메뉴 건너뛰기




Volumn 129, Issue 4, 2007, Pages 317-329

Uncoupling and turnover in a Cl-/H+ exchange transporter

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE ION; LIPOSOME; PROTON; PROTON PUMP; TYROSINE;

EID: 33947720910     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200709756     Document Type: Article
Times cited : (118)

References (30)
  • 1
    • 0041899029 scopus 로고    scopus 로고
    • Conformational changes in the pore of CLC-0
    • Accardi, A., and M. Pusch. 2003. Conformational changes in the pore of CLC-0. J. Gen. Physiol. 122:277-294.
    • (2003) J. Gen. Physiol , vol.122 , pp. 277-294
    • Accardi, A.1    Pusch, M.2
  • 3
    • 33748798473 scopus 로고    scopus 로고
    • Synergism between halide binding and proton transport CLC-type exchanger
    • Accardi, A., S. Lobet, C. Williams, C. Miller, and R. Dutzler. 2006. Synergism between halide binding and proton transport CLC-type exchanger. J. Mol. Biol. 362:691-699.
    • (2006) J. Mol. Biol , vol.362 , pp. 691-699
    • Accardi, A.1    Lobet, S.2    Williams, C.3    Miller, C.4    Dutzler, R.5
  • 6
    • 14644423369 scopus 로고
    • Quantitative analysis of pump-mediated fluxes in reconstituted vesicles
    • Apell, H.J., and P. Läuger. 1986. Quantitative analysis of pump-mediated fluxes in reconstituted vesicles. Biochim. Biophys. Acta. 861:302-310.
    • (1986) Biochim. Biophys. Acta , vol.861 , pp. 302-310
    • Apell, H.J.1    Läuger, P.2
  • 7
    • 33751385225 scopus 로고
    • Fluorescence quenching kinetics in monodisperse micellar solution with exchange of probes and quenchers
    • Barzykin, A.V., and I.K. Lednev. 1993. Fluorescence quenching kinetics in monodisperse micellar solution with exchange of probes and quenchers. J. Physiol. Chem. 97:2774-2777.
    • (1993) J. Physiol. Chem , vol.97 , pp. 2774-2777
    • Barzykin, A.V.1    Lednev, I.K.2
  • 9
    • 0042377364 scopus 로고    scopus 로고
    • Side chain charge effects and conductance determinants in the pore of ClC-0 chloride channels
    • Chen, M.F., and T.Y. Chen. 2003. Side chain charge effects and conductance determinants in the pore of ClC-0 chloride channels. J. Gen. Physiol. 122:133-145.
    • (2003) J. Gen. Physiol , vol.122 , pp. 133-145
    • Chen, M.F.1    Chen, T.Y.2
  • 11
    • 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., E.B. Campbell, M. Cadene, B.T. Chait, and R. MacKinnon. 2002. X-ray structure of a ClC chloride channel at 3.0 A 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
  • 12
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., E.B. Campbell, and R. MacKinnon. 2003. Gating the selectivity filter in ClC chloride channels. Science. 300:108-112.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 13
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • Iyer, R., T.M. Iverson, A. Accardi, and C. Miller. 2002. A biological role for prokaryotic ClC chloride channels. Nature. 419:715-718.
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.M.2    Accardi, A.3    Miller, C.4
  • 16
    • 0037055984 scopus 로고    scopus 로고
    • The dual-function glutamate transporters: Structure and molecular characterization of the substrate-binding sites
    • Kanner, B.I., and L. Borre. 2002. The dual-function glutamate transporters: structure and molecular characterization of the substrate-binding sites. Biochim. Biophys. Acta. 1555:92-95.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 92-95
    • Kanner, B.I.1    Borre, L.2
  • 17
    • 4143072800 scopus 로고    scopus 로고
    • The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • Lemieux, M.J., Y. Huang, and D.N. Wang. 2004. The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Curr. Opin. Struct. Biol. 14:405-412.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 405-412
    • Lemieux, M.J.1    Huang, Y.2    Wang, D.N.3
  • 18
    • 30444442312 scopus 로고    scopus 로고
    • Ion binding properties of the CLC chloride selectivity filter
    • Lobet, S., and R. Dutzler. 2005. Ion binding properties of the CLC chloride selectivity filter. EMBO J. 25:24-33.
    • (2005) EMBO J , vol.25 , pp. 24-33
    • Lobet, S.1    Dutzler, R.2
  • 19
    • 0027364807 scopus 로고
    • Functional stoichiometry of Shaker potassium channel inactivation
    • MacKinnon, R., R.W. Aldrich, and A.W. Lee. 1993. Functional stoichiometry of Shaker potassium channel inactivation. Science. 262:757-759.
    • (1993) Science , vol.262 , pp. 757-759
    • MacKinnon, R.1    Aldrich, R.W.2    Lee, A.W.3
  • 20
    • 0033873930 scopus 로고    scopus 로고
    • A decade of ClC chloride channels: Structure, mechanism, and many unsettled questions
    • Maduke, M., C. Miller, and J.A. Mindell. 2000. A decade of ClC chloride channels: Structure, mechanism, and many unsettled questions. Annu. Rev. Biophys. Biomol. Struct. 29:411-438.
    • (2000) Annu. Rev. Biophys. Biomol. Struct , vol.29 , pp. 411-438
    • Maduke, M.1    Miller, C.2    Mindell, J.A.3
  • 21
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • Maduke, M., D.J. Pheasant, and C. Miller. 1999. High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel. J. Gen. Physiol. 114:713-722.
    • (1999) J. Gen. Physiol , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 22
    • 0028102941 scopus 로고
    • Purification, reconstitution, and subunit composition of a voltage-gated chloride channel from Torpedo electroplax
    • Middleton, R.E., D.J. Pheasant, and C. Miller. 1994. Purification, reconstitution, and subunit composition of a voltage-gated chloride channel from Torpedo electroplax. Biochemistry. 33:13189-13198.
    • (1994) Biochemistry , vol.33 , pp. 13189-13198
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 23
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens
    • Miller, C. 2006. ClC chloride channels viewed through a transporter lens. Nature. 440:484-489.
    • (2006) Nature , vol.440 , pp. 484-489
    • Miller, C.1
  • 24
    • 33748310543 scopus 로고    scopus 로고
    • + exchange transporter by polyatomic anions
    • + exchange transporter by polyatomic anions. J. Mol. Biol. 362:682-690.
    • (2006) J. Mol. Biol , vol.362 , pp. 682-690
    • Nguitragool, W.1    Miller, C.2
  • 25
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo, A., and M. Pusch. 2005. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature. 436:420-423.
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 26
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion
    • Pusch, M., U. Ludewig, A. Rehfeldt, and T.J. Jentsch. 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
  • 27
    • 0025270712 scopus 로고
    • Steady-state coupling of ion-channel conformations to a transmembrane ion gradient
    • Richard, E.A., and C. Miller. 1990. Steady-state coupling of ion-channel conformations to a transmembrane ion gradient. Science. 247:1208-1210.
    • (1990) Science , vol.247 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 28
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel, O., A.A. Zdebik, S. Lourdel, and T.J. Jentsch. 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
  • 30


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.