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Volumn 14, Issue 4, 2004, Pages 440-446

Potassium channel structures: Do they conform?

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL; MEMBRANE PROTEIN; POTASSIUM CHANNEL; POTASSIUM ION; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 4143053760     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.06.008     Document Type: Review
Times cited : (27)

References (16)
  • 2
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Y. Jiang, A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon Crystal structure and mechanism of a calcium-gated potassium channel Nature 417 2002 515 522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait5    MacKinnon, R.B.T.6
  • 3
    • 0038076054 scopus 로고    scopus 로고
    • + channel
    • + channel with six putative transmembrane elements reveals an unexpected spatial relationship between the pore and voltage-sensing domains. A new 'paddle' model of voltage-dependent gating is proposed on the basis of the structure.
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Ruta, V.4    Cadene, M.5    Chait6    MacKinnon, R.B.T.7
  • 6
    • 0037158754 scopus 로고    scopus 로고
    • Multiple regulatory sites in large-conductance calcium-activated potassium channels
    • 2+ bowl and residues in the Rck domains.
    • (2002) Nature , vol.418 , pp. 880-884
    • Xia, X.M.1    Zeng2    Lingle, C.J.X.3
  • 8
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 ̊ resolution
    • M. Nishida, and R. MacKinnon Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 ̊ resolution Cell 111 2002 957 965
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida1    MacKinnon, R.M.2
  • 12
    • 0035949479 scopus 로고    scopus 로고
    • Controlling potassium channel activities: Interplay between the membrane and intracellular factors
    • B.A. Yi, D.L. Minor Jr., Y.F. Lin, Y.N. Jan, and L.Y. Jan Controlling potassium channel activities: interplay between the membrane and intracellular factors Proc Natl Acad Sci USA 98 2001 11016 11023
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11016-11023
    • Yi, B.A.1    Minor Jr., D.L.2    Lin, Y.F.3    Jan, Y.N.4    Jan, L.Y.5
  • 13
    • 0030054676 scopus 로고    scopus 로고
    • Functional characterization of Kv channel beta-subunits from rat brain
    • S.H. Heinemann, J. Rettig, H.R. Graack, and O. Pongs Functional characterization of Kv channel beta-subunits from rat brain J Physiol 493 1996 625 633
    • (1996) J Physiol , vol.493 , pp. 625-633
    • Heinemann, S.H.1    Rettig, J.2    Graack3    Pongs, O.H.R.4
  • 14
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • D.M. Starace, and F. Bezanilla A proton pore in a potassium channel voltage sensor reveals a focused electric field Nature 427 2004 548 553 This paper provides evidence to refute the 'paddle' model of voltage sensing. Key findings are that a relatively small movement of S4 is required to facilitate channel opening and that the transmembrane electric field is focused in a small region.
    • (2004) Nature , vol.427 , pp. 548-553
    • Starace1    Bezanilla, F.D.M.2
  • 15
    • 0033817708 scopus 로고    scopus 로고
    • Independence and cooperativity in rearrangements of a potassium channel voltage sensor revealed by single subunit fluorescence
    • L.M. Mannuzzu, and E.Y. Isacoff Independence and cooperativity in rearrangements of a potassium channel voltage sensor revealed by single subunit fluorescence J Gen Physiol 115 2000 257 268
    • (2000) J Gen Physiol , vol.115 , pp. 257-268
    • Mannuzzu1    Isacoff, E.Y.L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.