메뉴 건너뛰기




Volumn 4, Issue 1, 2005, Pages 49-57

Unique structure and function of chloride transporting CLC proteins

Author keywords

Channelopathy; Gating; Ion channel; Permeation

Indexed keywords

BACTERIA; BINDING ENERGY; BIOLOGICAL MEMBRANES; CHLORIDE MINERALS; CRYSTAL STRUCTURE; DISEASES; ELECTRIC CONDUCTANCE; GENES; IONS; LIPIDS; PHYSIOLOGICAL MODELS; STRUCTURE (COMPOSITION);

EID: 15244340198     PISSN: 15361241     EISSN: None     Source Type: Journal    
DOI: 10.1109/TNB.2004.842503     Document Type: Article
Times cited : (17)

References (100)
  • 1
    • 0018814495 scopus 로고
    • A voltage-dependent chloride conductance channel from Torpedo electroplax membrane
    • C. Miller and M. M. White, "A voltage-dependent chloride conductance channel from Torpedo electroplax membrane," Ann. N. Y. Acad. Sci., vol. 341, pp. 534-551, 1980.
    • (1980) Ann. N. Y. Acad. Sci. , vol.341 , pp. 534-551
    • Miller, C.1    White, M.M.2
  • 2
    • 0020521341 scopus 로고
    • Single chloride channels from Torpedo electroplax. Activation by protons
    • W. Hanke and C. Miller, "Single chloride channels from Torpedo electroplax. Activation by protons," J. Gen. Physiol., vol. 82, pp. 25-45, 1983.
    • (1983) J. Gen. Physiol. , vol.82 , pp. 25-45
    • Hanke, W.1    Miller, C.2
  • 3
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • C. Miller and M. M. White, "Dimeric structure of single chloride channels from Torpedo electroplax," Proc. Nat. Acad. Sci. USA, vol. 81, pp. 2772-2775, 1984.
    • (1984) Proc. Nat. Acad. Sci. USA , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 4
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes
    • T. J. Jentsch, K. Steinmeyer, and G. Schwarz, "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes," Nature, vol. 348, pp. 510-514, 1990.
    • (1990) Nature , vol.348 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 5
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • T. J. Jentsch, V. Stein, F. Weinreich, and A. A. Zdebik, "Molecular structure and physiological function of chloride channels," Physiol. Rev., vol. 82, pp. 503-568, 2002.
    • (2002) Physiol. Rev. , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4
  • 6
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • R. Dutzler, E. B. Campbell, M. Cadene, B. T. Chait, and R. MacKinnon, "X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity," Nature, vol. 415, pp. 287-294, 2002.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 7
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • R. Dutzler, E. B. Campbell, and R. MacKinnon, "Gating the selectivity filter in ClC chloride channels," Science, vol. 300, pp. 108-112, 2003.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 9
    • 0026039594 scopus 로고
    • Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel
    • K. Steinmeyer, C. Ortland, and T. J. Jentsch, "Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel," Nature, vol. 354, pp. 301-304, 1991.
    • (1991) Nature , vol.354 , pp. 301-304
    • Steinmeyer, K.1    Ortland, C.2    Jentsch, T.J.3
  • 12
    • 0029559938 scopus 로고
    • Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel
    • M. Pusch, K. Steinmeyer, M. C. Koch, and T. J. Jentsch, "Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel," Neuron, vol. 15, pp. 1455-1463, 1995.
    • (1995) Neuron , vol.15 , pp. 1455-1463
    • Pusch, M.1    Steinmeyer, K.2    Koch, M.C.3    Jentsch, T.J.4
  • 13
    • 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
    • C. Saviane, F. Conti, and M. Pusch, "The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia," J. Gen. Physiol., vol. 113, pp. 457-468, 1999.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 457-468
    • Saviane, C.1    Conti, F.2    Pusch, M.3
  • 14
    • 0026522116 scopus 로고
    • A chloride channel widely expressed in epithelial and nonepithelial cells
    • A. Thiemann, S. Gründer, M. Pusch, and T. J. Jentsch, "A chloride channel widely expressed in epithelial and nonepithelial cells," Nature, vol. 356, pp. 57-60, 1992.
    • (1992) Nature , vol.356 , pp. 57-60
    • Thiemann, A.1    Gründer, S.2    Pusch, M.3    Jentsch, T.J.4
  • 15
    • 0035868910 scopus 로고    scopus 로고
    • Male germ cells and photoreceptors, both dependent on close cell-cell interactions, degenerate upon ClC-2 Cl(-) channel disruption
    • M. R. Bösl, V. Stein, C. Hübner, A. A. Zdebik, S. E. Jordt, A. K. Mukhopadhyay, M. S. Davidoff, A. F. Holstein, and T. J. Jentsch, "Male germ cells and photoreceptors, both dependent on close cell-cell interactions, degenerate upon ClC-2 Cl(-) channel disruption," EMBO J., vol. 20, pp. 1289-1299, 2001.
    • (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    Davidoff, M.S.7    Holstein, A.F.8    Jentsch, T.J.9
  • 18
    • 15244362421 scopus 로고    scopus 로고
    • Functional evaluation of human ClC-2 chloride channel mutations associated with idiopathic generalized epilepsies
    • M. I. Niemeyer, Y. R. Yusef, I. Cornejo, C. A. Flores, F. V. Sepúlveda, and L. P. Cid, "Functional evaluation of human ClC-2 chloride channel mutations associated with idiopathic generalized epilepsies," Physiol. Genomics, vol. 13, p. 13, 2004.
    • (2004) Physiol. Genomics , vol.13 , pp. 13
    • Niemeyer, M.I.1    Yusef, Y.R.2    Cornejo, I.3    Flores, C.A.4    Sepúlveda, F.V.5    Cid, L.P.6
  • 19
    • 0027460432 scopus 로고
    • Molecular cloning of a chloride channel that is regulated by dehydration and expressed predominantly in kidney medulla
    • S. Uchida, S. Sasaki, T. Furukawa, M. Hiraoka, T. Imai, Y. Hirata, and F. Marumo, "Molecular cloning of a chloride channel that is regulated by dehydration and expressed predominantly in kidney medulla," J. Biol. Chem., vol. 268, pp. 3821-3824, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3821-3824
    • Uchida, S.1    Sasaki, S.2    Furukawa, T.3    Hiraoka, M.4    Imai, T.5    Hirata, Y.6    Marumo, F.7
  • 20
    • 0028360729 scopus 로고
    • Two highly homologous members of the ClC chloride channel family in both rat and human kidney
    • S. Kieferle, P. Fong, M. Bens, A. Vandewalle, and T. J. Jentsch, "Two highly homologous members of the ClC chloride channel family in both rat and human kidney," Proc. Nat. Acad. Sci. USA, vol. 91, pp. 6943-6947, 1994.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 6943-6947
    • Kieferle, S.1    Fong, P.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 26
    • 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
    • W. Günther, A. Luchow, F. Cluzeaud, A. Vandewalle, and T. J. Jentsch, "ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells," Proc. Nat. Acad. Sci. USA, vol. 95, pp. 8075-8080, 1998.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 8075-8080
    • Günther, W.1    Luchow, A.2    Cluzeaud, F.3    Vandewalle, A.4    Jentsch, T.J.5
  • 28
    • 0037274891 scopus 로고    scopus 로고
    • The ClC-5 chloride channel knock-out mouse - An animal model for Dent's disease
    • Nov 29
    • W. Günther, N. Piwon, and T. J. Jentsch, "The ClC-5 chloride channel knock-out mouse - an animal model for Dent's disease," Pflügers Arch., vol. 445, pp. 456-462, Nov 29, 2003.
    • (2003) Pflügers Arch. , vol.445 , pp. 456-462
    • Günther, W.1    Piwon, N.2    Jentsch, T.J.3
  • 32
    • 0028032140 scopus 로고
    • Multimeric structure of ClC-1 chloride channel revealed by mutations in dominant myotonia congenita (Thomsen)
    • K. Steinmeyer, C. Lorenz, M. Pusch, M. C. Koch, and T. J. Jentsch, "Multimeric structure of ClC-1 chloride channel revealed by mutations in dominant myotonia congenita (Thomsen)," EMBO J., vol. 13, pp. 737-743, 1994.
    • (1994) EMBO J. , vol.13 , pp. 737-743
    • Steinmeyer, K.1    Lorenz, C.2    Pusch, M.3    Koch, M.C.4    Jentsch, T.J.5
  • 33
    • 0029743660 scopus 로고    scopus 로고
    • Two physically distinct pores in the dimeric ClC-0 chloride channel
    • U. Ludewig, M. Pusch, and T. J. Jentsch, "Two physically distinct pores in the dimeric ClC-0 chloride channel," Nature, vol. 383, pp. 340-343, 1996.
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 34
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a ClC-type chloride ion channel
    • R. E. Middleton, D. J. Pheasant, and C. Miller, "Homodimeric architecture of a ClC-type chloride ion channel," Nature, vol. 383, pp. 337-340, 1996.
    • (1996) Nature , vol.383 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 35
    • 0035951822 scopus 로고    scopus 로고
    • Pores formed by single subunits in mixed dimers of different CLC chloride channels
    • F. Weinreich and T. J. Jentsch, "Pores formed by single subunits in mixed dimers of different CLC chloride channels," J. Biol. Chem., vol. 276, pp. 2347-2353, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2347-2353
    • Weinreich, F.1    Jentsch, T.J.2
  • 37
    • 0029119568 scopus 로고
    • RASMOL: Biomolecular graphics for all
    • R. A. Sayle and E. J. Milner-White, "RASMOL: biomolecular graphics for all," Trends Biochem. Sci., vol. 20, pp. 374-376, 1995.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 374-376
    • Sayle, R.A.1    Milner-White, E.J.2
  • 38
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • C. Miller, "Open-state substructure of single chloride channels from Torpedo electroplax," Philos. Trans. R. Soc. London B, Biol. Sci., vol. 299, pp. 401-411, 1982.
    • (1982) Philos. Trans. R. Soc. London B, Biol. Sci. , vol.299 , pp. 401-411
    • Miller, C.1
  • 39
    • 0026332208 scopus 로고
    • Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA
    • C. K. Bauer, K. Steinmeyer, J. R. Schwarz, and T. J. Jentsch, "Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA," Proc. Nat. Acad. Sci. USA, vol. 88, pp. 11052-11056, 1991.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 11052-11056
    • Bauer, C.K.1    Steinmeyer, K.2    Schwarz, J.R.3    Jentsch, T.J.4
  • 40
    • 0028040145 scopus 로고
    • Low single channel conductance of the major skeletal muscle chloride channel, ClC-1
    • M. Pusch, K. Steinmeyer, and T. J. Jentsch, "Low single channel conductance of the major skeletal muscle chloride channel, ClC-1," Biophys. J., vol. 66, pp. 149-152, 1994.
    • (1994) Biophys. J. , vol.66 , pp. 149-152
    • Pusch, M.1    Steinmeyer, K.2    Jentsch, T.J.3
  • 41
    • 0031046341 scopus 로고    scopus 로고
    • Analysis of a protein region involved in permeation and gating of the voltage-gated Torpedo chloride channel ClC-0
    • U. Ludewig, T. J. Jentsch, and M. Pusch, "Analysis of a protein region involved in permeation and gating of the voltage-gated Torpedo chloride channel ClC-0," J. Physiol., vol. 498, pp. 691-702, 1997.
    • (1997) J. Physiol. , vol.498 , pp. 691-702
    • Ludewig, U.1    Jentsch, T.J.2    Pusch, M.3
  • 42
    • 0031750188 scopus 로고    scopus 로고
    • Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions
    • G. Y. Rychkov, M. Pusch, M. L. Roberts, T. J. Jentsch, and A. H. Bretag, "Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions," J. Gen. Physiol., vol. 111, pp. 653-665, 1998.
    • (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
  • 43
    • 0029609597 scopus 로고
    • Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease
    • K. Steinmeyer, B. Schwappach, M. Bens, A. Vandewalle, and T. J. Jentsch, "Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease," J. Biol. Chem., vol. 270, pp. 31 172-31 177, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31172-31177
    • Steinmeyer, K.1    Schwappach, B.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 44
    • 0033534733 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents
    • T. Friedrich, T. Breiderhoff, and T. J. Jentsch, "Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents," J. Biol. Chem., vol. 274, pp. 896-902, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 896-902
    • Friedrich, T.1    Breiderhoff, T.2    Jentsch, T.J.3
  • 45
    • 0034680866 scopus 로고    scopus 로고
    • Biophysical properties of ClC-3 differentiate it from swelling-activated chloride channels in Chinese hamster ovary-K1 cells
    • X. Li, K. Shimada, L. A. Showalter, and S. A. Weinman, "Biophysical properties of ClC-3 differentiate it from swelling-activated chloride channels in Chinese hamster ovary-K1 cells," J. Biol. Chem., vol. 275, pp. 35994-35998, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35994-35998
    • Li, X.1    Shimada, K.2    Showalter, L.A.3    Weinman, S.A.4
  • 47
    • 0036521873 scopus 로고    scopus 로고
    • Functional characterization of recombinant human ClC-4 chloride channels in cultured mammalian cells
    • C. G. Vanoye and A. L. George Jr., "Functional characterization of recombinant human ClC-4 chloride channels in cultured mammalian cells," J. Physiol., vol. 539, pp. 373-383, 2002.
    • (2002) J. Physiol. , vol.539 , pp. 373-383
    • Vanoye, C.G.1    George Jr., A.L.2
  • 49
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion
    • M. Pusch, U. Ludewig, A. Rehfeldt, and T. J. Jentsch, "Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion," Nature, vol. 373, pp. 527-531, 1995.
    • (1995) Nature , vol.373 , pp. 527-531
    • Pusch, M.1    Ludewig, U.2    Rehfeldt, A.3    Jentsch, T.J.4
  • 50
    • 0031015280 scopus 로고    scopus 로고
    • Temperature dependence of fast and slow gating relaxations of ClC-0 chloride channels
    • M. Pusch, U. Ludewig, and T. J. Jentsch, "Temperature dependence of fast and slow gating relaxations of ClC-0 chloride channels," J. Gen. Physiol., vol. 109, pp. 105-116, 1997.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 105-116
    • Pusch, M.1    Ludewig, U.2    Jentsch, T.J.3
  • 52
    • 0025270712 scopus 로고
    • Steady-state coupling of ion-channel conformations to a transmembrane ion gradient
    • E. A. Richard and C. Miller, "Steady-state coupling of ion-channel conformations to a transmembrane ion gradient," Science, vol. 247, pp. 1208-1210, 1990.
    • (1990) Science , vol.247 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 53
    • 0030877627 scopus 로고    scopus 로고
    • Inward rectification in ClC-0 chloride channels caused by mutations in several protein regions
    • U. Ludewig, T. J. Jentsch, and M. Pusch, "Inward rectification in ClC-0 chloride channels caused by mutations in several protein regions," J. Gen. Physiol., vol. 110, pp. 165-171, 1997.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 165-171
    • Ludewig, U.1    Jentsch, T.J.2    Pusch, M.3
  • 54
    • 0032477820 scopus 로고    scopus 로고
    • Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains
    • M. Maduke, C. Williams, and C. Miller, "Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains," Biochemistry, vol. 37, pp. 1315-1321, 1998.
    • (1998) Biochemistry , vol.37 , pp. 1315-1321
    • Maduke, M.1    Williams, C.2    Miller, C.3
  • 55
    • 0031967874 scopus 로고    scopus 로고
    • Determinants of slow gating in ClC-0, the voltage-gated chloride channel of Torpedo marmorata
    • P. Fong, A. Rehfeldt, and T. J. Jentsch, "Determinants of slow gating in ClC-0, the voltage-gated chloride channel of Torpedo marmorata," Amer. J. Physiol., vol. 274, pp. C966-C973, 1998.
    • (1998) Amer. J. Physiol. , vol.274
    • Fong, P.1    Rehfeldt, A.2    Jentsch, T.J.3
  • 56
    • 0033000370 scopus 로고    scopus 로고
    • Elimination of the slow gating of ClC-0 chloride channel by a point mutation
    • Y. W. Lin, C. W. Lin, and T. Y. Chen, "Elimination of the slow gating of ClC-0 chloride channel by a point mutation," J. Gen. Physiol., vol. 114, pp. 1-12, 1999.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 1-12
    • Lin, Y.W.1    Lin, C.W.2    Chen, T.Y.3
  • 57
    • 0035426049 scopus 로고    scopus 로고
    • Drastic reduction of the slow gate of human muscle chloride channel (ClC-1) by mutation C277S
    • A. Accardi, L. Ferrera, and M. Pusch, "Drastic reduction of the slow gate of human muscle chloride channel (ClC-1) by mutation C277S," J. Physiol., vol. 534, pp. 745-752, 2001.
    • (2001) J. Physiol. , vol.534 , pp. 745-752
    • Accardi, A.1    Ferrera, L.2    Pusch, M.3
  • 58
    • 0037327607 scopus 로고    scopus 로고
    • Involvement of helices at the dimer interface in ClC-1 common gating
    • M. Duffield, G. Rychkov, A. Bretag, and M. Roberts, "Involvement of helices at the dimer interface in ClC-1 common gating," J. Gen. Physiol., vol. 121, pp. 149-161, 2003.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 149-161
    • Duffield, M.1    Rychkov, G.2    Bretag, A.3    Roberts, M.4
  • 59
    • 0141513678 scopus 로고    scopus 로고
    • Gating competence of constitutively open CLC-0 mutants revealed by the interaction with a small organic inhibitor
    • S. Traverso, L. Elia, and M. Pusch, "Gating competence of constitutively open CLC-0 mutants revealed by the interaction with a small organic inhibitor," J. Gen. Physiol., vol. 122, pp. 295-306, 2003.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 295-306
    • Traverso, S.1    Elia, L.2    Pusch, M.3
  • 60
    • 3042648417 scopus 로고    scopus 로고
    • Functional and structural conservation of CBS domains from CLC channels
    • R. Estévez, M. Pusch, C. Ferrer-Costa, M. Orozco, and T. J. Jentsch, "Functional and structural conservation of CBS domains from CLC channels," J. Physiol., vol. 557, pp. 363-378, 2004.
    • (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
  • 62
    • 0033811517 scopus 로고    scopus 로고
    • Fast and slow gating relaxations in the muscle chloride channel CLC-1
    • A. Accardi and M. Pusch, "Fast and slow gating relaxations in the muscle chloride channel CLC-1," J. Gen. Physiol., vol. 116, pp. 433-444, 2000.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 433-444
    • Accardi, A.1    Pusch, M.2
  • 63
    • 0027051182 scopus 로고
    • Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume
    • S. Gründer, A. Thiemann, M. Pusch, and T. J. Jentsch, "Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume," Nature, vol. 360, pp. 759-762, 1992.
    • (1992) Nature , vol.360 , pp. 759-762
    • Gründer, S.1    Thiemann, A.2    Pusch, M.3    Jentsch, T.J.4
  • 64
    • 0030934771 scopus 로고    scopus 로고
    • Molecular dissection of gating in the ClC-2 chloride channel
    • S. E. Jordt and T. J. Jentsch, "Molecular dissection of gating in the ClC-2 chloride channel," EMBO J., vol. 16, pp. 1582-1592, 1997.
    • (1997) EMBO J. , vol.16 , pp. 1582-1592
    • Jordt, S.E.1    Jentsch, T.J.2
  • 65
    • 0033106355 scopus 로고    scopus 로고
    • Chloride dependence of hyperpolarization-activated chloride channel gates
    • M. Pusch, S. E. Jordt, V. Stein, and T. J. Jentsch, "Chloride dependence of hyperpolarization-activated chloride channel gates," J. Physiol., vol. 515, pp. 341-353, 1999.
    • (1999) J. Physiol. , vol.515 , pp. 341-353
    • Pusch, M.1    Jordt, S.E.2    Stein, V.3    Jentsch, T.J.4
  • 66
    • 0037095890 scopus 로고    scopus 로고
    • Conformation-dependent regulation of inward rectifier chloride channel gating by extracellular protons
    • J. Arreola, T. Begenisich, and J. E. Melvin, "Conformation-dependent regulation of inward rectifier chloride channel gating by extracellular protons," J. Physiol., vol. 541, pp. 103-112, 2002.
    • (2002) J. Physiol. , vol.541 , pp. 103-112
    • Arreola, J.1    Begenisich, T.2    Melvin, J.E.3
  • 67
    • 0345767047 scopus 로고    scopus 로고
    • A conserved pore-lining glutamate as a voltage- And chloride-dependent gate in the ClC-2 chloride channel
    • Nov 14
    • M. I. Niemeyer, L. P. Cid, L. Zúñiga, M. Catalán, and F. V. Sepúlveda, "A conserved pore-lining glutamate as a voltage-and chloride-dependent gate in the ClC-2 chloride channel," J. Physiol., vol. 553, pp. 873-879, Nov 14, 2003.
    • (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
  • 68
    • 1642524953 scopus 로고    scopus 로고
    • The voltage-dependent ClC-2 chloride channel has a dual gating mechanism
    • Jan 14
    • L. Zúñiga, M. I. Niemeyer, D. Varela, M. Catalan, L. P. Cid, and F. V. Sepúlveda, "The voltage-dependent ClC-2 chloride channel has a dual gating mechanism," J. Physiol., vol. 555, pp. 671-682, Jan 14, 2004.
    • (2004) J. Physiol. , vol.555 , pp. 671-682
    • Zúñiga, L.1    Niemeyer, M.I.2    Varela, D.3    Catalan, M.4    Cid, L.P.5    Sepúlveda, F.V.6
  • 69
    • 0028292022 scopus 로고
    • Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle's loop and collecting ducts of rat kidney
    • S. Adachi, S. Uchida, H. Ito, M. Hata, M. Hiroe, F. Marumo, and S. Sasaki, "Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle's loop and collecting ducts of rat kidney," J. Biol. Chem., vol. 269, pp. 17 677-17 683, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17677-17683
    • Adachi, S.1    Uchida, S.2    Ito, H.3    Hata, M.4    Hiroe, M.5    Marumo, F.6    Sasaki, S.7
  • 70
    • 0028832124 scopus 로고
    • Localization and functional characterization of rat kidney-specific chloride channel, ClC-K1
    • S. Uchida, S. Sasaki, K. Nitta, K. Uchida, S. Horita, H. Nihei, and F. Marumo, "Localization and functional characterization of rat kidney-specific chloride channel, ClC-K1," J. Clin. Invest., vol. 95, pp. 104-113, 1995.
    • (1995) J. Clin. Invest. , vol.95 , pp. 104-113
    • Uchida, S.1    Sasaki, S.2    Nitta, K.3    Uchida, K.4    Horita, S.5    Nihei, H.6    Marumo, F.7
  • 72
    • 0034637572 scopus 로고    scopus 로고
    • Functional and structural analysis of ClC-K chloride channels involved in renal disease
    • S. Waldegger and T. J. Jentsch, "Functional and structural analysis of ClC-K chloride channels involved in renal disease," J. Biol. Chem., vol. 275, pp. 24 527-24 533, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24527-24533
    • Waldegger, S.1    Jentsch, T.J.2
  • 73
    • 0035253009 scopus 로고    scopus 로고
    • Interaction of hydrophobic anions with the rat skeletal muscle chloride channel ClC-1: Effects on permeation and gating
    • G. Rychkov, M. Pusch, M. Roberts, and A. Bretag, "Interaction of hydrophobic anions with the rat skeletal muscle chloride channel ClC-1: effects on permeation and gating," J. Physiol., vol. 530, pp. 379-393, 2001.
    • (2001) J. Physiol. , vol.530 , pp. 379-393
    • Rychkov, G.1    Pusch, M.2    Roberts, M.3    Bretag, A.4
  • 74
    • 1142310688 scopus 로고    scopus 로고
    • Conduction mechanisms of chloride ions in ClC-type channels
    • B. Corry, M. O'Mara, and S. H. Chung, "Conduction mechanisms of chloride ions in ClC-type channels," Biophys. J., vol. 86, pp. 846-860, 2004.
    • (2004) Biophys. J. , vol.86 , pp. 846-860
    • Corry, B.1    O'Mara, M.2    Chung, S.H.3
  • 75
    • 1142310684 scopus 로고    scopus 로고
    • - pores: Electrostatic effects of charged residues
    • - pores: electrostatic effects of charged residues," Biophys. J., vol. 86, pp. 825-835, 2004.
    • (2004) Biophys. J. , vol.86 , pp. 825-835
    • Miloshevsky, G.V.1    Jordan, P.C.2
  • 76
    • 1142291714 scopus 로고    scopus 로고
    • Mechanism of anionic conduction across ClC
    • J. Cohen and K. Schulten, "Mechanism of anionic conduction across ClC," Biophys. J., vol. 86, pp. 836-845, 2004.
    • (2004) Biophys. J. , vol.86 , pp. 836-845
    • Cohen, J.1    Schulten, K.2
  • 77
    • 4444366193 scopus 로고    scopus 로고
    • Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel
    • D. L. Bostick and M. L. Berkowitz, "Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel," Biophys. J., vol. 87, pp. 1686-1696, 2004.
    • (2004) Biophys. J. , vol.87 , pp. 1686-1696
    • Bostick, D.L.1    Berkowitz, M.L.2
  • 78
    • 0041899029 scopus 로고    scopus 로고
    • Conformational changes in the pore of CLC-0
    • A. Accardi and M. Pusch, "Conformational changes in the pore of CLC-0," J. Gen. Physiol., vol. 122, pp. 277-293, 2003.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 277-293
    • Accardi, A.1    Pusch, M.2
  • 79
    • 0242415285 scopus 로고    scopus 로고
    • Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels
    • T. Y. Chen, M. F. Chen, and C. W. Lin, "Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels," J. Gen. Physiol., vol. 122, pp. 641-651, 2003.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 641-651
    • Chen, T.Y.1    Chen, M.F.2    Lin, C.W.3
  • 80
    • 0042377363 scopus 로고    scopus 로고
    • Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents
    • C. W. Lin and T. Y. Chen, "Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents," J. Gen. Physiol., vol. 122, pp. 147-159, 2003.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 147-159
    • Lin, C.W.1    Chen, T.Y.2
  • 81
    • 0034930508 scopus 로고    scopus 로고
    • Mechanism of block of single protopores of the Torpedo chloride channel ClC-0 by 2-(p-chlorophenoxy)butyric acid (CPB)
    • M. Pusch, A. Accardi, A. Liantonio, L. Ferrera, A. De Luca, D. C. Camerino, and F. Conti, "Mechanism of block of single protopores of the Torpedo chloride channel ClC-0 by 2-(p-chlorophenoxy)butyric acid (CPB)," J. Gen. Physiol., vol. 118, pp. 45-62, 2001.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 45-62
    • Pusch, M.1    Accardi, A.2    Liantonio, A.3    Ferrera, L.4    De Luca, A.5    Camerino, D.C.6    Conti, F.7
  • 82
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • M. Maduke, D. J. Pheasant, and C. Miller, "High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel," J. Gen. Physiol., vol. 114, pp. 713-722, 1999.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 83
    • 4344666270 scopus 로고    scopus 로고
    • Molecular determinants of differential pore blocking of kidney CLC-K chloride channels
    • May 28
    • A. Picollo, A. Liantonio, M. P. Didonna, L. Elia, D. C. Camerino, and M. Pusch, "Molecular determinants of differential pore blocking of kidney CLC-K chloride channels," EMBO Rep., vol. 5, pp. 584-589, May 28, 2004.
    • (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
  • 84
    • 0036086313 scopus 로고    scopus 로고
    • The ClC-3 chloride channel promotes acidification of lysosomes in CHO-K1 and Huh-7 cells
    • X. Li, T. Wang, Z. Zhao, and S. A. Weinman, "The ClC-3 chloride channel promotes acidification of lysosomes in CHO-K1 and Huh-7 cells," Amer. J. Physioi. Cell. Physiol., vol. 282, pp. C1483-C1491, 2002.
    • (2002) Amer. J. Physioi. Cell. Physiol. , vol.282
    • Li, X.1    Wang, T.2    Zhao, Z.3    Weinman, S.A.4
  • 85
    • 0842304663 scopus 로고    scopus 로고
    • Ionic currents mediated by a prokaryotic homologue of CLC Cl-channels
    • Jan 12
    • A. Accardi, L. Kolmakova-Partensky, C. Williams, and C. Miller, "Ionic currents mediated by a prokaryotic homologue of CLC Cl-channels," J Gen Physiol, vol. 123, pp. 109-119, Jan 12, 2004.
    • (2004) J Gen Physiol , vol.123 , pp. 109-119
    • Accardi, A.1    Kolmakova-Partensky, L.2    Williams, C.3    Miller, C.4
  • 86
    • 0842283896 scopus 로고    scopus 로고
    • Structural insights into chloride and proton-mediated gating of CLC chloride channels
    • M. Pusch, "Structural insights into chloride and proton-mediated gating of CLC chloride channels," Biochemistry, vol. 43, pp. 1135-1144, 2004.
    • (2004) Biochemistry , vol.43 , pp. 1135-1144
    • Pusch, M.1
  • 88
    • 0033851904 scopus 로고    scopus 로고
    • Pharmacological characterization of chloride channels belonging to the ClC family by the use of chiral clofibric acid derivatives
    • M. Pusch, A. Liantonio, L. Bertorello, A. Accardi, A. De Luca, S. Pierno, V. Tortorella, and D. C. Camerino, "Pharmacological characterization of chloride channels belonging to the ClC family by the use of chiral clofibric acid derivatives," Mol. Pharmacol., vol. 58, pp. 498-507, 2000.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 498-507
    • Pusch, M.1    Liantonio, A.2    Bertorello, L.3    Accardi, A.4    De Luca, A.5    Pierno, S.6    Tortorella, V.7    Camerino, D.C.8
  • 89
    • 0015170319 scopus 로고
    • Chloride conductance in normal and myotonic muscle fibers and the action of monocarboxylic aromatic acids
    • S. H. Bryant and A. Morales-Aguilera, "Chloride conductance in normal and myotonic muscle fibers and the action of monocarboxylic aromatic acids," J. Physiol., vol. 219, pp. 367-383, 1971.
    • (1971) J. Physiol. , vol.219 , pp. 367-383
    • Bryant, S.H.1    Morales-Aguilera, A.2
  • 92
    • 0345146920 scopus 로고    scopus 로고
    • Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1
    • R. Estévez, B. C. Schroeder, A. Accardi, T. J. Jentsch, and M. Pusch, "Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1," Neuron, vol. 38, pp. 47-59, 2003.
    • (2003) Neuron , vol.38 , pp. 47-59
    • Estévez, R.1    Schroeder, B.C.2    Accardi, A.3    Jentsch, T.J.4    Pusch, M.5
  • 94
    • 9144241252 scopus 로고    scopus 로고
    • Investigations of pharmacologic properties of the renal CLC-K1 chloride channel coexpressed with barttin by the use of 2-(p-Chlorophenoxy)propionic acid derivatives and other structurally unrelated chloride channels blockers
    • A. Liantonio, M. Pusch, A. Picollo, P. Guida, A. De Luca, S. Pierno, G. Fracchiolla, F. Loiodice, P. Tortorella, and D. C. Camerino, "Investigations of pharmacologic properties of the renal CLC-K1 chloride channel coexpressed with barttin by the use of 2-(p-Chlorophenoxy)propionic acid derivatives and other structurally unrelated chloride channels blockers," J. Amer. Soc. Nephrol., vol. 15, pp. 13-20, 2004.
    • (2004) J. Amer. Soc. Nephrol. , vol.15 , pp. 13-20
    • Liantonio, A.1    Pusch, M.2    Picollo, A.3    Guida, P.4    De Luca, A.5    Pierno, S.6    Fracchiolla, G.7    Loiodice, F.8    Tortorella, P.9    Camerino, D.C.10
  • 95
    • 0029162517 scopus 로고
    • An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels
    • C. Fahlke, R. Rüdel, N. Mitrovic, M. Zhou, and A. L. George jr, "An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels," Neuron, vol. 15, pp. 463-472, 1995.
    • (1995) Neuron , vol.15 , pp. 463-472
    • Fahlke, C.1    Rüdel, R.2    Mitrovic, N.3    Zhou, M.4    George Jr., A.L.5
  • 96
    • 0036667742 scopus 로고    scopus 로고
    • CLC chloride channels: Correlating structure with function
    • R. Estévez and T. J. Jentsch, "CLC chloride channels: correlating structure with function," Curr. Opin. Struct. Biol., vol. 12, pp. 531-539, 2002.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 531-539
    • Estévez, R.1    Jentsch, T.J.2
  • 97
    • 0030976029 scopus 로고    scopus 로고
    • CBS domains in CIC chloride channels implicated in myotonia and nephrolithiasis (kidney stones)
    • C. P. Ponting, "CBS domains in CIC chloride channels implicated in myotonia and nephrolithiasis (kidney stones)," J. Mol. Med., vol. 75, pp. 160-163, 1997.
    • (1997) J. Mol. Med. , vol.75 , pp. 160-163
    • Ponting, C.P.1
  • 98
    • 1842424664 scopus 로고    scopus 로고
    • The role of the carboxyl terminus in ClC chloride channel function
    • Jan 12
    • S. Hebeisen, A. Biela, B. Giese, G. Müller-Newen, P. Hidalgo, and C. Fahlke, "The role of the carboxyl terminus in ClC chloride channel function," J. Biol. Chem., vol. 279, pp. 13 140-13 147, Jan 12, 2004.
    • (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
  • 99
    • 8144222566 scopus 로고    scopus 로고
    • A two-holed story: Structural secrets about CLC proteins become unraveled?
    • E. Babini and M. Pusch, "A two-holed story: structural secrets about CLC proteins become unraveled?," Physiology, vol. 19, pp. 293-299, 2004.
    • (2004) Physiology , vol.19 , pp. 293-299
    • Babini, E.1    Pusch, M.2
  • 100
    • 85047691317 scopus 로고    scopus 로고
    • CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations
    • J. W. Scott, S. A. Hawley, K. A. Green, M. Anis, G. Stewart, G. A. Scullion, D. G. Norman, and D. G. Hardie, "CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations," J. Clin. Invest., vol. 113, pp. 274-284, 2004.
    • (2004) J. Clin. Invest. , vol.113 , pp. 274-284
    • Scott, J.W.1    Hawley, S.A.2    Green, K.A.3    Anis, M.4    Stewart, G.5    Scullion, G.A.6    Norman, D.G.7    Hardie, D.G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.