메뉴 건너뛰기




Volumn 45, Issue 22, 2006, Pages 6773-6782

Site-directed fluorescence studies of a prokaryotic ClC antiporter

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; FLUORESCENCE; MUTAGENESIS; PH EFFECTS; PHYSIOLOGY; PROTEINS;

EID: 33744950592     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0523815     Document Type: Article
Times cited : (34)

References (24)
  • 1
    • 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
  • 2
    • 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
  • 5
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., Campbell, E. B., and MacKinnon, R. (2003) Gating the selectivity filter in ClC chloride channels, Science 300, 108-112.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 6
    • 0345767047 scopus 로고    scopus 로고
    • A conserved pore-lining glutamate as a voltage- and chloride-dependent gate in the C1C-2 chloride channel
    • Niemeyer, M. I., Cid, L. P., Zuniga, L., Catalan, M., and Sepulveda, F. V. (2003) A conserved pore-lining glutamate as a voltage- and chloride-dependent gate in the C1C-2 chloride channel, J. Physiol. 553, 873-879.
    • (2003) J. Physiol. , vol.553 , pp. 873-879
    • Niemeyer, M.I.1    Cid, L.P.2    Zuniga, L.3    Catalan, M.4    Sepulveda, F.V.5
  • 8
    • 0345146920 scopus 로고    scopus 로고
    • Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1
    • Estevez, R., Schroeder, B. C., Accardi, A., Jentsch, T. J., and Pusch, M. (2003) Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1, Neuron 38, 47-59.
    • (2003) Neuron , vol.38 , pp. 47-59
    • Estevez, R.1    Schroeder, B.C.2    Accardi, A.3    Jentsch, T.J.4    Pusch, M.5
  • 9
    • 0141513678 scopus 로고    scopus 로고
    • Gating competence of constitutively open CLC-0 mutants revealed by the interaction with a small organic Inhibitor
    • Traverso, S., Elia, L., and Pusch, M. (2003) Gating competence of constitutively open CLC-0 mutants revealed by the interaction with a small organic Inhibitor, J. Gen. Physiol. 122, 295-306.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 295-306
    • Traverso, S.1    Elia, L.2    Pusch, M.3
  • 10
    • 0041899029 scopus 로고    scopus 로고
    • Conformational changes in the pore of CLC-0
    • Accardi, A., and Pusch, M. (2003) Conformational changes in the pore of CLC-0, J. Gen. Physiol. 122, 277-293.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 277-293
    • Accardi, A.1    Pusch, M.2
  • 13
    • 0028856707 scopus 로고
    • Fluorescent labeling of purified β2 adrenergic receptor. Evidence for ligand-specific conformational changes
    • Gether, U., Lin, S., and Kobilka, B. K. (1995) Fluorescent labeling of purified β2 adrenergic receptor. Evidence for ligand-specific conformational changes, J. Biol. Chem. 270, 28268-28275.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 14
    • 0030048243 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu, L. M., Moronne, M. M., and Isacoff, E. Y. (1996) Direct physical measure of conformational rearrangement underlying potassium channel gating, Science 271, 213-216.
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 15
    • 0030840167 scopus 로고    scopus 로고
    • + channel with fluorescence
    • + channel with fluorescence, Neuron 19, 1127-1140.
    • (1997) Neuron , vol.19 , pp. 1127-1140
    • Cha, A.1    Bezanilla, F.2
  • 17
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • Maduke, M., Pheasant, D. J., and Miller, C. (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
  • 18
    • 24144436098 scopus 로고    scopus 로고
    • Side-dependent inhibition of a prokaryotic ClC by DIDS
    • Matulef, K., and Maduke, M. (2005) Side-dependent inhibition of a prokaryotic ClC by DIDS, Biophys. J.
    • (2005) Biophys. J.
    • Matulef, K.1    Maduke, M.2
  • 19
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • Iyer, R., Iverson, T. M., Accardi, A., and Miller, C. (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
  • 20
    • 30444442312 scopus 로고    scopus 로고
    • Ion-binding properties of the ClC chloride selectivity filter
    • Lobet, S., and Dutzler, R. (2006) Ion-binding properties of the ClC chloride selectivity filter, EMBO J. 25, 24-33.
    • (2006) EMBO J. , vol.25 , pp. 24-33
    • Lobet, S.1    Dutzler, R.2
  • 22
    • 0034787375 scopus 로고    scopus 로고
    • Use of fluorescence spectroscopy to study conformational changes in the β2-adrenoceptor
    • Kobilka, B. K., and Gether, U. (2002) Use of fluorescence spectroscopy to study conformational changes in the β2-adrenoceptor, Methods Enzymol. 343, 170-182.
    • (2002) Methods Enzymol. , vol.343 , pp. 170-182
    • Kobilka, B.K.1    Gether, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.