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Volumn 126, Issue 5, 2005, Pages 529-538

Coupled K+-water flux through the HERG potassium channel measured by an osmotic pulse method

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL HERG; POTASSIUM ION; WATER;

EID: 27644494242     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200509377     Document Type: Article
Times cited : (41)

References (26)
  • 1
    • 0024535265 scopus 로고
    • + channels from skeletal and smooth muscle. Coupling of ion and water fluxes
    • + channels from skeletal and smooth muscle. Coupling of ion and water fluxes. Biophys. J. 55:367-371.
    • (1989) Biophys. J. , vol.55 , pp. 367-371
    • Alcayaga, C.1    Cecchi, X.2    Alvarez, O.3    Latorre, R.4
  • 3
    • 0032708637 scopus 로고    scopus 로고
    • Permeation of ions across the potassium channel: Brownian dynamics studies
    • Chung, S.H., T.W. Allen, M. Hoyles, and S. Kuyucak. 1999. Permeation of ions across the potassium channel: Brownian dynamics studies. Biophys. J. 77:2517-2533.
    • (1999) Biophys. J. , vol.77 , pp. 2517-2533
    • Chung, S.H.1    Allen, T.W.2    Hoyles, M.3    Kuyucak, S.4
  • 4
    • 0024511429 scopus 로고
    • Open channel structure and ion binding sites of the nicotinic acetylcholine receptor channel
    • Dani, J.A. 1989. Open channel structure and ion binding sites of the nicotinic acetylcholine receptor channel. J. Neurosci. 9:884-892.
    • (1989) J. Neurosci. , vol.9 , pp. 884-892
    • Dani, J.A.1
  • 5
    • 0019795013 scopus 로고
    • The gramicidin a channel: A review of its permeability characteristics with special reference to the single-file aspect of transport
    • Finkelstein, A., and O.S. Andersen. 1981. The gramicidin A channel: a review of its permeability characteristics with special reference to the single-file aspect of transport. J. Membr. Biol. 59:155-171.
    • (1981) J. Membr. Biol. , vol.59 , pp. 155-171
    • Finkelstein, A.1    Andersen, O.S.2
  • 10
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon. 2002. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 14
    • 0001244822 scopus 로고
    • Kinetics of movement in narrow channels
    • Levitt, D.G. 1984. Kinetics of movement in narrow channels. Curr. Top. Membr. Transp. 21:181-197.
    • (1984) Curr. Top. Membr. Transp. , vol.21 , pp. 181-197
    • Levitt, D.G.1
  • 15
    • 0018072320 scopus 로고
    • Number of water molecules coupled to the transport of sodium, potassium and hydrogen ions via gramicidin, nonactin or valinomycin
    • Levitt, D.G., S.R. Elias, and J.M. Hautman. 1978. Number of water molecules coupled to the transport of sodium, potassium and hydrogen ions via gramicidin, nonactin or valinomycin. Biochim. Biophys. Acta. 512:436-451.
    • (1978) Biochim. Biophys. Acta. , vol.512 , pp. 436-451
    • Levitt, D.G.1    Elias, S.R.2    Hautman, J.M.3
  • 17
    • 0035855251 scopus 로고    scopus 로고
    • + selectivity of the KcsA potassium channel from microscopic free energy perturbation calculations
    • + selectivity of the KcsA potassium channel from microscopic free energy perturbation calculations. Biochim. Biophys. Acta. 1548:194-202.
    • (2001) Biochim. Biophys. Acta. , vol.1548 , pp. 194-202
    • Luzhkov, V.B.1    Aqvist, J.2
  • 18
    • 0020148876 scopus 로고
    • +-selective channel of sarcoplasmic reticulum
    • +-selective channel of sarcoplasmic reticulum. Biophys. J. 38:227-230.
    • (1982) Biophys. J. , vol.38 , pp. 227-230
    • Miller, C.1
  • 20
    • 0017845979 scopus 로고
    • Water permeability of gramicidin A-treated lipid bilayer membranes
    • Rosenberg, P.A., and A. Finkelstein. 1978. Water permeability of gramicidin A-treated lipid bilayer membranes. J. Gen. Physiol. 72:327-340.
    • (1978) J. Gen. Physiol. , vol.72 , pp. 327-340
    • Rosenberg, P.A.1    Finkelstein, A.2
  • 21
    • 0242432457 scopus 로고    scopus 로고
    • Interaction between tetraethylammonium and permeant cations at the inactivation gate of the HERG potassium channel
    • Shimizu, H., C. Toyoshima, and S. Oiki. 2003. Interaction between tetraethylammonium and permeant cations at the inactivation gate of the HERG potassium channel. Jpn. J. Physiol. 53:25-34.
    • (2003) Jpn. J. Physiol. , vol.53 , pp. 25-34
    • Shimizu, H.1    Toyoshima, C.2    Oiki, S.3
  • 22
    • 0031806428 scopus 로고    scopus 로고
    • Streaming potentials in gramicidin channels measured with ion-selective microelectrodes
    • Tripathi, S., and S.B. Hladky. 1998. Streaming potentials in gramicidin channels measured with ion-selective microelectrodes. Biophys. J. 74:2912-2917.
    • (1998) Biophys. J. , vol.74 , pp. 2912-2917
    • Tripathi, S.1    Hladky, S.B.2
  • 23
    • 0029007356 scopus 로고
    • HERG, a human inward rectifier in the voltage-gated potassium channel family
    • Trudeau, M.C., J.W. Warmke, B. Ganetzky, and G.A. Robertson. 1995. HERG, a human inward rectifier in the voltage-gated potassium channel family. Science. 269:92-95.
    • (1995) Science , vol.269 , pp. 92-95
    • Trudeau, M.C.1    Warmke, J.W.2    Ganetzky, B.3    Robertson, G.A.4
  • 26
    • 0142185496 scopus 로고    scopus 로고
    • + selectivity filter: Charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates
    • + selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates. J. Mol. Biol. 333:965-975.
    • (2003) J. Mol. Biol. , vol.333 , pp. 965-975
    • Zhou, Y.1    MacKinnon, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.