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Volumn 2, Issue 9, 2001, Pages 643-651

Cyclic nucleotide-gated channels: Shedding light on the opening of a channel pore

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLIC NUCLEOTIDE; ION CHANNEL;

EID: 0035461292     PISSN: 14710048     EISSN: None     Source Type: Journal    
DOI: 10.1038/35090015     Document Type: Review
Times cited : (69)

References (105)
  • 1
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., Marty, A., Neher, E. Sakmann, B. & Sigworth, F. J. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 391, 85-100 (1981).
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 2
    • 0017743723 scopus 로고
    • Inactivation of the sodium channel. II. Gating current experiments
    • Armstrong, C. M. & Bezanilla, F. Inactivation of the sodium channel. II. Gating current experiments. J. Gen. Physiol. 70, 567-590 (1977).
    • (1977) J. Gen. Physiol. , vol.70 , pp. 567-590
    • Armstrong, C.M.1    Bezanilla, F.2
  • 3
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., Zagotta, W. N. & Aldrich, R. W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250, 533-538 (1990).
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 4
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science 250, 568-571 (1990).
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 5
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou, M., Morais-Cabral, J. H., Mann, S. & MacKinnon, R. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors, Nature 411, 657-661 (2001).
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 7
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280, 69-77 (1998). This landmark paper presents the first crystal structure of a P-loop-containing channel, KcsA.
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 9
    • 0033823118 scopus 로고    scopus 로고
    • The barium site in a potassium channel by X-ray crystallography
    • Jiang, Y. & MacKinnon, R. The barium site in a potassium channel by X-ray crystallography. J. Gen. Physiol. 115, 269-272 (2000).
    • (2000) J. Gen. Physiol. , vol.115 , pp. 269-272
    • Jiang, Y.1    MacKinnon, R.2
  • 10
    • 0033516590 scopus 로고    scopus 로고
    • + channel: Electrostatic stabilization of monovalent cations
    • + channel: electrostatic stabilization of monovalent cations. Science 285, 100-102 (1999).
    • (1999) Science , vol.285 , pp. 100-102
    • Roux, B.1    MacKinnon, R.2
  • 11
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • Yellen, G. The moving parts of voltage-gated ion channels. O. Rev. Biophys. 31, 239-295 (1998).
    • (1998) O. Rev. Biophys. , vol.31 , pp. 239-295
    • Yellen, G.1
  • 12
    • 0021987760 scopus 로고
    • Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segment
    • Fesenko, E. E., Kolesnikov, S. S. & Lyubarsky, A. L. Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segment. Nature 313, 310-313 (1985). The first paper to describe a channel that is activated by the direct binding of cyclic nucleotides and to establish that cGMP is the second message involved in phototransduction.
    • (1985) Nature , vol.313 , pp. 310-313
    • Fesenko, E.E.1    Kolesnikov, S.S.2    Lyubarsky, A.L.3
  • 13
    • 0023111437 scopus 로고
    • A cyclic nucleotide-gated conductance in olfactory receptor cilia
    • Nakamura, T. & Gold, G. H. A cyclic nucleotide-gated conductance in olfactory receptor cilia. Nature 325, 442-444 (1987).
    • (1987) Nature , vol.325 , pp. 442-444
    • Nakamura, T.1    Gold, G.H.2
  • 14
    • 0029998701 scopus 로고    scopus 로고
    • Structure and function of cyclic nucleotide-gated channels
    • Zagotta, W. N. & Siegelbaum, S. A. Structure and function of cyclic nucleotide-gated channels. Annu. Rev. Neurosci. 19, 235-263 (1996).
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 235-263
    • Zagotta, W.N.1    Siegelbaum, S.A.2
  • 15
    • 0024805680 scopus 로고
    • Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel
    • Kaupp, U. B. et al. Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel. Nature 342, 762-766 (1989). A paper that presents the first cloning and functional expression of a CNG channel from bovine rod photoreceptors.
    • (1989) Nature , vol.342 , pp. 762-766
    • Kaupp, U.B.1
  • 16
    • 0025073835 scopus 로고
    • Primary structure and functional expression of a cyclic nucleotide-activated channel from olfactory neurons
    • Dhallan, R. S., Yau, K. W., Schrader, K. A. & Reed, R. R. Primary structure and functional expression of a cyclic nucleotide-activated channel from olfactory neurons. Nature 347, 184-187 (1990).
    • (1990) Nature , vol.347 , pp. 184-187
    • Dhallan, R.S.1    Yau, K.W.2    Schrader, K.A.3    Reed, R.R.4
  • 17
    • 0025127344 scopus 로고
    • Primary structure of cAMP-gated channel from bovine olfactory epithelium
    • Ludwig, J., Margalit, T., Eismam, E., Lancet, D. & Kaupp, U. B. Primary structure of cAMP-gated channel from bovine olfactory epithelium. FEBS Lett. 270, 24-29 (1990).
    • (1990) FEBS Lett. , vol.270 , pp. 24-29
    • Ludwig, J.1    Margalit, T.2    Eismam, E.3    Lancet, D.4    Kaupp, U.B.5
  • 18
    • 0026601214 scopus 로고
    • Molecular cloning and single-channel properties of the cyclic nucleotide-gated channel from catfish olfactory neurons
    • Goulding, E. H. et al. Molecular cloning and single-channel properties of the cyclic nucleotide-gated channel from catfish olfactory neurons. Neuron 8, 45-58 (1992).
    • (1992) Neuron , vol.8 , pp. 45-58
    • Goulding, E.H.1
  • 19
    • 0027193853 scopus 로고
    • Rod and cone photoreceptor cells express distinct genes for cGMP-gated channels
    • Bonigk, W. et al. Rod and cone photoreceptor cells express distinct genes for cGMP-gated channels. Neuron 10, 865-877 (1993).
    • (1993) Neuron , vol.10 , pp. 865-877
    • Bonigk, W.1
  • 20
    • 0027158799 scopus 로고
    • A new subunit of the cyclic nucleotide-gated cation channel in retinal rods
    • Chen, T. Y. et al. A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. Nature 362, 764-767 (1993).
    • (1993) Nature , vol.362 , pp. 764-767
    • Chen, T.Y.1
  • 21
    • 0028587719 scopus 로고
    • Heteromeric olfactory cyclic nucleotide-gated channels: A subunit that confers increased sensitivity to cAMP
    • Bradley, J., Li J., Davidson, N., Lester, H. A. & Zinn, K. Heteromeric olfactory cyclic nucleotide-gated channels: a subunit that confers increased sensitivity to cAMP. Proc. Natl Acad. Sci. USA 91, 8890-8894 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8890-8894
    • Bradley, J.1    Li, J.2    Davidson, N.3    Lester, H.A.4    Zinn, K.5
  • 22
    • 0028111939 scopus 로고
    • A second subunit of the olfactory cyclic nucleotide-gated channel confers high sensitivity to cAMP
    • Liman, E. R. & Buck, L. B. A second subunit of the olfactory cyclic nucleotide-gated channel confers high sensitivity to cAMP. Neuron 13, 611-621 (1994).
    • (1994) Neuron , vol.13 , pp. 611-621
    • Liman, E.R.1    Buck, L.B.2
  • 23
    • 0029160032 scopus 로고
    • A 240 kDa protein represents the complete β subunit of the cyclic nucleotide-gated channel from rod photoreceptor
    • Korschen, H. G. et al. A 240 kDa protein represents the complete β subunit of the cyclic nucleotide-gated channel from rod photoreceptor. Neuron 15, 627-636 (1995).
    • (1995) Neuron , vol.15 , pp. 627-636
    • Korschen, H.G.1
  • 24
    • 0034652101 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a new modulatory cyclic nucleotide-gated channel subunit from mouse retina
    • Gerstner, A., Zong, X., Hofmann, F. & Biel, M. Molecular cloning and functional characterization of a new modulatory cyclic nucleotide-gated channel subunit from mouse retina. J. Neurosci. 20, 1324-1332 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 1324-1332
    • Gerstner, A.1    Zong, X.2    Hofmann, F.3    Biel, M.4
  • 25
    • 0025694726 scopus 로고
    • Developmental and tissue-specific expression of the rod photoreceptor cGMP-gated ion channel gene
    • Ahmad, I., Redmond, L. J. & Barnstable, C. J. Developmental and tissue-specific expression of the rod photoreceptor cGMP-gated ion channel gene. Biochem. Biophys. Res. Commun. 173, 463-470 (1990).
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 463-470
    • Ahmad, I.1    Redmond, L.J.2    Barnstable, C.J.3
  • 26
    • 0025986567 scopus 로고
    • Cyclic GMP-activated channel activity in renal epithelial cells (A6)
    • Marunaka, Y., Ohara, A., Matsumoto, P. & Eaton, D. C. Cyclic GMP-activated channel activity in renal epithelial cells (A6). Biochim. Biophys. Acta 1070, 152-156 (1991).
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 152-156
    • Marunaka, Y.1    Ohara, A.2    Matsumoto, P.3    Eaton, D.C.4
  • 27
    • 0027183484 scopus 로고
    • Primary structure and functional expression of a cyclic nucleotide-gated channel from rabbit aorta
    • Biel, M. et al. Primary structure and functional expression of a cyclic nucleotide-gated channel from rabbit aorta. FEBS Lett. 329, 134-138 (1993).
    • (1993) FEBS Lett. , vol.329 , pp. 134-138
    • Biel, M.1
  • 28
    • 0028231752 scopus 로고
    • Another member of the cyclic nucleotide-gated channel family, expressed in testis, kidney, and heart
    • Biel, M. et al. Another member of the cyclic nucleotide-gated channel family, expressed in testis, kidney, and heart. Proc. Natl Acad. Sci. USA 91, 3505-3509 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3505-3509
    • Biel, M.1
  • 29
    • 0028072158 scopus 로고
    • Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells
    • Ostler, M., Biel, M., Flockerzi, V. & Hofmann, F. Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology 33, 1275-1282 (1994).
    • (1994) Neuropharmacology , vol.33 , pp. 1275-1282
    • Ostler, M.1    Biel, M.2    Flockerzi, V.3    Hofmann, F.4
  • 30
    • 0028230414 scopus 로고
    • Cloning and functional expression of a cyclic-nucteotide-gated channel from mammalian sperm
    • Weyand, I. et al. Cloning and functional expression of a cyclic-nucteotide-gated channel from mammalian sperm. Nature 368, 859-863 (1994).
    • (1994) Nature , vol.368 , pp. 859-863
    • Weyand, I.1
  • 31
    • 0029909559 scopus 로고    scopus 로고
    • Two alternatively spliced forms of the cGMP-gated channel α-subunit from cone photoreceptor are expressed in the chick pineal organ
    • Bonigk, W., Muller, F., Middendorff, R., Weyand, I. & Kaupp, U. B. Two alternatively spliced forms of the cGMP-gated channel α-subunit from cone photoreceptor are expressed in the chick pineal organ. J. Neurosci. 16, 7458-7468 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 7458-7468
    • Bonigk, W.1    Muller, F.2    Middendorff, R.3    Weyand, I.4    Kaupp, U.B.5
  • 32
    • 0030057048 scopus 로고    scopus 로고
    • Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating
    • Sun, Z. P., Akabas, M. H., Goulding, E H., Karlin, A. & Siegelbaum, S. A. Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating. Neuron 16, 141-149 (1996).
    • (1996) Neuron , vol.16 , pp. 141-149
    • Sun, Z.P.1    Akabas, M.H.2    Goulding, E.H.3    Karlin, A.4    Siegelbaum, S.A.5
  • 33
    • 0032888454 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated channels. Pore topology studied through the accessibility of reporter cysteines
    • Becchetti, A., Gamel, K. & Torre, V. Cyclic nucleotide-gated channels. Pore topology studied through the accessibility of reporter cysteines. J. Gen. Physiol. 114, 377-392 (1999).
    • (1999) J. Gen. Physiol. , vol.114 , pp. 377-392
    • Becchetti, A.1    Gamel, K.2    Torre, V.3
  • 34
    • 0033931448 scopus 로고    scopus 로고
    • 2+ of substituted cysteine residues within the P-bop
    • 2+ of substituted cysteine residues within the P-bop. Pflugers Arch. 440, 556-565 (2000). References 32-34 establish the accessibility of residues in the P region of CNG1.
    • (2000) Pflugers Arch. , vol.440 , pp. 556-565
    • Beochetti, A.1    Roncaglia, P.2
  • 35
    • 0034520641 scopus 로고    scopus 로고
    • Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels
    • Liu, J. & Siegelbaum, S. A. Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels. Neuron 28, 899-909 (2000). This paper presents evidence that the pore helix of CNG1 moves during gating, perhaps by rotating.
    • (2000) Neuron , vol.28 , pp. 899-909
    • Liu, J.1    Siegelbaum, S.A.2
  • 36
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels
    • Flynn, G. E. & Zagotta, W. N. Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron 30, 689-698 (2001). A paper presenting evidence that the S6 of CNG1 moves during gating, but that the smokehole is not the gate.
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 37
    • 0347864692 scopus 로고    scopus 로고
    • Rotational movement during cyclic nucleotide-gated channel opening
    • in the press
    • Johnson, J. P. Jr & Zagotta, W. N. Rotational movement during cyclic nucleotide-gated channel opening. Nature (in the press). This paper presents evidence that the post-TM segments of CNG1 form a helix bundle and rotate during gating.
    • Nature
    • Johnson Jr., J.P.1    Zagotta, W.N.2
  • 38
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in Shaker potassium channels?
    • Yang, Y., Yan, Y. & Sigworth, F. J. How does the W434F mutation block current in Shaker potassium channels? J. Gen. Physiol. 109, 779-789 (1997).
    • (1997) J. Gen. Physiol. , vol.109 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 40
    • 0027194224 scopus 로고
    • Role of H5 domain in determining pore diameter and ion permeation through cyclic nucleotide-gated channels
    • Goulding, E. H., Tibbs, G. R., Liu, D. & Siegelbaum, S. A. Role of H5 domain in determining pore diameter and ion permeation through cyclic nucleotide-gated channels. Nature 364, 61-64 (1993).
    • (1993) Nature , vol.364 , pp. 61-64
    • Goulding, E.H.1    Tibbs, G.R.2    Liu, D.3    Siegelbaum, S.A.4
  • 42
    • 0027424793 scopus 로고
    • Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel
    • Root, M. J. & MacKinnon, R. Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel. Neuron 11, 459-466 (1993).
    • (1993) Neuron , vol.11 , pp. 459-466
    • Root, M.J.1    MacKinnon, R.2
  • 44
    • 0028077663 scopus 로고
    • Two identical noninteracting sites in an ion channel revealed by proton transfer
    • Root, M. J. & MacKinnon, R. Two identical noninteracting sites in an ion channel revealed by proton transfer. Science 265, 1852-1856 (1994).
    • (1994) Science , vol.265 , pp. 1852-1856
    • Root, M.J.1    MacKinnon, R.2
  • 45
    • 0028799234 scopus 로고
    • Divalent cation selectivity in a cyclic nudeotide-gated ion channel
    • Park, C. S. & MacKinnon, R. Divalent cation selectivity in a cyclic nudeotide-gated ion channel. Biochemistry 34, 13328-13333 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13328-13333
    • Park, C.S.1    MacKinnon, R.2
  • 46
    • 0029156541 scopus 로고
    • The multi-ion nature of the cGMP-gated channel from vertebrate rods
    • Sesti, F., Eismann, E., Kaupp, U. B., Nizzari, M. & Torre, V. The multi-ion nature of the cGMP-gated channel from vertebrate rods. J. Physiol. (Lond.) 487, 17-36 (1995).
    • (1995) J. Physiol. (Lond.) , vol.487 , pp. 17-36
    • Sesti, F.1    Eismann, E.2    Kaupp, U.B.3    Nizzari, M.4    Torre, V.5
  • 47
    • 0033032511 scopus 로고    scopus 로고
    • Isolation of a single carboxyl-carboxylate proton binding site in the pore of a cyclic nucleotide-gated channel
    • Morrill, J. A. & MacKinnon, R. Isolation of a single carboxyl-carboxylate proton binding site in the pore of a cyclic nucleotide-gated channel. J. Gen. Physiol. 114, 71-83 (1999).
    • (1999) J. Gen. Physiol. , vol.114 , pp. 71-83
    • Morrill, J.A.1    MacKinnon, R.2
  • 48
    • 0033521589 scopus 로고    scopus 로고
    • 2+-binding site in the pore of cyclic nucleotide-gated channels: S5/S6 segments control affinity of intrapore glutamates
    • 2+-binding site in the pore of cyclic nucleotide-gated channels: S5/S6 segments control affinity of intrapore glutamates. EMBO J. 18, 119-130 (1999).
    • (1999) EMBO J. , vol.18 , pp. 119-130
    • Seifert, R.1    Eismann, E.2    Ludwig, J.3    Baumann, A.4    Kaupp, U.B.5
  • 50
    • 0028927313 scopus 로고
    • Conductance and kinetics of single cGMP-activated channels in salamander rod outer segments
    • Taylor, W. R. & Baylor, D. A Conductance and kinetics of single cGMP-activated channels in salamander rod outer segments. J. Physiol. (Lond.) 483, 567-582 (1995).
    • (1995) J. Physiol. (Lond.) , vol.483 , pp. 567-582
    • Taylor, W.R.1    Baylor, D.A.2
  • 51
    • 0030778914 scopus 로고    scopus 로고
    • Single cyclic nucleotide-gated channels locked in different ligand-bound states
    • Ruiz, M. L. & Karpen, J. W. Single cyclic nucleotide-gated channels locked in different ligand-bound states. Nature 389, 389-392 (1997).
    • (1997) Nature , vol.389 , pp. 389-392
    • Ruiz, M.L.1    Karpen, J.W.2
  • 52
    • 0032971038 scopus 로고    scopus 로고
    • Divalent cation selectivity is a function of gating in native and recombinant cyclic nucleotide-gated ion channels from retinal photoreceptors
    • Hackos, D. H. & Korenbrot, J.I. Divalent cation selectivity is a function of gating in native and recombinant cyclic nucleotide-gated ion channels from retinal photoreceptors. J. Gen. Physiol. 113, 799-818 (1999).
    • (1999) J. Gen. Physiol. , vol.113 , pp. 799-818
    • Hackos, D.H.1    Korenbrot, J.I.2
  • 53
    • 0023657697 scopus 로고
    • 2+ release from bovine rod outer segment disks
    • 2+ release from bovine rod outer segment disks. Biochemistry 26, 3249-3253 (1987).
    • (1987) Biochemistry , vol.26 , pp. 3249-3253
    • Schnetkamp, P.P.1
  • 54
    • 0025820873 scopus 로고
    • Single-channel study of the cGMP-dependent conductance of retinal rods from incorporation of native vesicles into planar lipid bilayers
    • Ildefonse, M. & Bennett, N. Single-channel study of the cGMP-dependent conductance of retinal rods from incorporation of native vesicles into planar lipid bilayers. J. Membr. Biol. 123, 133-147 (1991).
    • (1991) J. Membr. Biol. , vol.123 , pp. 133-147
    • Ildefonse, M.1    Bennett, N.2
  • 55
    • 0030665893 scopus 로고    scopus 로고
    • Tetracaine reports a conformattonal change in the pore of cyclic nudeotide-gated channels
    • Fodor, A. A. Black, K. D. & Zagotta, W. N. Tetracaine reports a conformattonal change in the pore of cyclic nudeotide-gated channels. J. Gen. Physiol. 110, 591-600 (1997).
    • (1997) J. Gen. Physiol. , vol.110 , pp. 591-600
    • Fodor, A.A.1    Black, K.D.2    Zagotta, W.N.3
  • 56
    • 0031031447 scopus 로고    scopus 로고
    • Mechanism of tetracaine block of cyclic nucleotide-gated channels
    • Fodor, A. A., Gordon, S. E. & Zagotta, W. N. Mechanism of tetracaine block of cyclic nucleotide-gated channels. J. Gen. Physiol. 109, 3-14 (1997).
    • (1997) J. Gen. Physiol. , vol.109 , pp. 3-14
    • Fodor, A.A.1    Gordon, S.E.2    Zagotta, W.N.3
  • 57
    • 0029994037 scopus 로고    scopus 로고
    • Time-dependent current decline in cyclic GMP-gated bovine channels caused by point mutations in the pore region expressed in Xenopus oocytes
    • Bucossi, G. et al. Time-dependent current decline in cyclic GMP-gated bovine channels caused by point mutations in the pore region expressed in Xenopus oocytes. J. Physiol. (Lond.) 493, 409-418 (1996).
    • (1996) J. Physiol. (Lond.) , vol.493 , pp. 409-418
    • Bucossi, G.1
  • 58
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons
    • Armstrong, C. M. Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons. J. Gen. Physiol. 58, 413-437 (1971).
    • (1971) J. Gen. Physiol. , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 59
    • 0017884049 scopus 로고
    • Immobilisation of gating charge by a substance that simulates inactivation
    • Yeh, J. Z. & Armstrong, C. M. Immobilisation of gating charge by a substance that simulates inactivation. Nature 273, 387-389 (1978).
    • (1978) Nature , vol.273 , pp. 387-389
    • Yeh, J.Z.1    Armstrong, C.M.2
  • 60
    • 0026519665 scopus 로고
    • + channel correlate with occupancy of the pore
    • + channel correlate with occupancy of the pore. Biophys. J. 61, 639-648 (1992).
    • (1992) Biophys. J. , vol.61 , pp. 639-648
    • Demo, S.D.1    Yellen, G.2
  • 61
    • 0033516494 scopus 로고    scopus 로고
    • +-channel activation gating
    • +-channel activation gating. Science 285, 73-78 (1999). Electron paramagnetic resonance spectroscopy experiments indicate that the opening of KcsA involves a translation and rotation of the TM1 and TM2 segments.
    • (1999) Science , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 62
    • 0030818830 scopus 로고    scopus 로고
    • Selectivity changes during activation of mutant Shaker potassium channels
    • Zheng, J. & Skjworth, F. J. Selectivity changes during activation of mutant Shaker potassium channels. J. Gen. Physiol. 110, 101-117 (1997).
    • (1997) J. Gen. Physiol. , vol.110 , pp. 101-117
    • Zheng, J.1    Skjworth, F.J.2
  • 63
    • 0031022168 scopus 로고    scopus 로고
    • Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating
    • Chapman, M. L. VanDongen, H. M. & VanDongen, A. M. Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating. Biophys. J. 72, 708-719 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 708-719
    • Chapman, M.L.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 64
    • 0031718345 scopus 로고    scopus 로고
    • Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels
    • Zheng, J. & Sigworth, F. J. Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels. J. Gen. Physiol. 112, 457-474 (1998).
    • (1998) J. Gen. Physiol. , vol.112 , pp. 457-474
    • Zheng, J.1    Sigworth, F.J.2
  • 65
    • 0035119276 scopus 로고    scopus 로고
    • + channel with backbone mutations in the selectivity filter
    • + channel with backbone mutations in the selectivity filter. Nature Neurosci. 4, 239-246 (2001).
    • (2001) Nature Neurosci. , vol.4 , pp. 239-246
    • Lu, T.1
  • 67
    • 0033103166 scopus 로고    scopus 로고
    • + channel inner pore revealed by stoichiometric covalent modification
    • + channel inner pore revealed by stoichiometric covalent modification. Neuron 22, 571-680 (1999).
    • (1999) Neuron , vol.22 , pp. 571-680
    • Lu, T.1    Nguyen, B.2    Zhang, X.S.3    Yang, J.4
  • 68
    • 0034744617 scopus 로고    scopus 로고
    • Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels
    • Sadja, R., Smadja, K., Alagem, N. & Reuveny, E. Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels. Neuron 29, 669-680 (2001).
    • (2001) Neuron , vol.29 , pp. 669-680
    • Sadja, R.1    Smadja, K.2    Alagem, N.3    Reuveny, E.4
  • 69
    • 0035049090 scopus 로고    scopus 로고
    • Yeast screen for constitutively active mutant G protein-activated potassium channels
    • Yi, B. A, Lin, Y. F., Jan, Y. N. & Jan, L Y. Yeast screen for constitutively active mutant G protein-activated potassium channels. Neuron 29, 657-667 (2001).
    • (2001) Neuron , vol.29 , pp. 657-667
    • Yi, B.A.1    Lin, Y.F.2    Jan, Y.N.3    Jan, L.Y.4
  • 70
    • 0029732848 scopus 로고    scopus 로고
    • Block of the cGMP-gated cation channel of catfish rod and cone photoreceptors by organic cations
    • Stotz, S. C. & Haynes, L. W. Block of the cGMP-gated cation channel of catfish rod and cone photoreceptors by organic cations. Biophys. J. 71, 3136-3147 (1996).
    • (1996) Biophys. J. , vol.71 , pp. 3136-3147
    • Stotz, S.C.1    Haynes, L.W.2
  • 71
    • 0028324195 scopus 로고
    • Potassium channel inactivation peptide blocks cyclic nucteotide-gated channels by binding to the conserved pore domain
    • Kramer, R. H., Goulding, E. & Siegelbaum, S. A. Potassium channel inactivation peptide blocks cyclic nucteotide-gated channels by binding to the conserved pore domain. Neuron 12, 655-662 (1994).
    • (1994) Neuron , vol.12 , pp. 655-662
    • Kramer, R.H.1    Goulding, E.2    Siegelbaum, S.A.3
  • 72
    • 0028951220 scopus 로고
    • Localization of regions affecting an allosteric transition in cyclic nucleotide-activated channels
    • Gordon, S. E. & Zagotta, W. N. Localization of regions affecting an allosteric transition in cyclic nucleotide-activated channels. Neuron 14, 857-864 (1995).
    • (1995) Neuron , vol.14 , pp. 857-864
    • Gordon, S.E.1    Zagotta, W.N.2
  • 73
    • 0028821215 scopus 로고
    • A histidine residue associated with the gate of the cyclic nucleotide-activated channels in rod photoreceptors
    • 2+-binding site to the post-TM segment.
    • (1995) Neuron , vol.14 , pp. 177-183
    • Gordon, S.E.1    Zagotta, W.N.2
  • 74
    • 0030053720 scopus 로고    scopus 로고
    • Direct activation of the olfactory cyclic nucleotide-gated channel through modification of sulfhydryl groups by NO compounds
    • Broillet, M. C. & Firestein, S. Direct activation of the olfactory cyclic nucleotide-gated channel through modification of sulfhydryl groups by NO compounds. Neuron 16, 377-385 (1996).
    • (1996) Neuron , vol.16 , pp. 377-385
    • Broillet, M.C.1    Firestein, S.2
  • 75
    • 0029886520 scopus 로고    scopus 로고
    • Altered ligand specifcity by protonation in the ligand binding domain of cyclic nudeotide-gated channels
    • Gordon, S. E., Oakley, J. C., Vamum, M. D. & Zagotta, W. N. Altered ligand specifcity by protonation in the ligand binding domain of cyclic nudeotide-gated channels. Biochemistry 35, 3994-4001 (1996).
    • (1996) Biochemistry , vol.35 , pp. 3994-4001
    • Gordon, S.E.1    Oakley, J.C.2    Vamum, M.D.3    Zagotta, W.N.4
  • 76
    • 0030822693 scopus 로고    scopus 로고
    • Direct interaction between amino- and carboxyl-terminal domains of cyclic nucleotide-gated channels
    • Gordon, S. E. Vamum, M. D. & Zagotta, W. N. Direct interaction between amino-and carboxyl-terminal domains of cyclic nucleotide-gated channels. Neuron 19, 431-441 (1997).
    • (1997) Neuron , vol.19 , pp. 431-441
    • Gordon, S.E.1    Vamum, M.D.2    Zagotta, W.N.3
  • 77
    • 0031849951 scopus 로고    scopus 로고
    • Movement of gating machinery during the activation of rod cyclic nucleotide-gated channels
    • Brown, R. L., Snow, S. D. & Haley, T. L Movement of gating machinery during the activation of rod cyclic nucleotide-gated channels. Biophys. J. 75, 825-833 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 825-833
    • Brown, R.L.1    Snow, S.D.2    Haley, T.L.3
  • 78
    • 0032518786 scopus 로고    scopus 로고
    • Three amino acids in the C-linker are major determinants of gating in cycle nucleotide-gated channels
    • Zong, X., Zucker, H., Hofmann, F. & Biel, M. Three amino acids in the C-linker are major determinants of gating in cycle nucleotide-gated channels. EMBO J. 17, 353-362 (1998).
    • (1998) EMBO J. , vol.17 , pp. 353-362
    • Zong, X.1    Zucker, H.2    Hofmann, F.3    Biel, M.4
  • 79
    • 0032944369 scopus 로고    scopus 로고
    • C-Linker of cyclic nudeotide-gated channels controls coupling of ligand binding to channel gating
    • Paoletti, P., Young, E. C. & Siegelbaum, S. A. C-Linker of cyclic nudeotide-gated channels controls coupling of ligand binding to channel gating. J. Gen. Physiol. 113, 17-34 (1999).
    • (1999) J. Gen. Physiol. , vol.113 , pp. 17-34
    • Paoletti, P.1    Young, E.C.2    Siegelbaum, S.A.3
  • 80
    • 0033635163 scopus 로고    scopus 로고
    • Gating rearrangements in cyclic nucteotide-gated channels revealed by patch-damp fluorometry
    • Zheng, J. & Zagotta, W. N. Gating rearrangements in cyclic nucteotide-gated channels revealed by patch-damp fluorometry. Neuron 28, 369-374 (2000).
    • (2000) Neuron , vol.28 , pp. 369-374
    • Zheng, J.1    Zagotta, W.N.2
  • 82
    • 0025334980 scopus 로고
    • Improvements in protein secondary structure prediction by an enhanced neural network
    • Kneller, D. G., Cohen, F. E. & Langridge, R. Improvements in protein secondary structure prediction by an enhanced neural network. J. Mol. Boil. 214, 171-182 (1990).
    • (1990) J. Mol. Boil. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 83
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D. M., Cuello, L G. & Perozo, E. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117, 165-180 (2001). Electron paramagnetic resonance spectroscopy experiments show that the post-TM region of KcsA forms a helical bundle.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 85
    • 0032545321 scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang, G., Spencer, R. H., Lee, A. T., Barclay, M.T. & Rees, D.C. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282, 2220-2226 (1993).
    • (1993) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 86
    • 0032127530 scopus 로고    scopus 로고
    • Constraining ligand binding site stoichiometry suggests that a cyclic-nucleotide-gated channel is composed of two functional dimers
    • Liu, D. T., Tibbs, G. R., Paoletti, P. & Siegelbaum, S. A. Constraining ligand binding site stoichiometry suggests that a cyclic-nucleotide-gated channel is composed of two functional dimers. Neuron 21, 235-248 (1998). A paper that presents intriguing results, indicating that CNG channels gate as if formed as a dimer-of-dimers.
    • (1998) Neuron , vol.21 , pp. 235-248
    • Liu, D.T.1    Tibbs, G.R.2    Paoletti, P.3    Siegelbaum, S.A.4
  • 87
    • 0033180345 scopus 로고    scopus 로고
    • Stoichiometry and arrangement of subunits in rod cyclic nudeotide-gated channels
    • Shammat, I. M. & Gordon, S. E. Stoichiometry and arrangement of subunits in rod cyclic nudeotide-gated channels. Neuron 23, 809-819 (1999).
    • (1999) Neuron , vol.23 , pp. 809-819
    • Shammat, I.M.1    Gordon, S.E.2
  • 88
    • 0035954373 scopus 로고    scopus 로고
    • A functioning chimera of the cyclic nucleotide-binding domain from the bovine retinal rod ion channel and the DMA-binding domain from catabolite gene-activating protein
    • Scott, S. P., Weber, I. T., Harrison, R. W., Carey, J. & Tanaka, J. C. A functioning chimera of the cyclic nucleotide-binding domain from the bovine retinal rod ion channel and the DMA-binding domain from catabolite gene-activating protein. Biochemistry 40, 7464-7473 (2001).
    • (2001) Biochemistry , vol.40 , pp. 7464-7473
    • Scott, S.P.1    Weber, I.T.2    Harrison, R.W.3    Carey, J.4    Tanaka, J.C.5
  • 90
    • 0026758461 scopus 로고
    • Gating of retinal rod cation channel by different nucfeotides: Comparative study of unitary currents
    • Ildefonse, M., Crouzy, S. & Bennett, N. Gating of retinal rod cation channel by different nucfeotides: comparative study of unitary currents. J. Membr. Biol. 130, 91-104 (1992).
    • (1992) J. Membr. Biol. , vol.130 , pp. 91-104
    • Ildefonse, M.1    Crouzy, S.2    Bennett, N.3
  • 91
    • 0027418442 scopus 로고
    • Interactions between divalent cations and the gating machinery of cyclic GMP-activated channels in salamander retinal rods
    • Karpen, J.W. Brown, R. L, Stryer, L & Baylor, D. A. Interactions between divalent cations and the gating machinery of cyclic GMP-activated channels in salamander retinal rods. J. Gen. Physiol. 101, 1-25 (1993).
    • (1993) J. Gen. Physiol. , vol.101 , pp. 1-25
    • Karpen, J.W.1    Brown, R.L.2    Stryer, L.3    Baylor, D.A.4
  • 92
    • 0034759492 scopus 로고    scopus 로고
    • Calculation of rigid body conformational changes using restraint-driven cartesian transformations
    • in the press
    • Sompornpisut, P., Liu, Y.-S. & Perozo, E. Calculation of rigid body conformational changes using restraint-driven cartesian transformations. Biophys. J. (in the press).
    • Biophys. J.
    • Sompornpisut, P.1    Liu, Y.-S.2    Perozo, E.3
  • 93
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution
    • Weber, I. T. & Steitz, T. A. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution. J. Mol. Biol. 198, 311-326 (1987). This paper presents the crystal structure of CAP, showing the CNBD bound to cAMP.
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 94
    • 0026569976 scopus 로고
    • Molecular code for cooperativity in hemoglobin
    • Ackers, G. K., Doyle, M. L., Myers, D. & Daugherty, M. A. Molecular code for cooperativity in hemoglobin. Science 255, 54-63 (1992).
    • (1992) Science , vol.255 , pp. 54-63
    • Ackers, G.K.1    Doyle, M.L.2    Myers, D.3    Daugherty, M.A.4
  • 95
    • 0025946606 scopus 로고
    • Control of ligand specificity in cyclic nucleotide-gated channels from rod photoreceptors and olfactory epithelium
    • Altenhofen, W. et al. Control of ligand specificity in cyclic nucleotide-gated channels from rod photoreceptors and olfactory epithelium. Proc. Natl Acad. Sci. USA 88, 9868-9872 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9868-9872
    • Altenhofen, W.1
  • 96
    • 0029114464 scopus 로고
    • Molecular mechanism for ligand discrimination of cyclic nucleotide-gated channels
    • Vamum, M. D., Black, K. D. & Zagotta, W. N. Molecular mechanism for ligand discrimination of cyclic nucleotide-gated channels. Neuron 15, 619-625 (1995). The authors propose a mechanism for cyclic nucleotide selectivity and conformational change in the CNBD of CNG channels.
    • (1995) Neuron , vol.15 , pp. 619-625
    • Vamum, M.D.1    Black, K.D.2    Zagotta, W.N.3
  • 97
    • 0029999355 scopus 로고    scopus 로고
    • Predicted ligand interactions of 3′,5prime;-cyclic nucleotide-gated channel binding sites: Comparison of retina and olfactory binding site models
    • Scott, S. P., Harrison, R. W., Weber, I. T. & Tanaka, J. C. Predicted ligand interactions of 3′,5prime;-cyclic nucleotide-gated channel binding sites: comparison of retina and olfactory binding site models. Protein Eng. 9, 333-344 (1996).
    • (1996) Protein Eng. , vol.9 , pp. 333-344
    • Scott, S.P.1    Harrison, R.W.2    Weber, I.T.3    Tanaka, J.C.4
  • 98
    • 0030959460 scopus 로고    scopus 로고
    • Allosteric activation and tuning of ligand efficacy in cyclic-nucleotide-gated channels
    • Tibbs, G. R., Goulding, E. H. & Siegelbaum, S. A. Allosteric activation and tuning of ligand efficacy in cyclic-nucleotide-gated channels. Nature 386, 612-615 (1997).
    • (1997) Nature , vol.386 , pp. 612-615
    • Tibbs, G.R.1    Goulding, E.H.2    Siegelbaum, S.A.3
  • 99
    • 0032497929 scopus 로고    scopus 로고
    • Three residues predicted by molecular modeling to interact with the purine moiety alter ligand binding and channel gating in cyclic nucleotide-gated channels
    • Scott, S. P. & Tanaka, J. C. Three residues predicted by molecular modeling to interact with the purine moiety alter ligand binding and channel gating in cyclic nucleotide-gated channels. Biochemistry 37, 17239-17252 (1998).
    • (1998) Biochemistry , vol.37 , pp. 17239-17252
    • Scott, S.P.1    Tanaka, J.C.2
  • 100
    • 0033213381 scopus 로고    scopus 로고
    • Molecular rearrangements in the ligand-binding domain of cyclic nudeotide-gated channels
    • Matulef, K., Flynn, G. E. & Zagotta, W. N. Molecular rearrangements in the ligand-binding domain of cyclic nudeotide-gated channels. Neuron 24, 443-452 (1999).
    • (1999) Neuron , vol.24 , pp. 443-452
    • Matulef, K.1    Flynn, G.E.2    Zagotta, W.N.3
  • 101
    • 0032954086 scopus 로고    scopus 로고
    • Sequence of events underlying the allosteric transition of rod cyclic nucleotide-gated channels
    • Sunderman, E. R. & Zagotta, W. N. Sequence of events underlying the allosteric transition of rod cyclic nucleotide-gated channels. J. Gen. Physiol. 113, 621-640 (1999).
    • (1999) J. Gen. Physiol. , vol.113 , pp. 621-640
    • Sunderman, E.R.1    Zagotta, W.N.2
  • 102
    • 0032962379 scopus 로고    scopus 로고
    • Mechanism of allosteric modulation of rod cyclic nucleotide-gated channels
    • Sunderman, E. R. & Zagotta, W. N. Mechanism of allosteric modulation of rod cyclic nucleotide-gated channels. J. Gen. Physiol. 113, 601-620 (1999).
    • (1999) J. Gen. Physiol. , vol.113 , pp. 601-620
    • Sunderman, E.R.1    Zagotta, W.N.2
  • 105
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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