메뉴 건너뛰기




Volumn 38, Issue 1, 2003, Pages 47-59

Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1

Author keywords

[No Author keywords available]

Indexed keywords

9 ANTHROIC ACID; BACTERIAL PROTEIN; CHLORIDE CHANNEL; CHLORIDE ION; SERINE;

EID: 0345146920     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00168-5     Document Type: Article
Times cited : (152)

References (54)
  • 2
    • 0030012897 scopus 로고    scopus 로고
    • Characteristics of skeletal muscle chloride channel ClC-1 and point mutant R304E expressed in Sf9 insect cells
    • Astill D.S., Rychkov G., Clarke J.D., Hughes B.P., Roberts M.L., Bretag A.H. Characteristics of skeletal muscle chloride channel ClC-1 and point mutant R304E expressed in Sf9 insect cells. Biochim. Biophys. Acta. 1280:1996;178-186.
    • (1996) Biochim. Biophys. Acta , vol.1280 , pp. 178-186
    • Astill, D.S.1    Rychkov, G.2    Clarke, J.D.3    Hughes, B.P.4    Roberts, M.L.5    Bretag, A.H.6
  • 3
    • 0026332208 scopus 로고
    • Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA
    • Bauer C.K., Steinmeyer K., Schwarz J.R., Jentsch T.J. Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA. Proc. Natl. Acad. Sci. USA. 88:1991;11052-11056.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11052-11056
    • Bauer, C.K.1    Steinmeyer, K.2    Schwarz, J.R.3    Jentsch, T.J.4
  • 6
    • 0015170319 scopus 로고
    • Chloride conductance in normal and myotonic muscle fibres and the action of monocarboxylic aromatic acids
    • Bryant S.H., Morales-Aguilera A. Chloride conductance in normal and myotonic muscle fibres and the action of monocarboxylic aromatic acids. J. Physiol. 219:1971;367-383.
    • (1971) J. Physiol. , vol.219 , pp. 367-383
    • Bryant, S.H.1    Morales-Aguilera, A.2
  • 7
    • 0032007691 scopus 로고    scopus 로고
    • Characterization of the hyperpolarization-activated chloride current in dissociated rat sympathetic neurons
    • Clark S., Jordt S.E., Jentsch T.J., Mathie A. Characterization of the hyperpolarization-activated chloride current in dissociated rat sympathetic neurons. J. Physiol. 506:1998;665-678.
    • (1998) J. Physiol. , vol.506 , pp. 665-678
    • Clark, S.1    Jordt, S.E.2    Jentsch, T.J.3    Mathie, A.4
  • 8
    • 0003932766 scopus 로고
    • New York: W.H. Freeman and Co.
    • Creighton, T.E. (1993). Proteins (New York: W.H. Freeman and Co.).
    • (1993) Proteins
    • Creighton, T.E.1
  • 9
    • 0026584787 scopus 로고
    • Opposite effects of enantiomers of clofibric acid derivative on rat skeletal muscle chloride conductance: Antagonism studies and theoretical modeling of two different receptor site interactions
    • De Luca A., Tricarico D., Wagner R., Bryant S.H., Tortorella V., Conte Camerino D. Opposite effects of enantiomers of clofibric acid derivative on rat skeletal muscle chloride conductance. antagonism studies and theoretical modeling of two different receptor site interactions J. Pharmacol. Exp. Ther. 260:1992;364-368.
    • (1992) J. Pharmacol. Exp. Ther. , vol.260 , pp. 364-368
    • De Luca, A.1    Tricarico, D.2    Wagner, R.3    Bryant, S.H.4    Tortorella, V.5    Conte Camerino, D.6
  • 10
    • 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., MacKinnon R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature. 415:2002;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
  • 11
    • 0036667742 scopus 로고    scopus 로고
    • CLC chloride channels: Correlating structure and function
    • Estévez R., Jentsch T.J. CLC chloride channels. correlating structure and function Curr. Opin. Struct. Biol. 12:2002;531-539.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 531-539
    • Estévez, R.1    Jentsch, T.J.2
  • 13
    • 0029162517 scopus 로고
    • An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels
    • Fahlke C., Rüdel R., Mitrovic N., Zhou M., George A.L. Jr. An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels. Neuron. 15:1995;463-472.
    • (1995) Neuron , vol.15 , pp. 463-472
    • Fahlke, C.1    Rüdel, R.2    Mitrovic, N.3    Zhou, M.4    George A.L., Jr.5
  • 15
    • 0031468569 scopus 로고    scopus 로고
    • Pore-forming segments in voltage-gated chloride channels
    • b
    • Fahlke C., Yu H.T., Beck C.L., Rhodes T.H., George A.L. Jr. Pore-forming segments in voltage-gated chloride channels. Nature. 390:1997;529-532. b.
    • (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., Jr.5
  • 16
    • 0033534733 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents
    • Friedrich T., Breiderhoff T., Jentsch T.J. Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents. J. Biol. Chem. 274:1999;896-902.
    • (1999) J. Biol. Chem. , vol.274 , pp. 896-902
    • Friedrich, T.1    Breiderhoff, T.2    Jentsch, T.J.3
  • 17
    • 0027136757 scopus 로고
    • The GEF1 gene of Saccharomyces cerevisiae encodes an integral membrane protein; Mutations in which have effects on respiration and iron-limited growth
    • Greene J.R., Brown N.H., DiDomenico B.J., Kaplan J., Eide D.J. The GEF1 gene of Saccharomyces cerevisiae encodes an integral membrane protein; mutations in which have effects on respiration and iron-limited growth. Mol. Gen. Genet. 241:1993;542-553.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 542-553
    • Greene, J.R.1    Brown, N.H.2    DiDomenico, B.J.3    Kaplan, J.4    Eide, D.J.5
  • 18
    • 0027051182 scopus 로고
    • Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume
    • Gründer S., Thiemann A., Pusch M., Jentsch T.J. Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume. Nature. 360:1992;759-762.
    • (1992) Nature , vol.360 , pp. 759-762
    • Gründer, S.1    Thiemann, A.2    Pusch, M.3    Jentsch, T.J.4
  • 19
    • 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
    • Günther W., Lüchow A., Cluzeaud F., Vandewalle A., Jentsch T.J. 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. 95:1998;8075-8080.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8075-8080
    • Günther, W.1    Lüchow, A.2    Cluzeaud, F.3    Vandewalle, A.4    Jentsch, T.J.5
  • 21
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes
    • Jentsch T.J., Steinmeyer K., Schwarz G. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature. 348:1990;510-514.
    • (1990) Nature , vol.348 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 22
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • Jentsch T.J., Stein V., Weinreich F., Zdebik A.A. Molecular structure and physiological function of chloride channels. Physiol. Rev. 82:2002;503-568.
    • (2002) Physiol. Rev. , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4
  • 24
    • 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., Jentsch T.J. Two highly homologous members of the ClC chloride channel family in both rat and human kidney. Proc. Natl. Acad. Sci. USA. 91:1994;6943-6947.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6943-6947
    • Kieferle, S.1    Fong, P.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 27
    • 0014421612 scopus 로고
    • Acute muscular syndrome associated with administration of clofibrate
    • Langer T., Levy R.I. Acute muscular syndrome associated with administration of clofibrate. N. Engl. J. Med. 279:1968;856-858.
    • (1968) N. Engl. J. Med. , vol.279 , pp. 856-858
    • Langer, T.1    Levy, R.I.2
  • 28
    • 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., Chen T.Y. Elimination of the slow gating of ClC-0 chloride channel by a point mutation. J. Gen. Physiol. 114:1999;1-12.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 1-12
    • Lin, Y.W.1    Lin, C.W.2    Chen, T.Y.3
  • 30
    • 0029843417 scopus 로고    scopus 로고
    • Heteromultimeric CLC chloride channels with novel properties
    • Lorenz C., Pusch M., Jentsch T.J. Heteromultimeric CLC chloride channels with novel properties. Proc. Natl. Acad. Sci. USA. 93:1996;13362-13366.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13362-13366
    • Lorenz, C.1    Pusch, M.2    Jentsch, T.J.3
  • 31
    • 0029743660 scopus 로고    scopus 로고
    • Two physically distinct pores in the dimeric ClC-0 chloride channel
    • Ludewig U., Pusch M., Jentsch T.J. Two physically distinct pores in the dimeric ClC-0 chloride channel. Nature. 383:1996;340-343.
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 32
    • 0030877627 scopus 로고    scopus 로고
    • Inward rectification in ClC-0 chloride channels caused by mutations in several protein regions
    • Ludewig U., Jentsch T.J., Pusch M. Inward rectification in ClC-0 chloride channels caused by mutations in several protein regions. J. Gen. Physiol. 110:1997;165-171.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 165-171
    • Ludewig, U.1    Jentsch, T.J.2    Pusch, M.3
  • 34
    • 0028820679 scopus 로고
    • Spectrum of mutations in the major human skeletal muscle chloride channel gene (CLCN1) leading to myotonia
    • Meyer-Kleine C., Steinmeyer K., Ricker K., Jentsch T.J., Koch M.C. Spectrum of mutations in the major human skeletal muscle chloride channel gene (CLCN1) leading to myotonia. Am. J. Hum. Genet. 57:1995;1325-1334.
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 1325-1334
    • Meyer-Kleine, C.1    Steinmeyer, K.2    Ricker, K.3    Jentsch, T.J.4    Koch, M.C.5
  • 35
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a ClC-type chloride ion channel
    • Middleton R.E., Pheasant D.J., Miller C. Homodimeric architecture of a ClC-type chloride ion channel. Nature. 383:1996;337-340.
    • (1996) Nature , vol.383 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 36
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • Miller C., White M.M. Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl. Acad. Sci. USA. 81:1984;2772-2775.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 38
    • 0017750206 scopus 로고
    • On the inhibition of muscle membrane chloride conductance by aromatic carboxylic acids
    • Palade P.T., Barchi R.L. On the inhibition of muscle membrane chloride conductance by aromatic carboxylic acids. J. Gen. Physiol. 69:1977;879-896.
    • (1977) J. Gen. Physiol. , vol.69 , pp. 879-896
    • Palade, P.T.1    Barchi, R.L.2
  • 39
    • 0028040145 scopus 로고
    • Low single channel conductance of the major skeletal muscle chloride channel, ClC-1
    • Pusch M., Steinmeyer K., Jentsch T.J. Low single channel conductance of the major skeletal muscle chloride channel, ClC-1. Biophys. J. 66:1994;149-152.
    • (1994) Biophys. J. , vol.66 , pp. 149-152
    • Pusch, M.1    Steinmeyer, K.2    Jentsch, T.J.3
  • 40
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion
    • a
    • Pusch M., Ludewig U., Rehfeldt A., Jentsch T.J. Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion. Nature. 373:1995;527-531. a.
    • (1995) Nature , vol.373 , pp. 527-531
    • Pusch, M.1    Ludewig, U.2    Rehfeldt, A.3    Jentsch, T.J.4
  • 41
    • 0029559938 scopus 로고
    • Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel
    • b
    • Pusch M., Steinmeyer K., Koch M.C., Jentsch T.J. Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel. Neuron. 15:1995;1455-1463. b.
    • (1995) Neuron , vol.15 , pp. 1455-1463
    • Pusch, M.1    Steinmeyer, K.2    Koch, M.C.3    Jentsch, T.J.4
  • 42
    • 0033106355 scopus 로고    scopus 로고
    • Chloride dependence of hyperpolarization-activated chloride channel gates
    • Pusch M., Jordt S.E., Stein V., Jentsch T.J. Chloride dependence of hyperpolarization-activated chloride channel gates. J. Physiol. 515:1999;341-353.
    • (1999) J. Physiol. , vol.515 , pp. 341-353
    • Pusch, M.1    Jordt, S.E.2    Stein, V.3    Jentsch, T.J.4
  • 43
    • 0033851904 scopus 로고    scopus 로고
    • Pharmacological characterization of chloride channels belonging to the ClC family by the use of chiral clofibric acid derivatives
    • Pusch M., Liantonio A., Bertorello L., Accardi A., De Luca A., Pierno S., Tortorella V., Camerino D.C. Pharmacological characterization of chloride channels belonging to the ClC family by the use of chiral clofibric acid derivatives. Mol. Pharmacol. 58:2000;498-507.
    • (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
  • 44
    • 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)
    • Pusch M., Accardi A., Liantonio A., Ferrera L., De Luca A., Camerino D.C., Conti F. Mechanism of block of single protopores of the Torpedo chloride channel ClC-0 by 2-(p-chlorophenoxy)butyric acid (CPB). J. Gen. Physiol. 118:2001;45-62.
    • (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
  • 45
    • 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., Bretag A.H. Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions. J. Gen. Physiol. 111:1998;653-665.
    • (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
  • 46
    • 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., Pusch M. The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia. J. Gen. Physiol. 113:1999;457-468.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 457-468
    • Saviane, C.1    Conti, F.2    Pusch, M.3
  • 48
    • 0026039594 scopus 로고
    • Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel
    • Steinmeyer K., Ortland C., Jentsch T.J. Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel. Nature. 354:1991;301-304.
    • (1991) Nature , vol.354 , pp. 301-304
    • Steinmeyer, K.1    Ortland, C.2    Jentsch, T.J.3
  • 49
    • 0029609597 scopus 로고
    • Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease
    • Steinmeyer K., Schwappach B., Bens M., Vandewalle A., Jentsch T.J. Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease. J. Biol. Chem. 270:1995;31172-31177.
    • (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
  • 51
    • 0037107377 scopus 로고    scopus 로고
    • Effect of an N-terminus deletion on voltage-dependent gating of the ClC- 2 chloride channel
    • Varela D., Niemeyer M.I., Cid L.P., Sepulveda F.V. Effect of an N-terminus deletion on voltage-dependent gating of the ClC- 2 chloride channel. J. Physiol. 544:2002;363-372.
    • (2002) J. Physiol. , vol.544 , pp. 363-372
    • Varela, D.1    Niemeyer, M.I.2    Cid, L.P.3    Sepulveda, F.V.4
  • 52
    • 0034637572 scopus 로고    scopus 로고
    • Functional and structural analysis of ClC-K chloride channels involved in renal disease
    • Waldegger S., Jentsch T.J. Functional and structural analysis of ClC-K chloride channels involved in renal disease. J. Biol. Chem. 275:2000;24527-24533.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24527-24533
    • Waldegger, S.1    Jentsch, T.J.2
  • 53
    • 0035951822 scopus 로고    scopus 로고
    • Pores formed by single subunits in mixed dimers of different CLC chloride channels
    • Weinreich F., Jentsch T.J. Pores formed by single subunits in mixed dimers of different CLC chloride channels. J. Biol. Chem. 276:2001;2347-2353.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2347-2353
    • Weinreich, F.1    Jentsch, T.J.2
  • 54
    • 0030914684 scopus 로고    scopus 로고
    • Identification of functionally important regions of the muscular chloride channel CIC-1 by analysis of recessive and dominant myotonic mutations
    • Wollnik B., Kubisch C., Steinmeyer K., Pusch M. Identification of functionally important regions of the muscular chloride channel CIC-1 by analysis of recessive and dominant myotonic mutations. Hum. Mol. Genet. 6:1997;805-811.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 805-811
    • Wollnik, B.1    Kubisch, C.2    Steinmeyer, K.3    Pusch, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.