.G.1    Ren, J.L.2    Qiu, Q.Y.3    He, H.4    Guan, Y.Y.5
  • 71
    • 2942614762 scopus 로고    scopus 로고
    • AP-3-dependent mechanisms control the targeting of a chloride channel (ClC-3) in neuronal and non-neuronal cells
    • Salazar G., Love R., Styers M. L., Werner E., Peden A., Rodriguez S. et al. (2004) AP-3-dependent mechanisms control the targeting of a chloride channel (ClC-3) in neuronal and non-neuronal cells. J. Biol. Chem. 279: 25430-25439
    • (2004) J. Biol. Chem. , vol.279 , pp. 25430-25439
    • Salazar, G.1    Love, R.2    Styers, M.L.3    Werner, E.4    Peden, A.5    Rodriguez, S.6
  • 72
    • 0013236977 scopus 로고    scopus 로고
    • ClC-3 is a fundamental molecular component of volume-sensitive outwardly rectifying Cl channel and volume regulation in HeLa cells and Xenopus laevis oocytes
    • Hermoso M., Satterwhite C. M. andrade Y., Hidalgo J., Wilson S. M., Horowitz B. et al. (2002) ClC-3 is a fundamental molecular component of volume-sensitive outwardly rectifying Cl channel and volume regulation in HeLa cells and Xenopus laevis oocytes. J. Biol. Chem. 205: 132-200
    • (2002) J. Biol. Chem. , vol.205 , pp. 132-200
    • Hermoso, M.1    Satterwhite, C.M.2    Andrade, Y.3    Hidalgo, J.4    Wilson, S.M.5    Horowitz, B.6
  • 73
    • 0030746892 scopus 로고    scopus 로고
    • A large-conductance chloride channel in pigmented ciliary epithelial cells activated by GTP gamma S
    • Mitchell C. H., Wang L. and Jacob T. J. C. (1997) A large-conductance chloride channel in pigmented ciliary epithelial cells activated by GTP gamma S. J. Membr. Biol. 158: 167-175
    • (1997) J. Membr. Biol. , vol.158 , pp. 167-175
    • Mitchell, C.H.1    Wang, L.2    Jacob, T.J.C.3
  • 74
    • 0035476880 scopus 로고    scopus 로고
    • Okadaic acid-sensitive activation of Maxi Cl channels by triphenylethylene antioestrogens in C1300 mouse neuroblastoma cells
    • Diaz M., Bahamonde M. I., Lock H., Munoz F. J., Hardy S. P., Posas F. et al. (2001) Okadaic acid-sensitive activation of Maxi Cl channels by triphenylethylene antioestrogens in C1300 mouse neuroblastoma cells. J. Physiol. 536: 79-88
    • (2001) J. Physiol. , vol.536 , pp. 79-88
    • Diaz, M.1    Bahamonde, M.I.2    Lock, H.3    Munoz, F.J.4    Hardy, S.P.5    Posas, F.6
  • 75
    • 0025897101 scopus 로고
    • Blockade of Cl channels by organic and inorganic blockers in vascular smooth muscle cells
    • Kokubun S., Saigusa A. and Tamura T. (1991) Blockade of Cl channels by organic and inorganic blockers in vascular smooth muscle cells. Pflugers Arch. 418: 204-213
    • (1991) Pflugers Arch. , vol.418 , pp. 204-213
    • Kokubun, S.1    Saigusa, A.2    Tamura, T.3
  • 76
    • 0034853407 scopus 로고    scopus 로고
    • Volume-dependent ATP-conductive large-conductance anion channel as a pathway for swelling-induced ATP release
    • Sabirov R. Z., Dutta A. K. and Okada Y. (2001) Volume-dependent ATP-conductive large-conductance anion channel as a pathway for swelling-induced ATP release. J. Gen. Physiol. 118: 251-266
    • (2001) J. Gen. Physiol. , vol.118 , pp. 251-266
    • Sabirov, R.Z.1    Dutta, A.K.2    Okada, Y.3
  • 79
    • 0034662787 scopus 로고    scopus 로고
    • Human and mouse homologues of the Drosophila melanogaster tweety (tty) gene: A novel gene family encoding predicted transmembrane proteins
    • Campbell H. D., Kamei M., Claudianos C., Woollatt E., Sutherland G. R., Suzuki Y. et al. (2000) Human and mouse homologues of the Drosophila melanogaster tweety (tty) gene: a novel gene family encoding predicted transmembrane proteins. Genomics 68: 89-92
    • (2000) Genomics , vol.68 , pp. 89-92
    • Campbell, H.D.1    Kamei, M.2    Claudianos, C.3    Woollatt, E.4    Sutherland, G.R.5    Suzuki, Y.6
  • 80
    • 0035827504 scopus 로고    scopus 로고
    • Identification of a novel chloride channel expressed in the endoplasmic reticulum, Golgi apparatus, and nucleus
    • Nagasawa M., Kanzaki M., Iino Y., Morishita Y. and Kojima I. (2001) Identification of a novel chloride channel expressed in the endoplasmic reticulum, Golgi apparatus, and nucleus. J. Biol. Chem. 276: 20413-20418
    • (2001) J. Biol. Chem. , vol.276 , pp. 20413-20418
    • Nagasawa, M.1    Kanzaki, M.2    Iino, Y.3    Morishita, Y.4    Kojima, I.5
  • 81
    • 0033529578 scopus 로고    scopus 로고
    • Molecular identification of a eukaryotic, stretch-activated nonselective cation channel
    • Kanzaki M., Nagasawa M., Kojima I., Sato C., Naruse K., Sokabe M. et al. (1999) Molecular identification of a eukaryotic, stretch-activated nonselective cation channel. Science 285: 882-886
    • (1999) Science , vol.285 , pp. 882-886
    • Kanzaki, M.1    Nagasawa, M.2    Kojima, I.3    Sato, C.4    Naruse, K.5    Sokabe, M.6
  • 82
    • 15544390386 scopus 로고    scopus 로고
    • Function of chloride channels in the kidney
    • Uchida S. and Sasaki S. (2005) Function of chloride channels in the kidney. Annu. Rev. Physiol. 67: 759-778
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 759-778
    • Uchida, S.1    Sasaki, S.2
  • 83
    • 24144439165 scopus 로고    scopus 로고
    • Chloride transport in the kidney: Lessons from human disease and knockout mice
    • Jentsch T. J. (2005) Chloride transport in the kidney: lessons from human disease and knockout mice. J. Am. Soc. Nephrol. 16: 1549-1561
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 1549-1561
    • Jentsch, T.J.1
  • 85
    • 0024453308 scopus 로고
    • Identification of the cystic fibrosis gene:chromosome walking and jumping
    • Rommens J. M., Iannuzzi M. C., Kerem B., Drumm M. L., Melmer G., Dean M. et al. (1989) Identification of the cystic fibrosis gene:chromosome walking and jumping. Science 245: 1059-1065
    • (1989) Science , vol.245 , pp. 1059-1065
    • Rommens, J.M.1    Iannuzzi, M.C.2    Kerem, B.3    Drumm, M.L.4    Melmer, G.5    Dean, M.6
  • 86
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan J. R., Rommens J. M., Kerem B., Alon N., Rozmahel R., Grzelczak Z. et al. (1989) Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245: 1066-1072
    • (1989) Science , vol.245 , pp. 1066-1072
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.3    Alon, N.4    Rozmahel, R.5    Grzelczak, Z.6
  • 87
    • 0026077676 scopus 로고
    • Identification and regulation of the cystic fibrosis transmembrane conductance regulator-generated chloride channel
    • Berger H. A., Anderson M. P., Gregoryt R. J., Thompson S., Howard P. W., Maurer R. A. et al. (1991) Identification and regulation of the cystic fibrosis transmembrane conductance regulator-generated chloride channel. J. Clin. Invest. 88: 1422-1431
    • (1991) J. Clin. Invest. , vol.88 , pp. 1422-1431
    • Berger, H.A.1    Anderson, M.P.2    Gregoryt, R.J.3    Thompson, S.4    Howard, P.W.5    Maurer, R.A.6
  • 88
    • 0032478144 scopus 로고    scopus 로고
    • Chloride channel and chloride conductance regulator domains of CFTR, the cystic fibrosis transmembrane conductance regulator
    • USA
    • Hallows K. R., Raghuram V., Kemp B. E., Schwiebert E. M., Morales M. M., Lopes A. G. et al. (1998) Chloride channel and chloride conductance regulator domains of CFTR, the cystic fibrosis transmembrane conductance regulator. Proc. Natl. Acad. Sci. USA 95: 2674-2679
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 2674-2679
    • Hallows, K.R.1    Raghuram, V.2    Kemp, B.E.3    Schwiebert, E.M.4    Morales, M.M.5    Lopes, A.G.6
  • 90
    • 0034676433 scopus 로고    scopus 로고
    • ClC-5 Cl-channel disruption impairs endocytosis in a mouse model for Dent's disease
    • Piwon N., Gunther W., Schwake M., Bosl M. R. and Jentsch T. J. (2000) ClC-5 Cl-channel disruption impairs endocytosis in a mouse model for Dent's disease. Nature 408: 369-373
    • (2000) Nature , vol.408 , pp. 369-373
    • Piwon, N.1    Gunther, W.2    Schwake, M.3    Bosl, M.R.4    Jentsch, T.J.5
  • 92
    • 0032493276 scopus 로고    scopus 로고
    • ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells
    • USA
    • GuÈnther W., LuÈchow A., Cluzeaud F., Vandewalle A. and Jentsch T. J. (1998) ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells. Proc. Natl Acad. Sci. USA 95: 8075-8080
    • (1998) Proc. Natl Acad. Sci. , vol.95 , pp. 8075-8080
    • Guènther, W.1    Luèchow, A.2    Cluzeaud, F.3    Vandewalle, A.4    Jentsch, T.J.5
  • 93
    • 0033582543 scopus 로고    scopus 로고
    • An endocytic pathway essential for renal uptake and activation of the steroid 25-(OH) vitamin D3
    • Nykjaer A., Dragun D., Walther D., Vorum H., Jacobsen C., Herz J. et al. (1999) An endocytic pathway essential for renal uptake and activation of the steroid 25-(OH) vitamin D3. Cell 96: 507-515
    • (1999) Cell , vol.96 , pp. 507-515
    • Nykjaer, A.1    Dragun, D.2    Walther, D.3    Vorum, H.4    Jacobsen, C.5    Herz, J.6
  • 94
    • 0038153196 scopus 로고    scopus 로고
    • Loss of chloride channel ClC-5 impairs endocytosis by defective trafficking of megalin and cubilin in kidney proximal tubules
    • USA
    • Christensen E. I., Devuyst O., Dom G., Nielsen R., Van der Smissen P., Verroust P. et al. (2003) Loss of chloride channel ClC-5 impairs endocytosis by defective trafficking of megalin and cubilin in kidney proximal tubules. Proc. Natl. Acad. Sci. USA. 100: 8472-8477
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 8472-8477
    • Christensen, E.I.1    Devuyst, O.2    Dom, G.3    Nielsen, R.4    Van Der Smissen, P.5    Verroust, P.6
  • 95
    • 0035998271 scopus 로고    scopus 로고
    • CLC-3 deficiency leads to phenotypes similar to human neuronal ceroid lipofuscinosis
    • Yoshikawa M., Uchida S., Ezaki J., Rai T., Hayama A., Kobayashi K. et al. (2002) CLC-3 deficiency leads to phenotypes similar to human neuronal ceroid lipofuscinosis. Genes Cells 7: 597-605
    • (2002) Genes Cells , vol.7 , pp. 597-605
    • Yoshikawa, M.1    Uchida, S.2    Ezaki, J.3    Rai, T.4    Hayama, A.5    Kobayashi, K.6
  • 96
    • 20144387287 scopus 로고    scopus 로고
    • Loss of the chloride channel ClC-7 leads to lysosomal storage disease and neurodegeneration
    • Kasper D., Planells-Cases R., Fuhrmann J. C., Scheel O., Zeitz O., Ruether K. et al. (2005) Loss of the chloride channel ClC-7 leads to lysosomal storage disease and neurodegeneration. EMBO J. 24: 1079-1091
    • (2005) EMBO J. , vol.24 , pp. 1079-1091
    • Kasper, D.1    Planells-Cases, R.2    Fuhrmann, J.C.3    Scheel, O.4    Zeitz, O.5    Ruether, K.6
  • 97
    • 0033545980 scopus 로고    scopus 로고
    • Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia
    • USA
    • Yasui M., Kwon T. H., Knepper M. A., Nielsen S. and Agre P. (1999) Aquaporin-6: an intracellular vesicle water channel protein in renal epithelia. Proc. Natl. Acad. Sci. USA. 96: 5808-5813
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 5808-5813
    • Yasui, M.1    Kwon, T.H.2    Knepper, M.A.3    Nielsen, S.4    Agre, P.5
  • 98
    • 1642403597 scopus 로고    scopus 로고
    • Suppression of cell proliferation with induction of p21 by Cl(-) channel blockers in human leukemic cells
    • Jiang B., Hattori N., Liu B., Nakayama Y., Kitagawa K. and Inagaki C. (2004) Suppression of cell proliferation with induction of p21 by Cl(-) channel blockers in human leukemic cells. Eur J Pharmacol. 488: 27-34
    • (2004) Eur J Pharmacol. , vol.488 , pp. 27-34
    • Jiang, B.1    Hattori, N.2    Liu, B.3    Nakayama, Y.4    Kitagawa, K.5    Inagaki, C.6
  • 99
    • 2342637859 scopus 로고    scopus 로고
    • A role of reactive oxygen species in apoptotic activation of volume-sensitive Cl(-) channel
    • USA
    • Shimizu T., Numata T. and Okada Y. (2004) A role of reactive oxygen species in apoptotic activation of volume-sensitive Cl(-) channel. Proc. Natl. Acad. Sci. USA. 101: 6770-6773
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 6770-6773
    • Shimizu, T.1    Numata, T.2    Okada, Y.3
  • 101
    • 0025372566 scopus 로고
    • Flufenamic acid, mefenamic acid and niflumic acid inhibit single nonselective cation channels in the rat exocrine pancreas
    • Gogelein H., Dahlem D., Englert H. C. and Lang H. J. (1990) Flufenamic acid, mefenamic acid and niflumic acid inhibit single nonselective cation channels in the rat exocrine pancreas. FEBS Lett. 268: 79-82
    • (1990) FEBS Lett. , vol.268 , pp. 79-82
    • Gogelein, H.1    Dahlem, D.2    Englert, H.C.3    Lang, H.J.4
  • 102
    • 0036896008 scopus 로고    scopus 로고
    • Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxin-induced intestinal fluid secretion J
    • Ma T., Thiagarajah J. R., Yang H., Sonawane N. D., Folli C., Galietta L. J. V. et al. (2002) Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxin-induced intestinal fluid secretion J. Clin. Invest. 110: 1651-1658
    • (2002) Clin. Invest. , vol.110 , pp. 1651-1658
    • Ma, T.1    Thiagarajah, J.R.2    Yang, H.3    Sonawane, N.D.4    Folli, C.5    Galietta, L.J.V.6
  • 104
    • 0034023894 scopus 로고    scopus 로고
    • Chlorotoxin does not inhibit volume-regulated, calcium-activated and cyclic AMP-activated chloride channels
    • Maertens C., Wei L., Tytgat J., Droogmans G. and Nilius B. (2000) Chlorotoxin does not inhibit volume-regulated, calcium-activated and cyclic AMP-activated chloride channels. Br. J. Pharmacol. 129: 791-801
    • (2000) Br. J. Pharmacol. , vol.129 , pp. 791-801
    • Maertens, C.1    Wei, L.2    Tytgat, J.3    Droogmans, G.4    Nilius, B.5
  • 105
    • 20944442087 scopus 로고    scopus 로고
    • Phenylglycine and sulfonamide correctors of defective DF508 and G551D cystic fibrosis transmembrane conductance regulator chloride-channel gating
    • Pedemonte N., Sonawane N. D., Taddei A., Hu J., Zegarra-Moran O,. Suen Y. F. et al. (2005) Phenylglycine and sulfonamide correctors of defective DF508 and G551D cystic fibrosis transmembrane conductance regulator chloride-channel gating. Mol. Pharmacol. 67: 1797-1807
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1797-1807
    • Pedemonte, N.1    Sonawane, N.D.2    Taddei, A.3    Hu, J.4    Zegarra-Moran, O.5    Suen, Y.F.6
  • 106
    • 0033810904 scopus 로고    scopus 로고
    • Inhibition of volume-regulated and calcium-activated chloride channels by the antimalarial mefloquine
    • Maertens C., Wei L., Droogmans G. and Nilius B. (2000) Inhibition of volume-regulated and calcium-activated chloride channels by the antimalarial mefloquine. J. Pharmacol. Exp. Ther. 295: 29-36
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 29-36
    • Maertens, C.1    Wei, L.2    Droogmans, G.3    Nilius, B.4
  • 107
    • 30844447068 scopus 로고    scopus 로고
    • Suppressive action of erythromycin on cultured tracheal epithelial cell chloride channel activated by interferon-gamma
    • Nakaya Y., Kuzu N., Nakamura Y. and Sone S. (1998) Suppressive action of erythromycin on cultured tracheal epithelial cell chloride channel activated by interferon-gamma. Jpn. J. Antibiot. 51: 152-154
    • (1998) Jpn. J. Antibiot. , vol.51 , pp. 152-154
    • Nakaya, Y.1    Kuzu, N.2    Nakamura, Y.3    Sone, S.4
  • 108
    • 1142310688 scopus 로고    scopus 로고
    • Conduction mechanisms of chloride ions in ClC-type channels
    • Corry B., O'Mara M. and Chung S. H. (2004) Conduction mechanisms of chloride ions in ClC-type channels. Biophys. J. 86: 846-60
    • (2004) Biophys. J. , vol.86 , pp. 846-860
    • Corry, B.1    O'Mara, M.2    Chung, S.H.3
  • 109
    • 3042648417 scopus 로고    scopus 로고
    • Functional and structural conservation of CBS domains from CLC chloride channels
    • Estevez 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
    • (2004) J. Physiol. , vol.557 , pp. 363-378
    • Estevez, R.1    Pusch, M.2    Ferrer-Costa, C.3    Orozco, M.4    Jentsch, T.J.5
  • 110
    • 15544388091 scopus 로고    scopus 로고
    • Structure and function of ClC channels
    • Chen T. Y. (2005) Structure and function of ClC channels. Annu. Rev. Physiol. 67: 809-839
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 809-839
    • Chen, T.Y.1
  • 111
    • 8144222566 scopus 로고    scopus 로고
    • A two-holed story: Structural secrets about ClC proteins become unraveled?
    • Babini E. and Pusch M. (2004) A two-holed story: structural secrets about ClC proteins become unraveled? Physiology. 19: 293-299
    • (2004) Physiology , vol.19 , pp. 293-299
    • Babini, E.1    Pusch, M.2
  • 112
    • 3042648417 scopus 로고    scopus 로고
    • Functional and structural conservation of CBS domains from CLC chloride channels
    • Estevez 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
    • (2004) J. Physiol. , vol.557 , pp. 363-378
    • Estevez, R.1    Pusch, M.2    Ferrer-Costa, C.3    Orozco, M.4    Jentsch, T.J.5
  • 113
    • 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
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 114
    • 15544371839 scopus 로고    scopus 로고
    • Assembly of functional CFTR chloride channels
    • Riordan J. R. (2005) Assembly of functional CFTR chloride channels. Annu. Rev. Physiol. 67: 701-718
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 701-718
    • Riordan, J.R.1
  • 115
    • 0028058184 scopus 로고
    • Identification of an ion channel-forming motif in the primary structure of CFTR, the cystic fibrosis chloride channel
    • USA
    • Montal O. M., Reddy G. L., Iwamoto T., Tomich J. M. and Montal M. (1994) Identification of an ion channel-forming motif in the primary structure of CFTR, the cystic fibrosis chloride channel. Proc. Natl. Acad. Sci. USA. 91: 1495-1499
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 1495-1499
    • Montal, O.M.1    Reddy, G.L.2    Iwamoto, T.3    Tomich, J.M.4    Montal, M.5
  • 116
    • 0037062632 scopus 로고    scopus 로고
    • Distinct structural elements that direct solution aggregation and membrane assembly in the channel-forming peptide M2GlyR
    • Broughman J. R., Shank L. P., Takeguchi W., Schultz B. D., Iwamoto T., Mitchell K. E. et al. (2002) Distinct structural elements that direct solution aggregation and membrane assembly in the channel-forming peptide M2GlyR. Biochemistry 41: 7350-7358
    • (2002) Biochemistry , vol.41 , pp. 7350-7358
    • Broughman, J.R.1    Shank, L.P.2    Takeguchi, W.3    Schultz, B.D.4    Iwamoto, T.5    Mitchell, K.E.6
  • 118
    • 0023162271 scopus 로고
    • Mechanism of anion permeation through channels gated by glycine and gamma-aminobutyric acid in mouse cultured spinal neurones
    • Bormann J., Hamill O. P. and Sakmann B. (1987) Mechanism of anion permeation through channels gated by glycine and gamma-aminobutyric acid in mouse cultured spinal neurones. J. Physiol. 385: 243-286
    • (1987) J. Physiol. , vol.385 , pp. 243-286
    • Bormann, J.1    Hamill, O.P.2    Sakmann, B.3
  • 119
    • 0026077676 scopus 로고
    • Identification and regulation of the cystic fibrosis transmembrane conductance regulator-generated chloride channel
    • Berger H. A., Anderson M. P., Gregory R. J., Thompson S., Howard P. W. Maurer R. A. et al. (1991) Identification and regulation of the cystic fibrosis transmembrane conductance regulator-generated chloride channel. J. Clin. Invest. 88: 1422-1431
    • (1991) J. Clin. Invest. , vol.88 , pp. 1422-1431
    • Berger, H.A.1    Anderson, M.P.2    Gregory, R.J.3    Thompson, S.4    Howard, P.W.5    Maurer, R.A.6
  • 120
    • 0032523938 scopus 로고    scopus 로고
    • Functional expression of p64, an intracellular chloride channel protein
    • Edwards J. C., Tulk B. and Schlesinger P. H. (1998) Functional expression of p64, an intracellular chloride channel protein. J. Membr. Biol. 163: 119-127
    • (1998) J. Membr. Biol. , vol.163 , pp. 119-127
    • Edwards, J.C.1    Tulk, B.2    Schlesinger, P.H.3
  • 121
    • 0034680866 scopus 로고    scopus 로고
    • Biophysical properties of ClC-3 differentiate it from swelling activated chloride channels in Chinese hamster ovary-K1 cells
    • Li X., Shimada, K., Lori A., Showalter L. A. and Weinman S. A. (2000) Biophysical properties of ClC-3 differentiate it from swelling activated chloride channels in Chinese hamster ovary-K1 cells. J. Biol. Chem. 275: 35994-35998
    • (2000) J. Biol. Chem. , vol.275 , pp. 35994-35998
    • Li, X.1    Shimada, K.2    Lori, A.3    Showalter, L.A.4    Weinman, S.A.5
  • 122
    • 0032101645 scopus 로고    scopus 로고
    • Identification of endogenous outward currents in the human embryonic kidney (HEK 293) cell line
    • Zhu G., Zhang Y., Xu H. and Jiang C., (1998) Identification of endogenous outward currents in the human embryonic kidney (HEK 293) cell line. J. Neurosci. Methods 81: 73-83
    • (1998) J. Neurosci. Methods , vol.81 , pp. 73-83
    • Zhu, G.1    Zhang, Y.2    Xu, H.3    Jiang, C.4
  • 124
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and openchannel block
    • McDonough S., Davidson N., Lester H. A. and Mccarty N. A. (1994) Novel pore-lining residues in CFTR that govern permeation and openchannel block. Neuron 13: 623-634
    • (1994) Neuron , vol.13 , pp. 623-634
    • McDonough, S.1    Davidson, N.2    Lester, H.A.3    Mccarty, N.A.4
  • 125
    • 0032168579 scopus 로고    scopus 로고
    • Characterization of the putative chloride channel xClC-5 expressed in Xenopus laevis oocytes and comparison with endogenous chloride currents
    • Schmieder S., Lindenthal S., Banderali U. and Ehrenfeld J. (1998) Characterization of the putative chloride channel xClC-5 expressed in Xenopus laevis oocytes and comparison with endogenous chloride currents. J. Physiol. 511: 379-393
    • (1998) J. Physiol. , vol.511 , pp. 379-393
    • Schmieder, S.1    Lindenthal, S.2    Banderali, U.3    Ehrenfeld, J.4
  • 126
    • 0028365734 scopus 로고
    • Spontaneous transient inward currents and rhythmicity in canine and guinea-pig tracheal smooth muscle cells
    • Janssen L. J. and Sims S. M. (1994) Spontaneous transient inward currents and rhythmicity in canine and guinea-pig tracheal smooth muscle cells. Pflugers Arch. 427: 473-480
    • (1994) Pflugers Arch. , vol.427 , pp. 473-480
    • Janssen, L.J.1    Sims, S.M.2
  • 128
    • 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 J. 5: 584-589
    • (2004) EMBO J. , 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
  • 129
    • 0032944293 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator (CFTR) confers glibenclamide sensitivity to outwardly rectifying chloride channel (ORCC) in Hi-5 insect cells
    • Julien M., Verrier B., Cerutti M., Chappe V., Gole M., Devauchelle G. et al. (1999) Cystic fibrosis transmembrane conductance regulator (CFTR) confers glibenclamide sensitivity to outwardly rectifying chloride channel (ORCC) in Hi-5 insect cells. J. Membr. Biol. 168: 229-239
    • (1999) J. Membr. Biol. , vol.168 , pp. 229-239
    • Julien, M.1    Verrier, B.2    Cerutti, M.3    Chappe, V.4    Gole, M.5    Devauchelle, G.6
  • 131
  • 132
    • 0035144676 scopus 로고    scopus 로고
    • Inhibition of volume-regulated anion channels in cultured endothelial cells by the anti-oestrogens clomiphene and nafoxidine
    • Maertens C., Droogmans G., Chakraborty P. and Nilius B. (2001) Inhibition of volume-regulated anion channels in cultured endothelial cells by the anti-oestrogens clomiphene and nafoxidine. Br. J. Pharmacol. 132: 135-142
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 135-142
    • Maertens, C.1    Droogmans, G.2    Chakraborty, P.3    Nilius, B.4
  • 133
    • 0027173514 scopus 로고
    • Time course of spontaneous calcium-activated chloride currents in smooth muscle cells from the rabbit portal vein
    • Hogg R. C., Wang Q. and Large W. A. (1993) Time course of spontaneous calcium-activated chloride currents in smooth muscle cells from the rabbit portal vein. J. Physiol. 464: 15-31
    • (1993) J. Physiol. , vol.464 , pp. 15-31
    • Hogg, R.C.1    Wang, Q.2    Large, W.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.